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psmd14 (Cusabio)

Name: psmd14
Brand: Cusabio
Rating: 94 (2 reviews)

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Cusabio psmd14

Expression levels of HSPA9, DKK1, <t>PSMD14,</t> and TRIM21 proteins in MM patients. Serum samples were collected from 46 MM patients and 52 healthy controls, and ELISA was performed to detect the levels of HSPA9 (a), DKK1 (b), TRIM21 (c), and PSMD14 (d) proteins. Data are expressed as mean ± SD from three independent experiments. DKK1, dickkopf Wnt signaling pathway inhibitor 1; HSPA9, heat shock protein family A member 9; MM, multiple myeloma; PSMD14, proteasome 26S subunit non-ATPase 14; TRIM21, tripartite motif containing 21.

Psmd14, supplied by Cusabio, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 2 article reviews

psmd14 - by Bioz Stars, 2026-02

94/100 stars

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1) Product Images from "Serum heat shock protein family A member 9 protein as a biomarker for bortezomib resistance and poor prognosis in patients with multiple myeloma"

Article Title: Serum heat shock protein family A member 9 protein as a biomarker for bortezomib resistance and poor prognosis in patients with multiple myeloma

Journal: Anti-Cancer Drugs

doi: 10.1097/CAD.0000000000001764

Expression levels of HSPA9, DKK1, PSMD14, and TRIM21 proteins in MM patients. Serum samples were collected from 46 MM patients and 52 healthy controls, and ELISA was performed to detect the levels of HSPA9 (a), DKK1 (b), TRIM21 (c), and PSMD14 (d) proteins. Data are expressed as mean ± SD from three independent experiments. DKK1, dickkopf Wnt signaling pathway inhibitor 1; HSPA9, heat shock protein family A member 9; MM, multiple myeloma; PSMD14, proteasome 26S subunit non-ATPase 14; TRIM21, tripartite motif containing 21.

Figure Legend Snippet: Expression levels of HSPA9, DKK1, PSMD14, and TRIM21 proteins in MM patients. Serum samples were collected from 46 MM patients and 52 healthy controls, and ELISA was performed to detect the levels of HSPA9 (a), DKK1 (b), TRIM21 (c), and PSMD14 (d) proteins. Data are expressed as mean ± SD from three independent experiments. DKK1, dickkopf Wnt signaling pathway inhibitor 1; HSPA9, heat shock protein family A member 9; MM, multiple myeloma; PSMD14, proteasome 26S subunit non-ATPase 14; TRIM21, tripartite motif containing 21.

Techniques Used: Expressing, Enzyme-linked Immunosorbent Assay

Image Search Results

(A) Co-localization of PSMD14 (green) and EB-P (red) in HL-60 cells confirmed by immunofluorescence staining (scale bar = 10 μm). (B) Pull-down assay using EB-P, followed by Western blotting, confirming that EB binds to PSMD14 in situ . (C and D) Cellular thermal shift assay (CETSA)-WB indicating the direct interaction between EB and PSMD14. (E, Left) Structural model of the predicted PSMD14–EB complex. The protein is shown as a gray cartoon, and EB is depicted in orange sticks. Residues forming the predicted binding pocket are highlighted. (E, Right) Detailed view of the predicted binding interface. The key residue His183 of PSMD14 is represented as sticks and is labeled. (F) Mapping of the EB binding site on recombinant human PSMD14 by liquid chromatography-tandem mass spectrometry (LC-MS/MS). (G) Western blot showing PSMD14 protein levels in HL-60 cells incubated with or without EB (15 μM). (H) In vitro activity assay showing that EB (100 μM or 200 μM) significantly inhibits PSMD14 enzymatic activity. (I) Both EB (15 μM) and CZM (40 μM, a known PSMD14 inhibitor) markedly inhibited HL-60 cell proliferation. (J) Cell viability was assessed by CCK-8 assay following PSMD14 knockdown. (K) HL-60 cells transfected with siPSMD14-2 or siNC were treated with different concentrations of EB, and cell viability was measured by CCK-8 assay. (L–O) Cell cycle distribution of HL-60 cells treated with CZM. (P–S) PSMD14 knockdown significantly altered cell cycle progression in HL-60 cells. ** P < 0.01, *** P < 0.001, ns = not significant.

Journal: RSC Chemical Biology

Article Title: Covalent targeting of PSMD14 by Eupalinolide B induces oncoprotein degradation and apoptosis in acute promyelocytic leukemia cells

doi: 10.1039/d5cb00197h

Figure Lengend Snippet: (A) Co-localization of PSMD14 (green) and EB-P (red) in HL-60 cells confirmed by immunofluorescence staining (scale bar = 10 μm). (B) Pull-down assay using EB-P, followed by Western blotting, confirming that EB binds to PSMD14 in situ . (C and D) Cellular thermal shift assay (CETSA)-WB indicating the direct interaction between EB and PSMD14. (E, Left) Structural model of the predicted PSMD14–EB complex. The protein is shown as a gray cartoon, and EB is depicted in orange sticks. Residues forming the predicted binding pocket are highlighted. (E, Right) Detailed view of the predicted binding interface. The key residue His183 of PSMD14 is represented as sticks and is labeled. (F) Mapping of the EB binding site on recombinant human PSMD14 by liquid chromatography-tandem mass spectrometry (LC-MS/MS). (G) Western blot showing PSMD14 protein levels in HL-60 cells incubated with or without EB (15 μM). (H) In vitro activity assay showing that EB (100 μM or 200 μM) significantly inhibits PSMD14 enzymatic activity. (I) Both EB (15 μM) and CZM (40 μM, a known PSMD14 inhibitor) markedly inhibited HL-60 cell proliferation. (J) Cell viability was assessed by CCK-8 assay following PSMD14 knockdown. (K) HL-60 cells transfected with siPSMD14-2 or siNC were treated with different concentrations of EB, and cell viability was measured by CCK-8 assay. (L–O) Cell cycle distribution of HL-60 cells treated with CZM. (P–S) PSMD14 knockdown significantly altered cell cycle progression in HL-60 cells. ** P < 0.01, *** P < 0.001, ns = not significant.

Article Snippet: To identify the direct binding site of EB on PSMD14, 40 μg of recombinant human PSMD14 protein (Signalchem Lifesciences) was incubated with 40 μM EB for 2 h at 37 °C.

Techniques: Immunofluorescence, Staining, Pull Down Assay, Western Blot, In Situ, Thermal Shift Assay, Binding Assay, Residue, Labeling, Recombinant, Liquid Chromatography, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Incubation, In Vitro, Activity Assay, CCK-8 Assay, Knockdown, Transfection

(A and B) WB analysis of AKT1 and CDK4 protein expression following PSMD14 knockdown in HL-60 cells. (C and D) WB analysis of PSMD14, AKT1, and CDK4 in HL-60 cells treated with the PSMD14 inhibitor CZM. (E and F) Expression of PSMD14, AKT1, and CDK4 after treatment with cycloheximide (CHX, 20 μM), analyzed by Western blot. (G and H) WB analysis of PSMD14, AKT1, and CDK4 in HL-60 cells transfected with siPSMD14-2 and subsequently treated with EB; siNC was used as the negative control. (I–K) Quantification of PSMD14 (I), AKT1 (J), and CDK4 (K) protein levels with or without EB treatment. * P < 0.05, ** P < 0.01, *** P < 0.001, ns = not significant. Identical letters indicate no statistically significant difference, while different letters indicate P < 0.05.

Journal: RSC Chemical Biology

Article Title: Covalent targeting of PSMD14 by Eupalinolide B induces oncoprotein degradation and apoptosis in acute promyelocytic leukemia cells

doi: 10.1039/d5cb00197h

Figure Lengend Snippet: (A and B) WB analysis of AKT1 and CDK4 protein expression following PSMD14 knockdown in HL-60 cells. (C and D) WB analysis of PSMD14, AKT1, and CDK4 in HL-60 cells treated with the PSMD14 inhibitor CZM. (E and F) Expression of PSMD14, AKT1, and CDK4 after treatment with cycloheximide (CHX, 20 μM), analyzed by Western blot. (G and H) WB analysis of PSMD14, AKT1, and CDK4 in HL-60 cells transfected with siPSMD14-2 and subsequently treated with EB; siNC was used as the negative control. (I–K) Quantification of PSMD14 (I), AKT1 (J), and CDK4 (K) protein levels with or without EB treatment. * P < 0.05, ** P < 0.01, *** P < 0.001, ns = not significant. Identical letters indicate no statistically significant difference, while different letters indicate P < 0.05.

Article Snippet: To identify the direct binding site of EB on PSMD14, 40 μg of recombinant human PSMD14 protein (Signalchem Lifesciences) was incubated with 40 μM EB for 2 h at 37 °C.

Techniques: Expressing, Knockdown, Western Blot, Transfection, Negative Control

PSMD14 acts as a major regulator for SLC7A11 stability in response to DEX stimulation. A) Schematic illustration of the preparation of SLC7A11‐binding protein sample in MLO‐Y4 cells for LC‐MS/MS analysis to identify the deubiquitinase. B) After proofreading using the UbiBrowser library, the SLC7A11‐bound deubiquitinases were ranked according to sequence coverage. C) LC‐MS/MS analysis of SLC7A11‐bound deubiquitinase eluted from MLO‐Y4 cell lysate. PSM: Peptide Spectrum Match. D) Immunoprecipitation of SLC7A11 or control IgG was performed on MLO‐Y4 cells treated with PBS or DEX (100 µM) for 8 h. E) Immunoprecipitation of PSMD14 or control IgG was performed on MLO‐Y4 cells. F) Immunoprecipitation of the interaction between SLC7A11 and PSMD14 was performed on plasmid‐transfected MLO‐Y4 cells with the indicated antibodies. After transfection was completed, MLO‐Y4 cells were treated with MG132 (10 µM) for 8 h while adding PBS or DEX (100 µM). G) Western blot and quantitative analysis of Flag‐PSMD14 and SLC7A11 protein was performed on MLO‐Y4 cells transfected with indictaed plasmid (n = 5 per group). H) Western blot and quantitative analysis of PSMD14 protein was performed on MLO‐Y4 cells transfected with si‐RNA (50 nM si‐NC or si‐PSMD14 #1‐3 for 24 h) (n = 5 per group). I) Western blot and quantitative analysis of PSMD14 and SLC7A11 proteins were performed on siRNA‐transfected MLO‐Y4 cells (50 nM si‐NC or si‐PSMD14 for 24 h). After transfection was completed, MLO‐Y4 cells were treated with PBS or DEX (100 µM) for 8 h (n = 5 per group). J) Immunoprecipitation of SLC7A11 ubiquitination and its binding to PSMD14 were performed on siRNA‐transfected MLO‐Y4 cells (50 nM si‐NC or si‐PSMD14 for 24 h). After transfection was completed, MLO‐Y4 were treated with MG132 (10 µM) for 8 h while adding PBS or DEX (100 µM). K) Predicted binding complex model of SLC7A11 and PSMD14 (left). The picture showed the hydrogen bonds in the protein interaction region and the corresponding amino acid residues (right). L) Binding energy analysis of the PSMD14‐SLC7A11 complex and the PSMD14‐SLC7A11‐DEX complex based on molecular dynamics simulations. Data are expressed as mean ± SD, with biologically individual data points shown. p values were determined by one‐way ANOVA test with Tukey's multiple comparisons (H) and two‐way ANOVA test with Tukey's multiple comparisons (G,I), * p < 0.05, ** p < 0.01.

Journal: Advanced Science

Article Title: PSMD14 Stabilizes SLC7A11 to Ameliorate Glucocorticoid‐Induced Osteoporosis by Suppressing Osteocyte Ferroptosis

doi: 10.1002/advs.202414902

Figure Lengend Snippet: PSMD14 acts as a major regulator for SLC7A11 stability in response to DEX stimulation. A) Schematic illustration of the preparation of SLC7A11‐binding protein sample in MLO‐Y4 cells for LC‐MS/MS analysis to identify the deubiquitinase. B) After proofreading using the UbiBrowser library, the SLC7A11‐bound deubiquitinases were ranked according to sequence coverage. C) LC‐MS/MS analysis of SLC7A11‐bound deubiquitinase eluted from MLO‐Y4 cell lysate. PSM: Peptide Spectrum Match. D) Immunoprecipitation of SLC7A11 or control IgG was performed on MLO‐Y4 cells treated with PBS or DEX (100 µM) for 8 h. E) Immunoprecipitation of PSMD14 or control IgG was performed on MLO‐Y4 cells. F) Immunoprecipitation of the interaction between SLC7A11 and PSMD14 was performed on plasmid‐transfected MLO‐Y4 cells with the indicated antibodies. After transfection was completed, MLO‐Y4 cells were treated with MG132 (10 µM) for 8 h while adding PBS or DEX (100 µM). G) Western blot and quantitative analysis of Flag‐PSMD14 and SLC7A11 protein was performed on MLO‐Y4 cells transfected with indictaed plasmid (n = 5 per group). H) Western blot and quantitative analysis of PSMD14 protein was performed on MLO‐Y4 cells transfected with si‐RNA (50 nM si‐NC or si‐PSMD14 #1‐3 for 24 h) (n = 5 per group). I) Western blot and quantitative analysis of PSMD14 and SLC7A11 proteins were performed on siRNA‐transfected MLO‐Y4 cells (50 nM si‐NC or si‐PSMD14 for 24 h). After transfection was completed, MLO‐Y4 cells were treated with PBS or DEX (100 µM) for 8 h (n = 5 per group). J) Immunoprecipitation of SLC7A11 ubiquitination and its binding to PSMD14 were performed on siRNA‐transfected MLO‐Y4 cells (50 nM si‐NC or si‐PSMD14 for 24 h). After transfection was completed, MLO‐Y4 were treated with MG132 (10 µM) for 8 h while adding PBS or DEX (100 µM). K) Predicted binding complex model of SLC7A11 and PSMD14 (left). The picture showed the hydrogen bonds in the protein interaction region and the corresponding amino acid residues (right). L) Binding energy analysis of the PSMD14‐SLC7A11 complex and the PSMD14‐SLC7A11‐DEX complex based on molecular dynamics simulations. Data are expressed as mean ± SD, with biologically individual data points shown. p values were determined by one‐way ANOVA test with Tukey's multiple comparisons (H) and two‐way ANOVA test with Tukey's multiple comparisons (G,I), * p < 0.05, ** p < 0.01.

Article Snippet: The recombinant mouse PSMD14 protein was synthesized by MedChemExpress.

Techniques: Binding Assay, Liquid Chromatography with Mass Spectroscopy, Sequencing, Immunoprecipitation, Control, Plasmid Preparation, Transfection, Western Blot, Ubiquitin Proteomics

PSMD14 maintains SLC7A11 expression by cleaving K48‐linked polyubiquitin chains from SLC7A11. A) Schematic diagram of the PSMD14‐SLC7A11 protein complex and the PSMD14 mutant plasmids (residues 1–233 and 234–310) used in subsequent immunoprecipitation assays. B) Immunoprecipitation of the interaction between SLC7A11 and each PSMD14 fragment was performed on plasmid‐transfected MLO‐Y4 cells. C) Immunoprecipitation of the interaction between SLC7A11 and PSMD14 (234‐310) fragment was performed on plasmid‐transfected MLO‐Y4 cells. After transfection was completed, MLO‐Y4 cells were treated with PBS or DEX (100 µM) for 8 h. D,E) Immunoprecipitation was performed to identify the type of polyubiquitination of SLC7A11 in MLO‐Y4 cell. MLO‐Y4 cells were cotransfected with Myc‐SLC7A11 plasmid, Flag‐PSMD14 plasmid and HA‐Ub K48/K63 or HA‐Ub K48R/K63R plasmid. After transfection was completed, MLO‐Y4 cells were treated with MG132 (10 µM) for 8 h. F) Immunoprecipitation of SLC7A11 ubiquitination and its binding to PSMD14 was HA‐Ub K48/K48R plasmid‐treated MLO‐Y4 cells. After transfection was completed, MLO‐Y4 cells were treated with MG132 (10 µM) and supplemented with DEX (100 µM) and/or THL (2 µM) for 8 h. G) Stable PSMD14 knockout MLO‐Y4 cells were constructed by CRISPR‐Cas9 strategy. H) Deubiquitination of SLC7A11 requires the intact PSMD14 fragment. PSMD14 knockout MLO‐Y4 cells treated with HA‐Ub K48 plasmid, Myc‐SLC7A11 plasmid, and PSMD14 full‐length or deletion mutant plasmids upon MG132 (10 µM) treatment for 8 h. I) Deubiquitination of SLC7A11 requires the intact PSMD14 fragment. Stable PSMD14 knockout MLO‐Y4 cells were treated with HA‐Ub K48 plasmid, Myc‐SLC7A11 plasmid, and Flag‐PSMD14 or PSMD14 mutants upon MG132 (10 µM) treatment for 8 h. The experiments were repeated three times independently with similar results.

Journal: Advanced Science

Article Title: PSMD14 Stabilizes SLC7A11 to Ameliorate Glucocorticoid‐Induced Osteoporosis by Suppressing Osteocyte Ferroptosis

doi: 10.1002/advs.202414902

Figure Lengend Snippet: PSMD14 maintains SLC7A11 expression by cleaving K48‐linked polyubiquitin chains from SLC7A11. A) Schematic diagram of the PSMD14‐SLC7A11 protein complex and the PSMD14 mutant plasmids (residues 1–233 and 234–310) used in subsequent immunoprecipitation assays. B) Immunoprecipitation of the interaction between SLC7A11 and each PSMD14 fragment was performed on plasmid‐transfected MLO‐Y4 cells. C) Immunoprecipitation of the interaction between SLC7A11 and PSMD14 (234‐310) fragment was performed on plasmid‐transfected MLO‐Y4 cells. After transfection was completed, MLO‐Y4 cells were treated with PBS or DEX (100 µM) for 8 h. D,E) Immunoprecipitation was performed to identify the type of polyubiquitination of SLC7A11 in MLO‐Y4 cell. MLO‐Y4 cells were cotransfected with Myc‐SLC7A11 plasmid, Flag‐PSMD14 plasmid and HA‐Ub K48/K63 or HA‐Ub K48R/K63R plasmid. After transfection was completed, MLO‐Y4 cells were treated with MG132 (10 µM) for 8 h. F) Immunoprecipitation of SLC7A11 ubiquitination and its binding to PSMD14 was HA‐Ub K48/K48R plasmid‐treated MLO‐Y4 cells. After transfection was completed, MLO‐Y4 cells were treated with MG132 (10 µM) and supplemented with DEX (100 µM) and/or THL (2 µM) for 8 h. G) Stable PSMD14 knockout MLO‐Y4 cells were constructed by CRISPR‐Cas9 strategy. H) Deubiquitination of SLC7A11 requires the intact PSMD14 fragment. PSMD14 knockout MLO‐Y4 cells treated with HA‐Ub K48 plasmid, Myc‐SLC7A11 plasmid, and PSMD14 full‐length or deletion mutant plasmids upon MG132 (10 µM) treatment for 8 h. I) Deubiquitination of SLC7A11 requires the intact PSMD14 fragment. Stable PSMD14 knockout MLO‐Y4 cells were treated with HA‐Ub K48 plasmid, Myc‐SLC7A11 plasmid, and Flag‐PSMD14 or PSMD14 mutants upon MG132 (10 µM) treatment for 8 h. The experiments were repeated three times independently with similar results.

Article Snippet: The recombinant mouse PSMD14 protein was synthesized by MedChemExpress.

Techniques: Expressing, Mutagenesis, Immunoprecipitation, Plasmid Preparation, Transfection, Ubiquitin Proteomics, Binding Assay, Knock-Out, Construct, CRISPR

Activation of PSMD14 with Pantethine suppresses osteocyte ferroptosis and bone loss. A) Schematic diagram of screening and identification of PSMD14 agonist. B) Docking scores of the top 20 candidates based on virtual screening. C) CCK‐8 assay was performed on MLO‐Y4 cells treated with different 20 candidates (10 µM) and DEX for 48 h (n = 5 per group). D) Chemical structures of five drug candidates (CA, TA, TB, PT and PC). E) Western blot and quantitative analysis of GPX4 protein were performed on MLO‐Y4 cells treated with DEX (100 µM) supplemented with or wihtout candidates (CA, TA, TB, PT or PC 10 µM) for 48 h. F) Cystine uptake assay was performed on MLO‐Y4 cells treated with DEX (100 µM) supplemented with or wihtout candidates (CA, TA, TB, PT or PC 10 µM) for 48 h (n = 9 per group). G) Immunoprecipitation of SLC7A11 ubiquitination and its binding to PSMD14 were performed on MG132 and DEX‐exposed MLO‐Y4 cells (MG132 10µM and DEX 100 µM). MG132 and DEX‐expousred MLO‐Y4 cells were treated with PT (10 µM) and/or THL (2 µM) for 8 h. H) Binding affinity of PT with recombinant PSMD14 was determined using an SPR assay (K D = 5.14 µM). I) Recombinant PSMD14 were incubated with PT, followed by the measurement of the absorbance at OD 445 nm to detect PSMD14 activity using Ubiquitin‐AMC assay (n = 5 per group). J) CCK‐8 assay was performed on DEX‐exposed MLO‐Y4 cells treated with PT (0–100 µM) and/or THL (2 µM) for 48 h (n = 5 per group). K–N) Western blot and quantitative analysis of GPX4 protein (K), MDA concentration detection (L), C11‐BODIPY 581/591 staining (M) and quantitative analysis (N) were performed on DEX‐exposed MLO‐Y4 cells treated with PT (100 µM) and/or THL (2 µM) for 48 h (n = 5 per group). O) Schematic showing the experimental protocol for 8‐weeks of PT / PT + THL injections in GIOP mice. P) Micro‐CT 3D restruction and H&E staining of the distal femur of mice in each group. The processing details of each group are shown in (O). Q) Distal femur BV/TV, Tb.Th, Tb.Sp, Tb.N, and BMD of mice in each group were measured by micro‐CT (n = 6 per group). Quantitative analysis of the empty lacunae in cortical bone (Number of empty lacunae with respect to bone area, N. Empt. Lc./B. Ar. per mm 2 ) based on H&E staining (n = 6 per group). R) GPX4, SLC7A11 and PSMD14 IHC staining of the distal femur of mice in each group. The processing details of each group are shown in (O). S) Quantification of GPX4, SLC7A11 and PSMD14‐positive osteocytes in mouse cortical femurs based on IHC staining (n = 6 per group). T) MDA content in tibia tissue of mice in each group (n = 6 per group). U) Maximum load and Maximum deflection of femoral cortical bone evaluated by the three‐point bending test (n = 6 per group). Data are expressed as mean ± SD, with biologically individual data points shown. p values were determined by one‐way ANOVA test with Tukey's multiple comparisons (C,E,F,H,I,L,N,Q,S–U) and two‐way ANOVA test with Tukey's multiple comparisons (J,K), ns, p > 0.05, * p < 0.05, ** p < 0.01.

Journal: Advanced Science

Article Title: PSMD14 Stabilizes SLC7A11 to Ameliorate Glucocorticoid‐Induced Osteoporosis by Suppressing Osteocyte Ferroptosis

doi: 10.1002/advs.202414902

Figure Lengend Snippet: Activation of PSMD14 with Pantethine suppresses osteocyte ferroptosis and bone loss. A) Schematic diagram of screening and identification of PSMD14 agonist. B) Docking scores of the top 20 candidates based on virtual screening. C) CCK‐8 assay was performed on MLO‐Y4 cells treated with different 20 candidates (10 µM) and DEX for 48 h (n = 5 per group). D) Chemical structures of five drug candidates (CA, TA, TB, PT and PC). E) Western blot and quantitative analysis of GPX4 protein were performed on MLO‐Y4 cells treated with DEX (100 µM) supplemented with or wihtout candidates (CA, TA, TB, PT or PC 10 µM) for 48 h. F) Cystine uptake assay was performed on MLO‐Y4 cells treated with DEX (100 µM) supplemented with or wihtout candidates (CA, TA, TB, PT or PC 10 µM) for 48 h (n = 9 per group). G) Immunoprecipitation of SLC7A11 ubiquitination and its binding to PSMD14 were performed on MG132 and DEX‐exposed MLO‐Y4 cells (MG132 10µM and DEX 100 µM). MG132 and DEX‐expousred MLO‐Y4 cells were treated with PT (10 µM) and/or THL (2 µM) for 8 h. H) Binding affinity of PT with recombinant PSMD14 was determined using an SPR assay (K D = 5.14 µM). I) Recombinant PSMD14 were incubated with PT, followed by the measurement of the absorbance at OD 445 nm to detect PSMD14 activity using Ubiquitin‐AMC assay (n = 5 per group). J) CCK‐8 assay was performed on DEX‐exposed MLO‐Y4 cells treated with PT (0–100 µM) and/or THL (2 µM) for 48 h (n = 5 per group). K–N) Western blot and quantitative analysis of GPX4 protein (K), MDA concentration detection (L), C11‐BODIPY 581/591 staining (M) and quantitative analysis (N) were performed on DEX‐exposed MLO‐Y4 cells treated with PT (100 µM) and/or THL (2 µM) for 48 h (n = 5 per group). O) Schematic showing the experimental protocol for 8‐weeks of PT / PT + THL injections in GIOP mice. P) Micro‐CT 3D restruction and H&E staining of the distal femur of mice in each group. The processing details of each group are shown in (O). Q) Distal femur BV/TV, Tb.Th, Tb.Sp, Tb.N, and BMD of mice in each group were measured by micro‐CT (n = 6 per group). Quantitative analysis of the empty lacunae in cortical bone (Number of empty lacunae with respect to bone area, N. Empt. Lc./B. Ar. per mm 2 ) based on H&E staining (n = 6 per group). R) GPX4, SLC7A11 and PSMD14 IHC staining of the distal femur of mice in each group. The processing details of each group are shown in (O). S) Quantification of GPX4, SLC7A11 and PSMD14‐positive osteocytes in mouse cortical femurs based on IHC staining (n = 6 per group). T) MDA content in tibia tissue of mice in each group (n = 6 per group). U) Maximum load and Maximum deflection of femoral cortical bone evaluated by the three‐point bending test (n = 6 per group). Data are expressed as mean ± SD, with biologically individual data points shown. p values were determined by one‐way ANOVA test with Tukey's multiple comparisons (C,E,F,H,I,L,N,Q,S–U) and two‐way ANOVA test with Tukey's multiple comparisons (J,K), ns, p > 0.05, * p < 0.05, ** p < 0.01.

Article Snippet: The recombinant mouse PSMD14 protein was synthesized by MedChemExpress.

Techniques: Activation Assay, CCK-8 Assay, Western Blot, Immunoprecipitation, Ubiquitin Proteomics, Binding Assay, Recombinant, SPR Assay, Incubation, Activity Assay, Ub-AMC Assay, Concentration Assay, Staining, Micro-CT, Immunohistochemistry

Schematic diagram illustrating the mechanism of GC‐mediated osteocyte ferroptosis. Top: Under physiological conditions, PSMD14 binds to and deubiquitinates SLC7A11 to stabilize SLC7A11 expression and the cystine uptake capacity of osteocytes, thereby ensuring the GSH content and GPX4 activity in osteocytes to maintain cellular function and vitality. Down: During DEX exposure, SLC7A11 is degraded due to limited binding with PSMD14, leading to insufficient cystine in osteocytes and triggering ferroptosis. Combined with virtual screening, we identified PT as a PSMD14 agonist that stabilizes SLC7A11 expression against DEX‐mediated ferroptosis.

Journal: Advanced Science

Article Title: PSMD14 Stabilizes SLC7A11 to Ameliorate Glucocorticoid‐Induced Osteoporosis by Suppressing Osteocyte Ferroptosis

doi: 10.1002/advs.202414902

Figure Lengend Snippet: Schematic diagram illustrating the mechanism of GC‐mediated osteocyte ferroptosis. Top: Under physiological conditions, PSMD14 binds to and deubiquitinates SLC7A11 to stabilize SLC7A11 expression and the cystine uptake capacity of osteocytes, thereby ensuring the GSH content and GPX4 activity in osteocytes to maintain cellular function and vitality. Down: During DEX exposure, SLC7A11 is degraded due to limited binding with PSMD14, leading to insufficient cystine in osteocytes and triggering ferroptosis. Combined with virtual screening, we identified PT as a PSMD14 agonist that stabilizes SLC7A11 expression against DEX‐mediated ferroptosis.

Article Snippet: The recombinant mouse PSMD14 protein was synthesized by MedChemExpress.

Techniques: Expressing, Activity Assay, Cell Function Assay, Binding Assay

Journal: RSC Chemical Biology

Article Title: Covalent targeting of PSMD14 by Eupalinolide B induces oncoprotein degradation and apoptosis in acute promyelocytic leukemia cells

doi: 10.1039/d5cb00197h

Article Snippet: To identify the direct binding site of EB on PSMD14, 40 μg of recombinant human PSMD14 protein (Signalchem Lifesciences) was incubated with 40 μM EB for 2 h at 37 °C.

Journal: RSC Chemical Biology

Article Title: Covalent targeting of PSMD14 by Eupalinolide B induces oncoprotein degradation and apoptosis in acute promyelocytic leukemia cells

doi: 10.1039/d5cb00197h

Article Snippet: To identify the direct binding site of EB on PSMD14, 40 μg of recombinant human PSMD14 protein (Signalchem Lifesciences) was incubated with 40 μM EB for 2 h at 37 °C.

Techniques: Expressing, Knockdown, Western Blot, Transfection, Negative Control

Journal: Anti-Cancer Drugs

Article Title: Serum heat shock protein family A member 9 protein as a biomarker for bortezomib resistance and poor prognosis in patients with multiple myeloma

doi: 10.1097/CAD.0000000000001764

Figure Lengend Snippet: Expression levels of HSPA9, DKK1, PSMD14, and TRIM21 proteins in MM patients. Serum samples were collected from 46 MM patients and 52 healthy controls, and ELISA was performed to detect the levels of HSPA9 (a), DKK1 (b), TRIM21 (c), and PSMD14 (d) proteins. Data are expressed as mean ± SD from three independent experiments. DKK1, dickkopf Wnt signaling pathway inhibitor 1; HSPA9, heat shock protein family A member 9; MM, multiple myeloma; PSMD14, proteasome 26S subunit non-ATPase 14; TRIM21, tripartite motif containing 21.

Article Snippet: The following ELISA kits were used in the study: HSPA9 (order no. D711242; Sangon Biotech, Shanghai, China), DKK1 (order no. D711029; Sangon Biotech), PSMD14 (order no. CSB-PA018904OB01HU; CUSABIO, Wuhan, China), and TRIM21 (order no. ml106271; Enzyme-linked Biotechnology, Shanghai, China).

Techniques: Expressing, Enzyme-linked Immunosorbent Assay

High expression of PSMD14 is associated with poor prognosis in LUAD. (A) Comparison of PSMD14 expression between tumor and normal tissues across multiple cancer types (pan-cancer analysis). (B) mRNA expression levels of PSMD14 in LUAD and normal tissues from the TCGA and GTEx databases. (C) Protein expression levels of PSMD14 in LUAD and normal tissues based on the CPTAC-LUAD dataset. (D) Receiver operating characteristic (ROC) curve evaluating the diagnostic value of PSMD14 in LUAD. (E) Calibration curve for the PSMD14-based diagnostic model. (F) Positive correlation between PSMD14 expression and advanced tumor stage in LUAD patients. (G) Distribution of patient survival status across PSMD14 expression quartiles: Q1 (top 25%) to Q4 (bottom 25%). The Q1 group showed a significantly higher number of deceased patients. (H) Kaplan–Meier curves comparing overall survival (OS), disease-specific survival (DSS), progression-free interval (PFI), and disease-free interval (DFI) between PSMD14 high- and low-expression groups. (I) Kaplan–Meier analysis of OS based on PSMD14 protein expression in the CPTAC-LUAD cohort. (J) Forest plot summarizing the association between PSMD14 expression and patient survival across multiple GEO datasets. * P < 0.05, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: High expression of PSMD14 is associated with poor prognosis in LUAD. (A) Comparison of PSMD14 expression between tumor and normal tissues across multiple cancer types (pan-cancer analysis). (B) mRNA expression levels of PSMD14 in LUAD and normal tissues from the TCGA and GTEx databases. (C) Protein expression levels of PSMD14 in LUAD and normal tissues based on the CPTAC-LUAD dataset. (D) Receiver operating characteristic (ROC) curve evaluating the diagnostic value of PSMD14 in LUAD. (E) Calibration curve for the PSMD14-based diagnostic model. (F) Positive correlation between PSMD14 expression and advanced tumor stage in LUAD patients. (G) Distribution of patient survival status across PSMD14 expression quartiles: Q1 (top 25%) to Q4 (bottom 25%). The Q1 group showed a significantly higher number of deceased patients. (H) Kaplan–Meier curves comparing overall survival (OS), disease-specific survival (DSS), progression-free interval (PFI), and disease-free interval (DFI) between PSMD14 high- and low-expression groups. (I) Kaplan–Meier analysis of OS based on PSMD14 protein expression in the CPTAC-LUAD cohort. (J) Forest plot summarizing the association between PSMD14 expression and patient survival across multiple GEO datasets. * P < 0.05, **** P < 0.0001.

Article Snippet: The sections were then blocked with 5% goat serum and incubated overnight at 4°C with primary antibodies targeting PSMD14 (1:100; Proteintech, China) and HMMR (1:100; Abways, China).

Techniques: Expressing, Comparison, Diagnostic Assay

Correlation of PSMD14 expression with functional states, signaling pathways, drug sensitivity, and metabolic activity in LUAD. (A) Scatter plots showing the correlation between PSMD14 expression and activity scores of 8 functional states in LUAD. (B) Correlation of PSMD14 expression with pathway activity scores derived from TCPA-RPPA proteomic data. (C) Comparison of activity scores for multiple oncogenic pathways (EGFR, hypoxia, PI3K, TGF-β) between PSMD14 high- and low-expression groups in LUAD. (D) Correlation analysis between PSMD14 expression and sensitivity, represented by the area under the dose–response curve (AUC), to various common chemotherapeutic and targeted agents from the CTRP and PRISM databases. Higher AUC indicates lower drug sensitivity. (E) GSVA identifying specific metabolic pathways that are activated or suppressed in the PSMD14 high-expression group compared to the low-expression group in LUAD.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: Correlation of PSMD14 expression with functional states, signaling pathways, drug sensitivity, and metabolic activity in LUAD. (A) Scatter plots showing the correlation between PSMD14 expression and activity scores of 8 functional states in LUAD. (B) Correlation of PSMD14 expression with pathway activity scores derived from TCPA-RPPA proteomic data. (C) Comparison of activity scores for multiple oncogenic pathways (EGFR, hypoxia, PI3K, TGF-β) between PSMD14 high- and low-expression groups in LUAD. (D) Correlation analysis between PSMD14 expression and sensitivity, represented by the area under the dose–response curve (AUC), to various common chemotherapeutic and targeted agents from the CTRP and PRISM databases. Higher AUC indicates lower drug sensitivity. (E) GSVA identifying specific metabolic pathways that are activated or suppressed in the PSMD14 high-expression group compared to the low-expression group in LUAD.

Techniques: Expressing, Functional Assay, Protein-Protein interactions, Activity Assay, Derivative Assay, Comparison

PSMD14 expression associates with immunosuppressive microenvironment in LUAD. (A) Distribution of six immune subtypes in PSMD14 high- versus low-expression groups (TCGA-LUAD cohort). (B) Expression patterns of immune-related molecules in PSMD14 high- and low-expression groups. Key upregulated molecules indicated. (C) Negative correlation between PSMD14 expression and Tumor Immunity Cycle (TIP) scores. (D) Single-cell RNA-seq reveals cellular composition: malignant cells enriched in PSMD14 + populations, CD8 + T cells in PSMD14 − populations. (E) PSMD14 expression correlates with distinct immune and genomic features: low expression with BCR/TCR diversity and IFN-γ response, high expression with DNA repair deficiency and proliferation. * P < 0.05, ** P < 0.01, *** P < 0.001.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: PSMD14 expression associates with immunosuppressive microenvironment in LUAD. (A) Distribution of six immune subtypes in PSMD14 high- versus low-expression groups (TCGA-LUAD cohort). (B) Expression patterns of immune-related molecules in PSMD14 high- and low-expression groups. Key upregulated molecules indicated. (C) Negative correlation between PSMD14 expression and Tumor Immunity Cycle (TIP) scores. (D) Single-cell RNA-seq reveals cellular composition: malignant cells enriched in PSMD14 + populations, CD8 + T cells in PSMD14 − populations. (E) PSMD14 expression correlates with distinct immune and genomic features: low expression with BCR/TCR diversity and IFN-γ response, high expression with DNA repair deficiency and proliferation. * P < 0.05, ** P < 0.01, *** P < 0.001.

Techniques: Expressing, RNA Sequencing

PSMD14 interacts with and positively regulates HMMR expression. (A) IP-MS analysis identifies potential PSMD14-interacting proteins in H1299 cells overexpressing PSMD14. (B, C) Co-immunoprecipitation assays confirm the interaction between PSMD14 and HMMR in LUAD cells. (D, E) Knockdown and overexpression of PSMD14 demonstrate its positive regulation of HMMR expression at both mRNA and protein levels. (F) Analysis of TCGA-LUAD data reveals significant positive correlation between PSMD14 and HMMR mRNA expression in clinical samples. ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: PSMD14 interacts with and positively regulates HMMR expression. (A) IP-MS analysis identifies potential PSMD14-interacting proteins in H1299 cells overexpressing PSMD14. (B, C) Co-immunoprecipitation assays confirm the interaction between PSMD14 and HMMR in LUAD cells. (D, E) Knockdown and overexpression of PSMD14 demonstrate its positive regulation of HMMR expression at both mRNA and protein levels. (F) Analysis of TCGA-LUAD data reveals significant positive correlation between PSMD14 and HMMR mRNA expression in clinical samples. ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Techniques: Expressing, Protein-Protein interactions, Immunoprecipitation, Knockdown, Over Expression

Coordinated upregulation of PSMD14 and HMMR in LUAD tissues. (A) Western blot showing elevated protein expression of both PSMD14 and HMMR in multiple LUAD cell lines compared to normal bronchial epithelial cells. (B) Western blot and scatter plot demonstrating strong positive correlation between PSMD14 and HMMR protein levels in 12 paired LUAD and adjacent normal tissues. (C) IHC staining showing concurrent upregulation of PSMD14 and HMMR proteins in LUAD specimens compared to adjacent normal tissues. (D) Immunofluorescence imaging revealing spatial co-localization of PSMD14 and HMMR in LUAD cells.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: Coordinated upregulation of PSMD14 and HMMR in LUAD tissues. (A) Western blot showing elevated protein expression of both PSMD14 and HMMR in multiple LUAD cell lines compared to normal bronchial epithelial cells. (B) Western blot and scatter plot demonstrating strong positive correlation between PSMD14 and HMMR protein levels in 12 paired LUAD and adjacent normal tissues. (C) IHC staining showing concurrent upregulation of PSMD14 and HMMR proteins in LUAD specimens compared to adjacent normal tissues. (D) Immunofluorescence imaging revealing spatial co-localization of PSMD14 and HMMR in LUAD cells.

Techniques: Western Blot, Expressing, Immunohistochemistry, Immunofluorescence, Imaging

PSMD14 stabilizes HMMR through K63-linked deubiquitination. (A, B) Cycloheximide (CHX) chase assays show that PSMD14 knockdown reduces while its overexpression extends the half-life of HMMR protein in LUAD cells. (C, D) Ubiquitination assays demonstrate that PSMD14 knockdown enhances whereas its overexpression reduces ubiquitination of HMMR in MG132-treated cells. (E) Ubiquitination analysis using K48R and K63R mutants reveals that PSMD14 specifically removes K63-linked ubiquitin chains from HMMR. ‘ns’ indicates non-significance, ** P < 0.01, *** P < 0.001.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: PSMD14 stabilizes HMMR through K63-linked deubiquitination. (A, B) Cycloheximide (CHX) chase assays show that PSMD14 knockdown reduces while its overexpression extends the half-life of HMMR protein in LUAD cells. (C, D) Ubiquitination assays demonstrate that PSMD14 knockdown enhances whereas its overexpression reduces ubiquitination of HMMR in MG132-treated cells. (E) Ubiquitination analysis using K48R and K63R mutants reveals that PSMD14 specifically removes K63-linked ubiquitin chains from HMMR. ‘ns’ indicates non-significance, ** P < 0.01, *** P < 0.001.

Techniques: Knockdown, Over Expression, Ubiquitin Proteomics

PSMD14 promotes proliferation of lung adenocarcinoma cells and regulates cell cycle progression. (A) CCK-8 assay shows that PSMD14 knockdown inhibits proliferation of H1299, while its overexpression enhances proliferation of H1975 cells. (B) Colony formation assay demonstrates that PSMD14 knockdown reduces colony-forming ability in H1299, whereas its overexpression increases colony formation in H1975 cells. (C) EdU assay further confirms the pro-proliferative effect of PSMD14 in LUAD cells. ** P < 0.01, *** P < 0.001, **** P < 0.0001. (D) Single-cell RNA sequencing analysis depicting PSMD14 expression dynamics across cell cycle phases. (E) Flow cytometric analysis of cell cycle distribution following PSMD14 knockdown in LUAD cells. (F) Depletion of PSMD14 induces G0/G1 phase arrest in LUAD cells. (G) Western blot showing expression changes of key cell cycle regulators upon PSMD14 knockdown.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: PSMD14 promotes proliferation of lung adenocarcinoma cells and regulates cell cycle progression. (A) CCK-8 assay shows that PSMD14 knockdown inhibits proliferation of H1299, while its overexpression enhances proliferation of H1975 cells. (B) Colony formation assay demonstrates that PSMD14 knockdown reduces colony-forming ability in H1299, whereas its overexpression increases colony formation in H1975 cells. (C) EdU assay further confirms the pro-proliferative effect of PSMD14 in LUAD cells. ** P < 0.01, *** P < 0.001, **** P < 0.0001. (D) Single-cell RNA sequencing analysis depicting PSMD14 expression dynamics across cell cycle phases. (E) Flow cytometric analysis of cell cycle distribution following PSMD14 knockdown in LUAD cells. (F) Depletion of PSMD14 induces G0/G1 phase arrest in LUAD cells. (G) Western blot showing expression changes of key cell cycle regulators upon PSMD14 knockdown.

Techniques: CCK-8 Assay, Knockdown, Over Expression, Colony Assay, EdU Assay, RNA Sequencing, Expressing, Western Blot

PSMD14 enhances migration and invasion capabilities of LUAD cells and regulates DNA damage repair in LUAD. (A) Wound healing assay reveals that PSMD14 knockdown impairs cell migration in LUAD cells, while its overexpression promotes migratory capacity. (B) Transwell assay indicates that PSMD14 silencing attenuates migration and invasion abilities of LUAD cells, whereas its overexpression enhances these malignant phenotypes. (C) Western blot analysis of epithelial-mesenchymal transition (EMT)-related markers after PSMD14 knockdown. (D) Western blot analysis of DNA damage repair proteins following PSMD14 depletion. ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: PSMD14 enhances migration and invasion capabilities of LUAD cells and regulates DNA damage repair in LUAD. (A) Wound healing assay reveals that PSMD14 knockdown impairs cell migration in LUAD cells, while its overexpression promotes migratory capacity. (B) Transwell assay indicates that PSMD14 silencing attenuates migration and invasion abilities of LUAD cells, whereas its overexpression enhances these malignant phenotypes. (C) Western blot analysis of epithelial-mesenchymal transition (EMT)-related markers after PSMD14 knockdown. (D) Western blot analysis of DNA damage repair proteins following PSMD14 depletion. ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Techniques: Migration, Wound Healing Assay, Knockdown, Over Expression, Transwell Assay, Western Blot

PSMD14 promotes proliferation, migration, and invasion of LUAD cells by targeting HMMR. (A) HMMR overexpression rescues PSMD14-knockdown phenotypes in H1299 cells (CCK-8, colony formation, and Transwell assays). (B) Similar rescue of malignant phenotypes by HMMR in PSMD14-deficient PC9 cells. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: PSMD14 promotes proliferation, migration, and invasion of LUAD cells by targeting HMMR. (A) HMMR overexpression rescues PSMD14-knockdown phenotypes in H1299 cells (CCK-8, colony formation, and Transwell assays). (B) Similar rescue of malignant phenotypes by HMMR in PSMD14-deficient PC9 cells. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Techniques: Migration, Over Expression, Knockdown, CCK-8 Assay

PSMD14 promotes LUAD progression through HMMR-mediated activation of TGF-β/Smad and PI3K/AKT/mTOR signaling pathways. (A) Kaplan-Meier survival analysis of LUAD patients stratified by PSMD14 and HMMR co-expression patterns. (B) Western blot analysis of TGF-β/Smad pathway components and CD44 expression following PSMD14 modulation. (C) Western blot analysis of PI3K/AKT/mTOR pathway components after PSMD14 knockdown or overexpression. (D) Tumor growth curves in PC9 xenograft models treated with Capzimin, Galunisertib, or their combination. (E) Schematic diagram of the potential mechanism of PSMD14 in LUAD progression. *** P < 0.001, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: PSMD14 drives lung adenocarcinoma progression through HMMR stabilization and dual activation of TGF-β/Smad and PI3K/AKT/mTOR signaling

doi: 10.3389/fimmu.2025.1720799

Figure Lengend Snippet: PSMD14 promotes LUAD progression through HMMR-mediated activation of TGF-β/Smad and PI3K/AKT/mTOR signaling pathways. (A) Kaplan-Meier survival analysis of LUAD patients stratified by PSMD14 and HMMR co-expression patterns. (B) Western blot analysis of TGF-β/Smad pathway components and CD44 expression following PSMD14 modulation. (C) Western blot analysis of PI3K/AKT/mTOR pathway components after PSMD14 knockdown or overexpression. (D) Tumor growth curves in PC9 xenograft models treated with Capzimin, Galunisertib, or their combination. (E) Schematic diagram of the potential mechanism of PSMD14 in LUAD progression. *** P < 0.001, **** P < 0.0001.

Techniques: Activation Assay, Protein-Protein interactions, Expressing, Western Blot, Knockdown, Over Expression

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