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( A ) HCT116 SIRT2 WT and KO cells were treated with 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. The image shown is representative of data from 3 separate experiments conducted independently. ( B ) Quantitation of IR-induced phosphorylation of <t>KAP1</t> and CHK2 relative to total KAP1 and CHK2 protein levels. Data are represented as the mean ± SD from 3 independent experiments. ** P < 0.01 and *** P < 0.001, by 2-tail Student’s t test. ( C ) HCT116 SIRT2 KO cells expressing SFB-MRE11 WT, K393Q, and K393R were treated with or without 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. Shown is a representative image of 3 independent experiments. ( D and E ) Quantitation of phosphorylation of KAP1 and CHK2 relative to total KAP1 and CHK2 protein levels. Data are presented as the mean ± SD of 3 independent experiments. Statistical significance was determined using 1-way ANOVA followed by Dunnett’s post hoc test for multiple comparisons. **** P < 0.0001.
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( A ) HCT116 SIRT2 WT and KO cells were treated with 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. The image shown is representative of data from 3 separate experiments conducted independently. ( B ) Quantitation of IR-induced phosphorylation of <t>KAP1</t> and CHK2 relative to total KAP1 and CHK2 protein levels. Data are represented as the mean ± SD from 3 independent experiments. ** P < 0.01 and *** P < 0.001, by 2-tail Student’s t test. ( C ) HCT116 SIRT2 KO cells expressing SFB-MRE11 WT, K393Q, and K393R were treated with or without 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. Shown is a representative image of 3 independent experiments. ( D and E ) Quantitation of phosphorylation of KAP1 and CHK2 relative to total KAP1 and CHK2 protein levels. Data are presented as the mean ± SD of 3 independent experiments. Statistical significance was determined using 1-way ANOVA followed by Dunnett’s post hoc test for multiple comparisons. **** P < 0.0001.
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( A ) HCT116 SIRT2 WT and KO cells were treated with 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. The image shown is representative of data from 3 separate experiments conducted independently. ( B ) Quantitation of IR-induced phosphorylation of <t>KAP1</t> and CHK2 relative to total KAP1 and CHK2 protein levels. Data are represented as the mean ± SD from 3 independent experiments. ** P < 0.01 and *** P < 0.001, by 2-tail Student’s t test. ( C ) HCT116 SIRT2 KO cells expressing SFB-MRE11 WT, K393Q, and K393R were treated with or without 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. Shown is a representative image of 3 independent experiments. ( D and E ) Quantitation of phosphorylation of KAP1 and CHK2 relative to total KAP1 and CHK2 protein levels. Data are presented as the mean ± SD of 3 independent experiments. Statistical significance was determined using 1-way ANOVA followed by Dunnett’s post hoc test for multiple comparisons. **** P < 0.0001.
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Image Search Results


( A ) HCT116 SIRT2 WT and KO cells were treated with 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. The image shown is representative of data from 3 separate experiments conducted independently. ( B ) Quantitation of IR-induced phosphorylation of KAP1 and CHK2 relative to total KAP1 and CHK2 protein levels. Data are represented as the mean ± SD from 3 independent experiments. ** P < 0.01 and *** P < 0.001, by 2-tail Student’s t test. ( C ) HCT116 SIRT2 KO cells expressing SFB-MRE11 WT, K393Q, and K393R were treated with or without 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. Shown is a representative image of 3 independent experiments. ( D and E ) Quantitation of phosphorylation of KAP1 and CHK2 relative to total KAP1 and CHK2 protein levels. Data are presented as the mean ± SD of 3 independent experiments. Statistical significance was determined using 1-way ANOVA followed by Dunnett’s post hoc test for multiple comparisons. **** P < 0.0001.

Journal: The Journal of Clinical Investigation

Article Title: MRE11 deacetylation by SIRT2 promotes DNA binding to facilitate DNA end resection and ATM-dependent signaling

doi: 10.1172/JCI186711

Figure Lengend Snippet: ( A ) HCT116 SIRT2 WT and KO cells were treated with 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. The image shown is representative of data from 3 separate experiments conducted independently. ( B ) Quantitation of IR-induced phosphorylation of KAP1 and CHK2 relative to total KAP1 and CHK2 protein levels. Data are represented as the mean ± SD from 3 independent experiments. ** P < 0.01 and *** P < 0.001, by 2-tail Student’s t test. ( C ) HCT116 SIRT2 KO cells expressing SFB-MRE11 WT, K393Q, and K393R were treated with or without 6 Gy IR, harvested after 4 hours, run on SDS-PAGE, and probed with the indicated antibodies. Shown is a representative image of 3 independent experiments. ( D and E ) Quantitation of phosphorylation of KAP1 and CHK2 relative to total KAP1 and CHK2 protein levels. Data are presented as the mean ± SD of 3 independent experiments. Statistical significance was determined using 1-way ANOVA followed by Dunnett’s post hoc test for multiple comparisons. **** P < 0.0001.

Article Snippet: The antibodies used in this study included SIRT2 (MilliporeSigma, 09-843; Santa Cruz Biotechnology, sc-20966), GAPDH (Santa Cruz, sc-47724), Flag (Santa Cruz Biotechnology, sc-51590), GFP (Abcam, Ab6556), pan acetyl-Lys (Santa Cruz Biotechnology, sc-8649), RPA70 (Cell Signaling Technology, 2267), P-CHK2 T68 (Cell Signaling Technology, 2661S), CHK2 (Santa Cruz Biotechnology, sc-7898), P-KAP1 (Invitrogen, Thermo Fisher Scientific, MA1-2023), and KAP1 (Bethyl Laboratories, A300-767A).

Techniques: SDS Page, Quantitation Assay, Phospho-proteomics, Expressing

(Step 1) DNA damage results in DSBs. (Step 2) SIRT2 deacetylates MRE11 at K393 in response to DNA damage. (Step 3) MRE11 K393 deacetylation by SIRT2 facilitates its recruitment and binding to DNA at DSBs. (Step 4) MRE11-RAD50-NBS1 assembles and promotes DNA end resection and ATM-dependent phosphorylation of downstream substrates, including CHK2 and KAP1.

Journal: The Journal of Clinical Investigation

Article Title: MRE11 deacetylation by SIRT2 promotes DNA binding to facilitate DNA end resection and ATM-dependent signaling

doi: 10.1172/JCI186711

Figure Lengend Snippet: (Step 1) DNA damage results in DSBs. (Step 2) SIRT2 deacetylates MRE11 at K393 in response to DNA damage. (Step 3) MRE11 K393 deacetylation by SIRT2 facilitates its recruitment and binding to DNA at DSBs. (Step 4) MRE11-RAD50-NBS1 assembles and promotes DNA end resection and ATM-dependent phosphorylation of downstream substrates, including CHK2 and KAP1.

Article Snippet: The antibodies used in this study included SIRT2 (MilliporeSigma, 09-843; Santa Cruz Biotechnology, sc-20966), GAPDH (Santa Cruz, sc-47724), Flag (Santa Cruz Biotechnology, sc-51590), GFP (Abcam, Ab6556), pan acetyl-Lys (Santa Cruz Biotechnology, sc-8649), RPA70 (Cell Signaling Technology, 2267), P-CHK2 T68 (Cell Signaling Technology, 2661S), CHK2 (Santa Cruz Biotechnology, sc-7898), P-KAP1 (Invitrogen, Thermo Fisher Scientific, MA1-2023), and KAP1 (Bethyl Laboratories, A300-767A).

Techniques: Binding Assay, Phospho-proteomics