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antibodies against pinx1 12368-1-ap (Proteintech)

Name: antibodies against pinx1 12368-1-ap
Brand: Proteintech
Rating: 90 (1 reviews)

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Proteintech antibodies against pinx1 12368-1-ap
Antibodies Against Pinx1 12368 1 Ap, supplied by Proteintech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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A Volcano plot of proximity proteomics of a PARP1-TurboID against a TurboID control. B Volcano plot of proximity proteomics of a PARP1-TurboID with or without biotin treatment. The p -values were calculated by a two-sample t -test. Curves indicate a minimal fold change >2, <−2, and 5% FDR calculated by Perseus. Proteins that show significant proximity to PARP1 are depicted in black dots, while proteins that show significant proximity to PARP1 both in ( A ) and in ( B ) are marked with red stars. C Venn diagram of proximity proteins in ( A ) and ( B ). D – F Exogenous co-IP to confirm the binding between PINX1/UTP14A/ZNF24 and PARP1. PARP1-Myc and PINX1/UTP14A/ZNF24-FLAG constructs were co-transfected into HEK293T cells, and IP of whole cell lysates with anti-FLAG agarose beads was performed. G – I Reciprocal exogenous co-IP to confirm the binding between PINX1/UTP14A/ZNF24 and PARP1. PARP1-Myc and PINX1/UTP14A/ZNF24-FLAG constructs were co-transfected into HEK293T cells, and IP of whole cell lysates with anti-Myc agarose beads was performed.

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: A Volcano plot of proximity proteomics of a PARP1-TurboID against a TurboID control. B Volcano plot of proximity proteomics of a PARP1-TurboID with or without biotin treatment. The p -values were calculated by a two-sample t -test. Curves indicate a minimal fold change >2, <−2, and 5% FDR calculated by Perseus. Proteins that show significant proximity to PARP1 are depicted in black dots, while proteins that show significant proximity to PARP1 both in ( A ) and in ( B ) are marked with red stars. C Venn diagram of proximity proteins in ( A ) and ( B ). D – F Exogenous co-IP to confirm the binding between PINX1/UTP14A/ZNF24 and PARP1. PARP1-Myc and PINX1/UTP14A/ZNF24-FLAG constructs were co-transfected into HEK293T cells, and IP of whole cell lysates with anti-FLAG agarose beads was performed. G – I Reciprocal exogenous co-IP to confirm the binding between PINX1/UTP14A/ZNF24 and PARP1. PARP1-Myc and PINX1/UTP14A/ZNF24-FLAG constructs were co-transfected into HEK293T cells, and IP of whole cell lysates with anti-Myc agarose beads was performed.

Article Snippet: Following primary antibodies were used for western blot analysis in this study: FLAG (GNI, Cat# GNI4110-FG), Myc (Cell Signaling, Cat# 2276S), GAPDH (Proteintech, Cat# 10494-1-AP-100UL), γ-tubulin (Sigma-Aldrich, Cat# T6557), Vinculin (Sigma, Cat# V4505), PINX1 (Proteintech, Cat# 12368-1-AP-50ul), PAR (R&D, Cat# 4335-MC-100), PARP1 (Cell Signaling, Cat# 9542S), Lamin B1 (Bimake, Cat# A5106), β-tubulin (Eastacres Biologicals, Cat# MaTub-b), XRCC1 (Bimake, Cat# A5299), PCNA (Santa Cruz, Cat# sc-7907), γH2AX (Millipore, Cat# 05-636), Histone H3 (Bimake, Cat# A5885), Lamin B (Santa Cruz, Cat# sc-6216), FLAG (Abclonal, Cat# AE063), Myc (Abclonal, Cat# AE070), UTP14A (Abclonal, Cat# A5960), ZNF24 (Santa Cruz, Cat# sc-393359), ATM (Beyotime, Cat# AF1399), ATM p-Ser1981 (Abclonal, Cat# AP0008), ATR (Beyotime, Cat# AF6267), ATR p-Thr1989 (GeneTex, Cat# GTX637560-S), GFP (BBI, Cat# D110008), mCherry (OriGene, Cat# AB8181-200).

Techniques: Control, Co-Immunoprecipitation Assay, Binding Assay, Construct, Transfection

$A Sensitivity of WT and PINX1 KO Hela cells to Talazoparib. PINX1 KO -1 and PINX1 KO -2 represent two distinct PINX1 KO single clones derived from WT Hela cells. B , C Sensitivity of indicated Hela cell lines to Talazoparib ( B ) or Olaparib ( C ). WT_EV, PINX1 KO _EV, PINX1 KO _PINX1, and PINX1 KO _PINX1[1-253aa] are stable cell lines reconstituted with corresponding empty vector (EV), full-length PINX1 or TID domain truncated PINX1 (PINX1[1-253aa]) using lentivirus. D – F Sensitivity of PINX1 knockdown OVCAR8 ( D ), OC316 ( E ), and BEL7404 ( F ) cells to Talazoparib. shLuc was used as a non-targeted control. A – F The cell lines were treated with indicated drugs and allowed to grow for 6 days. Cell viability was assessed by the Cell Titer-Glo assay. Surviving fractions were calculated relative to control untreated cells. All dots and error bars represent means ± SDs from at least three independent experiments. Statistical analyses were performed using two-way ANOVA testing. G Schematic illustration of the treatment protocol in the OC316 xenograft model. H Tumor growth curves of OC316 xenograft tumor-bearing mice for each indicated group ( n = 5). Significance was determined by an unpaired t-test at the endpoint. Error bars show ±1 SEM. I Tumor weight measurement at the endpoint of ( G ). Significance was determined by an unpaired t -test. Error bars show ±1 SD. J Images of dissected tumor tissues for each indicated group. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.$

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: A Sensitivity of WT and PINX1 KO Hela cells to Talazoparib. PINX1 KO -1 and PINX1 KO -2 represent two distinct PINX1 KO single clones derived from WT Hela cells. B , C Sensitivity of indicated Hela cell lines to Talazoparib ( B ) or Olaparib ( C ). WT_EV, PINX1 KO _EV, PINX1 KO _PINX1, and PINX1 KO _PINX1[1-253aa] are stable cell lines reconstituted with corresponding empty vector (EV), full-length PINX1 or TID domain truncated PINX1 (PINX1[1-253aa]) using lentivirus. D – F Sensitivity of PINX1 knockdown OVCAR8 ( D ), OC316 ( E ), and BEL7404 ( F ) cells to Talazoparib. shLuc was used as a non-targeted control. A – F The cell lines were treated with indicated drugs and allowed to grow for 6 days. Cell viability was assessed by the Cell Titer-Glo assay. Surviving fractions were calculated relative to control untreated cells. All dots and error bars represent means ± SDs from at least three independent experiments. Statistical analyses were performed using two-way ANOVA testing. G Schematic illustration of the treatment protocol in the OC316 xenograft model. H Tumor growth curves of OC316 xenograft tumor-bearing mice for each indicated group ( n = 5). Significance was determined by an unpaired t-test at the endpoint. Error bars show ±1 SEM. I Tumor weight measurement at the endpoint of ( G ). Significance was determined by an unpaired t -test. Error bars show ±1 SD. J Images of dissected tumor tissues for each indicated group. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

Techniques: Clone Assay, Derivative Assay, Stable Transfection, Plasmid Preparation, Knockdown, Control, Glo Assay

$A Sensitivity of WT, PINX1 KO , and PARP1 KO PINX1 KO Hela cells to etoposide. B Sensitivity of indicated Hela cell lines to etoposide. PINX1 KO _EV, PINX1 KO _PINX1, and PINX1 KO _PINX1[1–253aa] are stable cell lines reconstituted with corresponding empty vector (EV), full-length PINX1 or TID domain truncated PINX1 (PINX1[1–253aa]) using lentivirus. A , B The cell lines were treated with indicated drugs and allowed to grow for 6 days. Cell viability was assessed by the Cell Titer-Glo assay. Surviving fractions were calculated relative to control untreated cells. All dots and error bars represent means ± SDs from at least three independent experiments. Statistical analyses were performed using two-way ANOVA testing. C Unrepaired DNA strand breaks quantified by alkaline comet assays in the WT and the indicated gene-edited Hela cell lines following treatment with 10 µM etoposide for 30 min and recovery for 30 min. Data plotted are the individual comet tail moments (an arbitrary measure of DNA strand breakage) of ≥116 cells per condition normalized to corresponding no-treatment control (NTC) cells. Significance was determined by an unpaired t -test. Error bars show ±1 SEM. D Representative images of the levels of γH2AX in WT, PARP1 KO , PINX1 KO , and PARP1 KO PINX1 KO Hela cells upon treatment with 10 µM etoposide for 30 min and recovery for 3 h. Red, γH2AX; blue, DAPI. Scale bar, 20 μm. E Measurement of remaining γH2AX levels in WT, PARP1 KO , PINX1 KO, and PARP1 KO PINX1 KO Hela cells by immunofluorescence upon treatment with 10 µM etoposide for 30 min and recovery for 3 h. γH2AX intensity was normalized to 0 for untreated cells and 100% for cells without recovery in each cell line. More than 65 cells were analyzed per condition. Significance was determined by an unpaired t-test. Error bars show ±1 SEM. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.$

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: A Sensitivity of WT, PINX1 KO , and PARP1 KO PINX1 KO Hela cells to etoposide. B Sensitivity of indicated Hela cell lines to etoposide. PINX1 KO _EV, PINX1 KO _PINX1, and PINX1 KO _PINX1[1–253aa] are stable cell lines reconstituted with corresponding empty vector (EV), full-length PINX1 or TID domain truncated PINX1 (PINX1[1–253aa]) using lentivirus. A , B The cell lines were treated with indicated drugs and allowed to grow for 6 days. Cell viability was assessed by the Cell Titer-Glo assay. Surviving fractions were calculated relative to control untreated cells. All dots and error bars represent means ± SDs from at least three independent experiments. Statistical analyses were performed using two-way ANOVA testing. C Unrepaired DNA strand breaks quantified by alkaline comet assays in the WT and the indicated gene-edited Hela cell lines following treatment with 10 µM etoposide for 30 min and recovery for 30 min. Data plotted are the individual comet tail moments (an arbitrary measure of DNA strand breakage) of ≥116 cells per condition normalized to corresponding no-treatment control (NTC) cells. Significance was determined by an unpaired t -test. Error bars show ±1 SEM. D Representative images of the levels of γH2AX in WT, PARP1 KO , PINX1 KO , and PARP1 KO PINX1 KO Hela cells upon treatment with 10 µM etoposide for 30 min and recovery for 3 h. Red, γH2AX; blue, DAPI. Scale bar, 20 μm. E Measurement of remaining γH2AX levels in WT, PARP1 KO , PINX1 KO, and PARP1 KO PINX1 KO Hela cells by immunofluorescence upon treatment with 10 µM etoposide for 30 min and recovery for 3 h. γH2AX intensity was normalized to 0 for untreated cells and 100% for cells without recovery in each cell line. More than 65 cells were analyzed per condition. Significance was determined by an unpaired t-test. Error bars show ±1 SEM. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

Techniques: Stable Transfection, Plasmid Preparation, Glo Assay, Control, Immunofluorescence

A Representative images of the recruitment of indicated proteins to the laser-induced DNA damage sites. U2OS cells were co-transfected with PARP1–EGFP and PINX1/UTP14A/ZNF24–FLAG constructs, pre-sensitized with Hoechst 33342 before micro-irradiation with a 405 nm laser, and subjected to immunostaining with an anti-FLAG antibody. The enrichment of PARP1–EGFP was used to track the DNA damage sites, and PCNA was used as a positive control for the immunostaining. Red, FLAG; green, EGFP; blue, Hoechst 33342. Scale bar, 10 μm. B , C Recruitment kinetics of PINX1-mCherry ( B ) and PARP1-EGFP ( C ) to DNA lesions in Hela cells. Hela cells were co-transfected with PINX1-mCherry and PARP1-EGFP constructs and pre-sensitized with Hoechst 33342 before micro-irradiation coupled live-cell imaging. Seventeen nuclei were analyzed, and the intensity of the damaged region was normalized to that of the undamaged region for the relative recruitment. The vertical dotted line indicates the time of laser stimulation. Curves are shown as means ± SEMs. D Violin plot of Pearson’s R value of colocalization between PINX1–EGFP and γH2AX at indicated time points after laser-induced DNA damage. Hela cells were transfected with PINX1–EGFP and subjected to micro-irradiation as described in Methods and fixed at different time points for immunostaining of γH2AX. More than twenty-nine cells were analyzed per condition. E Representative images of the recruitment of PINX1-mCherry to the laser-induced DNA damage sites in PARP1 KO PINX1 KO Hela cells transfected with a PARP1 construct (+PARP1) or corresponding empty vector (+EV). Laser stimulation was performed at 10 s. Scale bar, 10 μm. F Recruitment kinetics of PINX1-mCherry to the laser-induced DNA damage sites in PARP1 KO PINX1 KO Hela cells transfected with a PARP1 construct (+PARP1) or corresponding empty vector (+EV). More than sixty nuclei were analyzed per condition. The vertical dotted line indicates the time of laser stimulation. Curves are shown as means ± SEMs. Statistical analyses were performed using two-way ANOVA testing. G Representative images of the recruitment of XRCC1–EGFP to the laser-induced DNA damage sites in WT_EV (WT), PINX1 KO _EV (PINX1 KO ), PINX1 KO _PINX1 Hela cells. Laser stimulation was performed at 10 s. Scale bar, 10 μm. H Recruitment kinetics of XRCC1–EGFP to the laser-induced DNA damage sites in WT_EV (WT), PINX1 KO _EV (PINX1 KO ), PINX1 KO _PINX1 Hela cells. More than 31 nuclei were analyzed per condition. The vertical dotted line indicates the time of laser stimulation. Curves are shown as means ± SEMs. Statistical analyses were performed using two-way ANOVA testing. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: A Representative images of the recruitment of indicated proteins to the laser-induced DNA damage sites. U2OS cells were co-transfected with PARP1–EGFP and PINX1/UTP14A/ZNF24–FLAG constructs, pre-sensitized with Hoechst 33342 before micro-irradiation with a 405 nm laser, and subjected to immunostaining with an anti-FLAG antibody. The enrichment of PARP1–EGFP was used to track the DNA damage sites, and PCNA was used as a positive control for the immunostaining. Red, FLAG; green, EGFP; blue, Hoechst 33342. Scale bar, 10 μm. B , C Recruitment kinetics of PINX1-mCherry ( B ) and PARP1-EGFP ( C ) to DNA lesions in Hela cells. Hela cells were co-transfected with PINX1-mCherry and PARP1-EGFP constructs and pre-sensitized with Hoechst 33342 before micro-irradiation coupled live-cell imaging. Seventeen nuclei were analyzed, and the intensity of the damaged region was normalized to that of the undamaged region for the relative recruitment. The vertical dotted line indicates the time of laser stimulation. Curves are shown as means ± SEMs. D Violin plot of Pearson’s R value of colocalization between PINX1–EGFP and γH2AX at indicated time points after laser-induced DNA damage. Hela cells were transfected with PINX1–EGFP and subjected to micro-irradiation as described in Methods and fixed at different time points for immunostaining of γH2AX. More than twenty-nine cells were analyzed per condition. E Representative images of the recruitment of PINX1-mCherry to the laser-induced DNA damage sites in PARP1 KO PINX1 KO Hela cells transfected with a PARP1 construct (+PARP1) or corresponding empty vector (+EV). Laser stimulation was performed at 10 s. Scale bar, 10 μm. F Recruitment kinetics of PINX1-mCherry to the laser-induced DNA damage sites in PARP1 KO PINX1 KO Hela cells transfected with a PARP1 construct (+PARP1) or corresponding empty vector (+EV). More than sixty nuclei were analyzed per condition. The vertical dotted line indicates the time of laser stimulation. Curves are shown as means ± SEMs. Statistical analyses were performed using two-way ANOVA testing. G Representative images of the recruitment of XRCC1–EGFP to the laser-induced DNA damage sites in WT_EV (WT), PINX1 KO _EV (PINX1 KO ), PINX1 KO _PINX1 Hela cells. Laser stimulation was performed at 10 s. Scale bar, 10 μm. H Recruitment kinetics of XRCC1–EGFP to the laser-induced DNA damage sites in WT_EV (WT), PINX1 KO _EV (PINX1 KO ), PINX1 KO _PINX1 Hela cells. More than 31 nuclei were analyzed per condition. The vertical dotted line indicates the time of laser stimulation. Curves are shown as means ± SEMs. Statistical analyses were performed using two-way ANOVA testing. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

Techniques: Transfection, Construct, Irradiation, Immunostaining, Positive Control, Live Cell Imaging, Plasmid Preparation

A The schematic diagram of PARP1 motifs and mutants used for domain mapping and the summary of their binding ability with PINX1. Numbers indicate the respective amino acid positions. B Effect of PARP activation or inhibition on the association between PARP1 and PINX1. PINX1–FLAG was co-transfected with PARP1-Myc into HEK293T cells. Cells were pre-treated with DMSO or 1 µM Olaparib for 40 min before treatment with 50 µM MNNG for 15 min or 2 mM H 2 O 2 for 5 min. IP of whole cell lysates with anti-FLAG agarose beads was performed.

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: A The schematic diagram of PARP1 motifs and mutants used for domain mapping and the summary of their binding ability with PINX1. Numbers indicate the respective amino acid positions. B Effect of PARP activation or inhibition on the association between PARP1 and PINX1. PINX1–FLAG was co-transfected with PARP1-Myc into HEK293T cells. Cells were pre-treated with DMSO or 1 µM Olaparib for 40 min before treatment with 50 µM MNNG for 15 min or 2 mM H 2 O 2 for 5 min. IP of whole cell lysates with anti-FLAG agarose beads was performed.

Techniques: Binding Assay, Activation Assay, Inhibition, Transfection

$A Chromatin fractionation of WT, PINX1 KO , and PARP1 KO cells was treated with 10 µM etoposide for 30 min and recovered for the indicated time. Soluble and chromatin fractions were subjected to western blot analysis using the indicated antibodies. B Chromatin fractionation of WT_EV (WT), PINX1 KO _EV (PINX1 KO ), and PINX1 KO _PINX1 cells treated with DMSO or 10 µM for 1 h. Whole-cell lysates (WCL) and chromatin fractions were subjected to western blot analysis using the indicated antibodies. The data are representative of two independent experiments. C–F mRNA levels of XRCC1 ( C ), PCNA ( D ), ATM ( E ), and ATR ( F ) in WT_EV, PINX1 KO _EV, and PINX1 KO _PINX1 cells. mRNA expression was measured by qRT-PCR. Error bars show the means ± SDs of samples from at least three replicates, using GAPDH as an endogenous control. G WT_EV, PINX1 KO _EV, and PINX1 KO _PINX1 cells were treated with 10 μM of etoposide for 17 h and lysed for WB analysis. H WT_EV, PINX1 KO _EV, and PINX1 KO _PINX1 cells were treated with 4 mM of hydroxyurea (HU) for 23 h and lysed for WB analysis. Significance was determined by an unpaired t -test. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.$

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: A Chromatin fractionation of WT, PINX1 KO , and PARP1 KO cells was treated with 10 µM etoposide for 30 min and recovered for the indicated time. Soluble and chromatin fractions were subjected to western blot analysis using the indicated antibodies. B Chromatin fractionation of WT_EV (WT), PINX1 KO _EV (PINX1 KO ), and PINX1 KO _PINX1 cells treated with DMSO or 10 µM for 1 h. Whole-cell lysates (WCL) and chromatin fractions were subjected to western blot analysis using the indicated antibodies. The data are representative of two independent experiments. C–F mRNA levels of XRCC1 ( C ), PCNA ( D ), ATM ( E ), and ATR ( F ) in WT_EV, PINX1 KO _EV, and PINX1 KO _PINX1 cells. mRNA expression was measured by qRT-PCR. Error bars show the means ± SDs of samples from at least three replicates, using GAPDH as an endogenous control. G WT_EV, PINX1 KO _EV, and PINX1 KO _PINX1 cells were treated with 10 μM of etoposide for 17 h and lysed for WB analysis. H WT_EV, PINX1 KO _EV, and PINX1 KO _PINX1 cells were treated with 4 mM of hydroxyurea (HU) for 23 h and lysed for WB analysis. Significance was determined by an unpaired t -test. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

Techniques: Fractionation, Western Blot, Expressing, Quantitative RT-PCR, Control

A Volcano plot of differential PARP1 binding peaks between PINX1 KO _EV and WT_EV cells. ChIP-seq was performed using an anti-PARP1 antibody. The differential peaks were determined by more than 2-fold change in read counts and p -value ≤ 0.05. Red dots represent a total of 241 upregulated PARP1 binding peaks (Up: 241), blue dots represent a total of 216 downregulated PARP1 binding peaks (Down: 216), gray dots are nonsignificant peaks (No Significant), and differential PARP1 binding peaks adjacent to genes involved in protein expression regulation were labeled and marked by stars. B Volcano plot of differential PARP1 binding peaks between PINX1 KO _PINX1 and PINX1 KO _EV cells. ChIP-seq was performed using an anti-PARP1 antibody. The differential peaks were determined by more than 2-fold change in read counts and p -value ≤ 0.05. Red dots represent a total of 235 upregulated PARP1 binding peaks (Up: 235), blue dots represent a total of 244 downregulated PARP1 binding peaks (Down: 244), gray dots are nonsignificant peaks (No Significant), and differential PARP1 binding peaks adjacent to genes involved in protein expression regulation were labeled and marked by stars. C mRNA levels of genes with differential PARP1 binding upon PINX1 depletion in WT_EV, PINX1 KO _EV, PINX1 KO _PINX1 cells. mRNA expression was measured by qRT-PCR. Error bars show the means ± SDs of samples from at least three replicates, using GAPDH as an endogenous control. Significance was determined by an unpaired t -test. D GLIS3 supplementation in PINX1 KO cells partially rescued the susceptibility to Talazoparib. PINX1 KO _EV, PINX1 KO _GLIS3, and PINX1 KO _PINX1 are stable cell lines reconstituted with corresponding empty vector (EV), GLIS3, or PINX1 using lentivirus. E HNF4G supplementation in PINX1 KO cells partially rescued the susceptibility to Talazoparib. PINX1 KO _EV, PINX1 KO _HNF4G, and PINX1 KO _PINX1 are stable cell lines reconstituted with corresponding empty vector (EV), HNF4G, or PINX1 using lentivirus. Error bars show the means ± SDs of samples from at least three replicates. Significance was determined by an unpaired t -test. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: A Volcano plot of differential PARP1 binding peaks between PINX1 KO _EV and WT_EV cells. ChIP-seq was performed using an anti-PARP1 antibody. The differential peaks were determined by more than 2-fold change in read counts and p -value ≤ 0.05. Red dots represent a total of 241 upregulated PARP1 binding peaks (Up: 241), blue dots represent a total of 216 downregulated PARP1 binding peaks (Down: 216), gray dots are nonsignificant peaks (No Significant), and differential PARP1 binding peaks adjacent to genes involved in protein expression regulation were labeled and marked by stars. B Volcano plot of differential PARP1 binding peaks between PINX1 KO _PINX1 and PINX1 KO _EV cells. ChIP-seq was performed using an anti-PARP1 antibody. The differential peaks were determined by more than 2-fold change in read counts and p -value ≤ 0.05. Red dots represent a total of 235 upregulated PARP1 binding peaks (Up: 235), blue dots represent a total of 244 downregulated PARP1 binding peaks (Down: 244), gray dots are nonsignificant peaks (No Significant), and differential PARP1 binding peaks adjacent to genes involved in protein expression regulation were labeled and marked by stars. C mRNA levels of genes with differential PARP1 binding upon PINX1 depletion in WT_EV, PINX1 KO _EV, PINX1 KO _PINX1 cells. mRNA expression was measured by qRT-PCR. Error bars show the means ± SDs of samples from at least three replicates, using GAPDH as an endogenous control. Significance was determined by an unpaired t -test. D GLIS3 supplementation in PINX1 KO cells partially rescued the susceptibility to Talazoparib. PINX1 KO _EV, PINX1 KO _GLIS3, and PINX1 KO _PINX1 are stable cell lines reconstituted with corresponding empty vector (EV), GLIS3, or PINX1 using lentivirus. E HNF4G supplementation in PINX1 KO cells partially rescued the susceptibility to Talazoparib. PINX1 KO _EV, PINX1 KO _HNF4G, and PINX1 KO _PINX1 are stable cell lines reconstituted with corresponding empty vector (EV), HNF4G, or PINX1 using lentivirus. Error bars show the means ± SDs of samples from at least three replicates. Significance was determined by an unpaired t -test. ns, p > 0.05; *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

Techniques: Binding Assay, ChIP-sequencing, Expressing, Labeling, Quantitative RT-PCR, Control, Stable Transfection, Plasmid Preparation

PINX1 acts as a multifaceted partner of PARP1 that promotes cellular response to DNA damage and PARP inhibitors. Under normal conditions, PINX1 constitutively binds to PARP1, aiding in chromatin association and transcriptional regulation of PARP1, enhancing the expression of DNA repair genes such as XRCC1 and transcriptional regulatory factors such as GLIS3, ensuring cellular DNA damage repair capacity. At the time of DNA damage, PINX1 is rapidly recruited to the damage sites via PARP1, facilitating the recruitment of early repair factor XRCC1 and downstream DNA repair processes. Both mechanisms contribute to cellular defense against PARP inhibitors.

Journal: Cell Death & Disease

Article Title: PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells

doi: 10.1038/s41419-024-07009-6

Figure Lengend Snippet: PINX1 acts as a multifaceted partner of PARP1 that promotes cellular response to DNA damage and PARP inhibitors. Under normal conditions, PINX1 constitutively binds to PARP1, aiding in chromatin association and transcriptional regulation of PARP1, enhancing the expression of DNA repair genes such as XRCC1 and transcriptional regulatory factors such as GLIS3, ensuring cellular DNA damage repair capacity. At the time of DNA damage, PINX1 is rapidly recruited to the damage sites via PARP1, facilitating the recruitment of early repair factor XRCC1 and downstream DNA repair processes. Both mechanisms contribute to cellular defense against PARP inhibitors.

Techniques: Expressing

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