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• W2511341418 endingPage "e0157860" @default.
• W2511341418 startingPage "e0157860" @default.
• W2511341418 abstract "The NEIL1 DNA glycosylase is one of eleven mammalian DNA glycosylases that partake in the first step of the base excision repair (BER) pathway. NEIL1 recognizes and cleaves mainly oxidized pyrimidines from DNA. The past decade has witnessed the identification of an increasing number of post-translational modifications (PTMs) in BER enzymes including phosphorylation, acetylation, and sumoylation, which modulate enzyme function. In this work, we performed the first comprehensive analysis of phosphorylation sites in human NEIL1 expressed in human cells. Mass spectrometry (MS) analysis revealed phosphorylation at three serine residues: S207, S306, and a third novel site, S61. We expressed, purified, and characterized phosphomimetic (glutamate) and phosphoablating (alanine) mutants of the three phosphorylation sites in NEIL1 revealed by the MS analysis. All mutant enzymes were active and bound tightly to DNA, indicating that phosphorylation does not affect DNA binding and enzyme activity at these three serine sites. We also characterized phosphomimetic mutants of two other sites of phosphorylation, Y263 and S269, reported previously, and observed that mutation of Y263 to E yielded a completely inactive enzyme. Furthermore, based on sequence motifs and kinase prediction algorithms, we identified the c-Jun N-terminal kinase 1 (JNK1) as the kinase involved in the phosphorylation of NEIL1. JNK1, a member of the mitogen activated protein kinase (MAPK) family, was detected in NEIL1 immunoprecipitates, interacted with NEIL1 in vitro, and was able to phosphorylate the enzyme at residues S207, S306, and S61." @default.
• W2511341418 created "2016-09-16" @default.
• W2511341418 creator A5001458814 @default.
• W2511341418 creator A5088798352 @default.
• W2511341418 creator A5090439392 @default.
• W2511341418 date "2016-08-12" @default.
• W2511341418 modified "2023-09-24" @default.
• W2511341418 title "Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase" @default.
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• W2511341418 doi "https://doi.org/10.1371/journal.pone.0157860" @default.
• W2511341418 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4982613" @default.
• W2511341418 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27518429" @default.
• W2511341418 hasPublicationYear "2016" @default.
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