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• W2012362589 abstract "The DNA damage response likely includes a global phosphorylation signaling cascade process for sensing the damaged DNA condition and coordinating responses to cope with and repair the perturbed cellular state. We utilized a label-free liquid chromatography-mass spectrometry approach to evaluate changes in protein phosphorylation associated with PP5 activity during the DNA damage response. Biological replicate analyses of bleomycin-treated HeLa cells expressing either WT-PP5 or mutant inactive PP5 lead to the identification of six potential target proteins of PP5 action. Four of these putative targets have been previously reported to be involved in DNA damage responses. Using phospho-site specific antibodies, we confirmed that phosphorylation of one target, ribosomal protein S6, was selectively decreased in cells overexpressing catalytically inactive PP5. Our findings also suggest that PP5 may play a role in controlling translation and in regulating substrates for proline-directed kinases, such as MAP kinases and cyclin-dependent protein kinases that are involved in response to DNA damage." @default.
• W2012362589 created "2016-06-24" @default.
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• W2012362589 date "2009-12-29" @default.
• W2012362589 modified "2023-10-14" @default.
• W2012362589 title "Novel Ser/Thr Protein Phosphatase 5 (PP5) Regulated Targets during DNA Damage Identified by Proteomics Analysis" @default.
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• W2012362589 doi "https://doi.org/10.1021/pr9008207" @default.
• W2012362589 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2818885" @default.
• W2012362589 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20039704" @default.
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