Identification and functional characterizations of N-Terminal α-N-Methylation and Phosphorylation of Serine 461 in human Poly(ADP-ribose) Polymerase 3

Dai, Xiaoxia, Rulten, Stuart L, You, Changjun, Caldecott, Keith W and Wang, Yinsheng (2015) Identification and functional characterizations of N-Terminal α-N-Methylation and Phosphorylation of Serine 461 in human Poly(ADP-ribose) Polymerase 3. Journal of proteome research, 14 (6). pp. 2575-2582. ISSN 1535-3907

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Abstract

Poly(ADP-ribose) polymerase 3 (PARP3) is a member of the PARP family enzymes which catalyze the ADP-ribosylation of proteins. PARP3 plays an important role in DNA damage repair and mitotic progression. In this study, we identified, using mass spectrometric techniques, two novel post-translational modification sites in PARP3, α-N-methylation and phosphorylation of serine 461 (S461). We found that the N-terminal α-amino group of PARP3 is heavily methylated in human cells, and N-terminal RCC1 methyltransferase (NRMT) is a key enzyme required for this methylation. We also observed that the phosphorylation level of S461 in PARP3 could be reduced in human cells upon treatment with flavopiridol, a cyclin-dependent kinase inhibitor. Moreover, we demonstrated that S461 phosphorylation, but not α-N-methylation of PARP3, may be involved in the cellular response toward DNA double-strand breaks. These findings provide novel insights into the post-translational regulation of PARP3.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Subjects: Q Science > QP Physiology
Related URLs:
Depositing User: Stuart Rulten
Date Deposited: 18 Sep 2015 12:00
Last Modified: 05 Aug 2016 06:49
URI: http://srodev.sussex.ac.uk/id/eprint/56816
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Project NameSussex Project NumberFunderFunder Ref
Non-homologous End-Joining Protein Complexes and Genome StabilityG1305CANCER RESEARCH UKC6563/A16771