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KEY RESOURCES TABLE
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KEY RESOURCES TABLE
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a , b Hallmark pathway of TNFA_NFKB ( a ) and KRAS ( b ) signaling AUC score cluster distributions. c , d Violin plots of the AUC score in TNFA_NFKB ( c ) and KRAS ( d ) signaling in KCs. e – g IB analysis of the indicated proteins of NF-κB and MAPK signaling pathway in HaCaT after treatment with LZTR1 sgRNA ( e ), primary mouse KC ( f ), and mouse epidermis ( g ). h – n MFI level of membrane HLA-ABC or mRNA level of HLA-A, HLA-B in Ctrl and LZTR1 KO HaCaT treated with 5 μM NF-κB inhibitor QNZ ( h – j ), si <t>NFKB1</t> ( k , l ) or overexpressed (oe)- NFKB1 ( m , n ). veh, vehicle ( n = 2–4). o qPCR of H2-D1 and H2-K1 mRNA expression in KCs from mice treated with si Nfkb1 and IFNγ ( n = 4). p , q Schematic diagram of promoter site construction and results for dual luciferase assay of HLA-A ( p ) and HLA-B ( q ) with si NFKB1 or oe- NFKB1 ( n = 3). r Relative enrichment fold of HLA-A and HLA-B promoter sequence immunoprecipitated with NF-κB1 in HaCaT analyzed by qPCR ( n = 3). s NF-κB1 predictive binding site on HLA-A and HLA-B promoter. t Schematic diagram of NF-κB1-binding deficiency promoter construction. u – x Quantification of luciferase activity level of HLA-A and HLA-B in WT or mutant promoter combined with si NFKB1 ( u , v ) and LZTR1 KO ( w , x ) ( n = 3). y Schematic mechanism diagram of LZTR1 regulating MHC-I. ns: not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by Wilcoxon rank test ( c ), one-way ANOVA ( k ) and two-way ANOVA ( i , j , l , n – r , u – x ). Data are shown as mean ± SEM.
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a , b Hallmark pathway of TNFA_NFKB ( a ) and KRAS ( b ) signaling AUC score cluster distributions. c , d Violin plots of the AUC score in TNFA_NFKB ( c ) and KRAS ( d ) signaling in KCs. e – g IB analysis of the indicated proteins of NF-κB and MAPK signaling pathway in HaCaT after treatment with LZTR1 sgRNA ( e ), primary mouse KC ( f ), and mouse epidermis ( g ). h – n MFI level of membrane HLA-ABC or mRNA level of HLA-A, HLA-B in Ctrl and LZTR1 KO HaCaT treated with 5 μM NF-κB inhibitor QNZ ( h – j ), si <t>NFKB1</t> ( k , l ) or overexpressed (oe)- NFKB1 ( m , n ). veh, vehicle ( n = 2–4). o qPCR of H2-D1 and H2-K1 mRNA expression in KCs from mice treated with si Nfkb1 and IFNγ ( n = 4). p , q Schematic diagram of promoter site construction and results for dual luciferase assay of HLA-A ( p ) and HLA-B ( q ) with si NFKB1 or oe- NFKB1 ( n = 3). r Relative enrichment fold of HLA-A and HLA-B promoter sequence immunoprecipitated with NF-κB1 in HaCaT analyzed by qPCR ( n = 3). s NF-κB1 predictive binding site on HLA-A and HLA-B promoter. t Schematic diagram of NF-κB1-binding deficiency promoter construction. u – x Quantification of luciferase activity level of HLA-A and HLA-B in WT or mutant promoter combined with si NFKB1 ( u , v ) and LZTR1 KO ( w , x ) ( n = 3). y Schematic mechanism diagram of LZTR1 regulating MHC-I. ns: not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by Wilcoxon rank test ( c ), one-way ANOVA ( k ) and two-way ANOVA ( i , j , l , n – r , u – x ). Data are shown as mean ± SEM.
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a , b Hallmark pathway of TNFA_NFKB ( a ) and KRAS ( b ) signaling AUC score cluster distributions. c , d Violin plots of the AUC score in TNFA_NFKB ( c ) and KRAS ( d ) signaling in KCs. e – g IB analysis of the indicated proteins of NF-κB and MAPK signaling pathway in HaCaT after treatment with LZTR1 sgRNA ( e ), primary mouse KC ( f ), and mouse epidermis ( g ). h – n MFI level of membrane HLA-ABC or mRNA level of HLA-A, HLA-B in Ctrl and LZTR1 KO HaCaT treated with 5 μM NF-κB inhibitor QNZ ( h – j ), si <t>NFKB1</t> ( k , l ) or overexpressed (oe)- NFKB1 ( m , n ). veh, vehicle ( n = 2–4). o qPCR of H2-D1 and H2-K1 mRNA expression in KCs from mice treated with si Nfkb1 and IFNγ ( n = 4). p , q Schematic diagram of promoter site construction and results for dual luciferase assay of HLA-A ( p ) and HLA-B ( q ) with si NFKB1 or oe- NFKB1 ( n = 3). r Relative enrichment fold of HLA-A and HLA-B promoter sequence immunoprecipitated with NF-κB1 in HaCaT analyzed by qPCR ( n = 3). s NF-κB1 predictive binding site on HLA-A and HLA-B promoter. t Schematic diagram of NF-κB1-binding deficiency promoter construction. u – x Quantification of luciferase activity level of HLA-A and HLA-B in WT or mutant promoter combined with si NFKB1 ( u , v ) and LZTR1 KO ( w , x ) ( n = 3). y Schematic mechanism diagram of LZTR1 regulating MHC-I. ns: not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by Wilcoxon rank test ( c ), one-way ANOVA ( k ) and two-way ANOVA ( i , j , l , n – r , u – x ). Data are shown as mean ± SEM.
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a , b Hallmark pathway of TNFA_NFKB ( a ) and KRAS ( b ) signaling AUC score cluster distributions. c , d Violin plots of the AUC score in TNFA_NFKB ( c ) and KRAS ( d ) signaling in KCs. e – g IB analysis of the indicated proteins of NF-κB and MAPK signaling pathway in HaCaT after treatment with LZTR1 sgRNA ( e ), primary mouse KC ( f ), and mouse epidermis ( g ). h – n MFI level of membrane HLA-ABC or mRNA level of HLA-A, HLA-B in Ctrl and LZTR1 KO HaCaT treated with 5 μM NF-κB inhibitor QNZ ( h – j ), si <t>NFKB1</t> ( k , l ) or overexpressed (oe)- NFKB1 ( m , n ). veh, vehicle ( n = 2–4). o qPCR of H2-D1 and H2-K1 mRNA expression in KCs from mice treated with si Nfkb1 and IFNγ ( n = 4). p , q Schematic diagram of promoter site construction and results for dual luciferase assay of HLA-A ( p ) and HLA-B ( q ) with si NFKB1 or oe- NFKB1 ( n = 3). r Relative enrichment fold of HLA-A and HLA-B promoter sequence immunoprecipitated with NF-κB1 in HaCaT analyzed by qPCR ( n = 3). s NF-κB1 predictive binding site on HLA-A and HLA-B promoter. t Schematic diagram of NF-κB1-binding deficiency promoter construction. u – x Quantification of luciferase activity level of HLA-A and HLA-B in WT or mutant promoter combined with si NFKB1 ( u , v ) and LZTR1 KO ( w , x ) ( n = 3). y Schematic mechanism diagram of LZTR1 regulating MHC-I. ns: not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by Wilcoxon rank test ( c ), one-way ANOVA ( k ) and two-way ANOVA ( i , j , l , n – r , u – x ). Data are shown as mean ± SEM.
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Image Search Results


KEY RESOURCES TABLE

Journal: Molecular cell

Article Title: Phosphorylated RB Promotes Cancer Immunity by Inhibiting NF-κB Activation and PD-L1 Expression

doi: 10.1016/j.molcel.2018.10.034

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Mouse monoclonal anti-c-Rel , Santa Cruz , Cat# sc-6955; RRID: AB_670194.

Techniques: Virus, Recombinant, Control, Mutagenesis, Kinase Assay, Sequencing, CRAfT Assay, Software

a , b Hallmark pathway of TNFA_NFKB ( a ) and KRAS ( b ) signaling AUC score cluster distributions. c , d Violin plots of the AUC score in TNFA_NFKB ( c ) and KRAS ( d ) signaling in KCs. e – g IB analysis of the indicated proteins of NF-κB and MAPK signaling pathway in HaCaT after treatment with LZTR1 sgRNA ( e ), primary mouse KC ( f ), and mouse epidermis ( g ). h – n MFI level of membrane HLA-ABC or mRNA level of HLA-A, HLA-B in Ctrl and LZTR1 KO HaCaT treated with 5 μM NF-κB inhibitor QNZ ( h – j ), si NFKB1 ( k , l ) or overexpressed (oe)- NFKB1 ( m , n ). veh, vehicle ( n = 2–4). o qPCR of H2-D1 and H2-K1 mRNA expression in KCs from mice treated with si Nfkb1 and IFNγ ( n = 4). p , q Schematic diagram of promoter site construction and results for dual luciferase assay of HLA-A ( p ) and HLA-B ( q ) with si NFKB1 or oe- NFKB1 ( n = 3). r Relative enrichment fold of HLA-A and HLA-B promoter sequence immunoprecipitated with NF-κB1 in HaCaT analyzed by qPCR ( n = 3). s NF-κB1 predictive binding site on HLA-A and HLA-B promoter. t Schematic diagram of NF-κB1-binding deficiency promoter construction. u – x Quantification of luciferase activity level of HLA-A and HLA-B in WT or mutant promoter combined with si NFKB1 ( u , v ) and LZTR1 KO ( w , x ) ( n = 3). y Schematic mechanism diagram of LZTR1 regulating MHC-I. ns: not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by Wilcoxon rank test ( c ), one-way ANOVA ( k ) and two-way ANOVA ( i , j , l , n – r , u – x ). Data are shown as mean ± SEM.

Journal: Cell Discovery

Article Title: LZTR1 regulates epithelial MHC-I expression via NF-κB1 to modulate CD8 + T cells activation

doi: 10.1038/s41421-025-00837-6

Figure Lengend Snippet: a , b Hallmark pathway of TNFA_NFKB ( a ) and KRAS ( b ) signaling AUC score cluster distributions. c , d Violin plots of the AUC score in TNFA_NFKB ( c ) and KRAS ( d ) signaling in KCs. e – g IB analysis of the indicated proteins of NF-κB and MAPK signaling pathway in HaCaT after treatment with LZTR1 sgRNA ( e ), primary mouse KC ( f ), and mouse epidermis ( g ). h – n MFI level of membrane HLA-ABC or mRNA level of HLA-A, HLA-B in Ctrl and LZTR1 KO HaCaT treated with 5 μM NF-κB inhibitor QNZ ( h – j ), si NFKB1 ( k , l ) or overexpressed (oe)- NFKB1 ( m , n ). veh, vehicle ( n = 2–4). o qPCR of H2-D1 and H2-K1 mRNA expression in KCs from mice treated with si Nfkb1 and IFNγ ( n = 4). p , q Schematic diagram of promoter site construction and results for dual luciferase assay of HLA-A ( p ) and HLA-B ( q ) with si NFKB1 or oe- NFKB1 ( n = 3). r Relative enrichment fold of HLA-A and HLA-B promoter sequence immunoprecipitated with NF-κB1 in HaCaT analyzed by qPCR ( n = 3). s NF-κB1 predictive binding site on HLA-A and HLA-B promoter. t Schematic diagram of NF-κB1-binding deficiency promoter construction. u – x Quantification of luciferase activity level of HLA-A and HLA-B in WT or mutant promoter combined with si NFKB1 ( u , v ) and LZTR1 KO ( w , x ) ( n = 3). y Schematic mechanism diagram of LZTR1 regulating MHC-I. ns: not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by Wilcoxon rank test ( c ), one-way ANOVA ( k ) and two-way ANOVA ( i , j , l , n – r , u – x ). Data are shown as mean ± SEM.

Article Snippet: Equal amounts of protein were resolved by SDS–PAGE and immunoblotted with anti-LZTR1 (cat. ab289965, Abcam, 1:1000), anti-HLA-A (cat. ab52922, Abcam, 1:1000), anti-HLA-B (cat. ab193415, Abcam, 1:1000), anti-HLA-C (cat. sc-166057, Santa Cruz, 1:100), anti-GAPDH (cat. 60004-I-Ig, Proteintech, 1:3000), anti-HLA-C (cat. PA5-79367, Thermo Fisher, 1:1000), anti-NFκB1 p105/p50 (cat. 13586S, CST, 1:1000), anti-NFκB2 p100/p52 (cat. 37359S, CST, 1:1000), anti-NFκB p65 (cat. 8242S, CST, 1:1000), anti-pho-NFκB p65 (cat. 3033S, CST, 1:1000), anti-c-REL (cat. ab133251, Abcam, 1:1000), Anti-Erk (cat. 4695S, CST, 1:1000), anti-p-Erk (cat. 4370S, CST, 1:1000), anti-P38 (cat. 8690S, CST, 1:1000), anti-p-P38 (cat. 4511S, CST, 1:1000), anti-TUBULIN (cat. 11224-1-AP, Proteintech, 1:2000), anti-FLAG (cat. F1804-1MG, Sigma, 1:1000), anti-HA-Tag (cat. sc-7392, Santa Cruz, 1:100), anti-PSMA6 (cat. ab109377, Abcam, 1:50000), anti-PAMS7 (cat. ab133502, Abcam, 1:1000), anti-RPS3 (cat. ab128995, Abcam, 1:1000), anti-Ubiquitin (cat. sc-8017, Santa Cruz, 1:100).

Techniques: Membrane, Expressing, Luciferase, Sequencing, Immunoprecipitation, Binding Assay, Activity Assay, Mutagenesis

a , b IB analysis of HaCaT treated with 400 nM Baf-A1 ( a ) and 20 μM MG132 ( b ) for the indicated times. Right: summary plot of IB. c – f Ctrl and LZTR1 KO HaCaT cells were treated with 50 μg/mL CHX ( c ) and 20 μM MG132 ( d ) for the indicated times, and corresponding NF-κB1 quantification ( e , f ). g IB analysis of FLAG-LZTR1, PSMA6, PSMA7, and RPS3 in FLAG-LZTR1 precipitates immunoprecipitated from HaCaT cells reconstituted with either empty vector (EV) or FLAG-tagged human LZTR1. WCL: whole cell lysate. h Schematic domain structure of LZTR1 and design on domain mutation. i IB analysis of FLAG-LZTR1 and HA-RPS3 in FLAG-LZTR1 precipitates immunoprecipitated from HaCaT cells transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2) along with HA-RPS3. j IF of proteasome alpha unit and RPS3 in LZTR1 KO HaCaT cells transfected with different plasmid by confocal microscopy. Scale bars, 5 μm. k IB analysis of NF-κB1 (p50) and HLA-C expression in LZTR1 KO HaCaT cells additionally transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2). l , m FCM of HLA-ABC expression in LZTR1 KO HaCaT cells additionally transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2) and Quantitation ( m ) ( n = 3). n qPCR of HLA-A, HLA-B mRNA expression among LZTR1 KO HaCaT cells transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2) ( n = 3). o Mechanistic model of LZTR1 on co-translational biogenesis process. Up: ubiquitination-dependent p50 generation from p105; down: ubiquitination-independent but LZTR1-involved p50 generation from p105. ns: not significant; ** P < 0.01, **** P < 0.0001 by one-way ANOVA ( m , n ). Data are shown as mean ± SEM.

Journal: Cell Discovery

Article Title: LZTR1 regulates epithelial MHC-I expression via NF-κB1 to modulate CD8 + T cells activation

doi: 10.1038/s41421-025-00837-6

Figure Lengend Snippet: a , b IB analysis of HaCaT treated with 400 nM Baf-A1 ( a ) and 20 μM MG132 ( b ) for the indicated times. Right: summary plot of IB. c – f Ctrl and LZTR1 KO HaCaT cells were treated with 50 μg/mL CHX ( c ) and 20 μM MG132 ( d ) for the indicated times, and corresponding NF-κB1 quantification ( e , f ). g IB analysis of FLAG-LZTR1, PSMA6, PSMA7, and RPS3 in FLAG-LZTR1 precipitates immunoprecipitated from HaCaT cells reconstituted with either empty vector (EV) or FLAG-tagged human LZTR1. WCL: whole cell lysate. h Schematic domain structure of LZTR1 and design on domain mutation. i IB analysis of FLAG-LZTR1 and HA-RPS3 in FLAG-LZTR1 precipitates immunoprecipitated from HaCaT cells transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2) along with HA-RPS3. j IF of proteasome alpha unit and RPS3 in LZTR1 KO HaCaT cells transfected with different plasmid by confocal microscopy. Scale bars, 5 μm. k IB analysis of NF-κB1 (p50) and HLA-C expression in LZTR1 KO HaCaT cells additionally transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2). l , m FCM of HLA-ABC expression in LZTR1 KO HaCaT cells additionally transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2) and Quantitation ( m ) ( n = 3). n qPCR of HLA-A, HLA-B mRNA expression among LZTR1 KO HaCaT cells transfected with EV (−), FLAG-LZTR1 (FULL), FLAG-LZTR1 ΔKelch (ΔKelch), FLAG-LZTR1 ΔBTB1 (ΔBTB1), FLAG-LZTR1 ΔBTB2 (ΔBTB2) ( n = 3). o Mechanistic model of LZTR1 on co-translational biogenesis process. Up: ubiquitination-dependent p50 generation from p105; down: ubiquitination-independent but LZTR1-involved p50 generation from p105. ns: not significant; ** P < 0.01, **** P < 0.0001 by one-way ANOVA ( m , n ). Data are shown as mean ± SEM.

Article Snippet: Equal amounts of protein were resolved by SDS–PAGE and immunoblotted with anti-LZTR1 (cat. ab289965, Abcam, 1:1000), anti-HLA-A (cat. ab52922, Abcam, 1:1000), anti-HLA-B (cat. ab193415, Abcam, 1:1000), anti-HLA-C (cat. sc-166057, Santa Cruz, 1:100), anti-GAPDH (cat. 60004-I-Ig, Proteintech, 1:3000), anti-HLA-C (cat. PA5-79367, Thermo Fisher, 1:1000), anti-NFκB1 p105/p50 (cat. 13586S, CST, 1:1000), anti-NFκB2 p100/p52 (cat. 37359S, CST, 1:1000), anti-NFκB p65 (cat. 8242S, CST, 1:1000), anti-pho-NFκB p65 (cat. 3033S, CST, 1:1000), anti-c-REL (cat. ab133251, Abcam, 1:1000), Anti-Erk (cat. 4695S, CST, 1:1000), anti-p-Erk (cat. 4370S, CST, 1:1000), anti-P38 (cat. 8690S, CST, 1:1000), anti-p-P38 (cat. 4511S, CST, 1:1000), anti-TUBULIN (cat. 11224-1-AP, Proteintech, 1:2000), anti-FLAG (cat. F1804-1MG, Sigma, 1:1000), anti-HA-Tag (cat. sc-7392, Santa Cruz, 1:100), anti-PSMA6 (cat. ab109377, Abcam, 1:50000), anti-PAMS7 (cat. ab133502, Abcam, 1:1000), anti-RPS3 (cat. ab128995, Abcam, 1:1000), anti-Ubiquitin (cat. sc-8017, Santa Cruz, 1:100).

Techniques: Immunoprecipitation, Plasmid Preparation, Mutagenesis, Transfection, Confocal Microscopy, Expressing, Quantitation Assay, Ubiquitin Proteomics