期刊
MOLECULAR ASPECTS OF MEDICINE
卷 34, 期 6, 页码 1066-1087出版社
ELSEVIER
DOI: 10.1016/j.mam.2012.12.005
关键词
PARP; PARG; Poly(ADP-ribose); WWE; PBZ; Macro domain
资金
- Canadian Institutes of Health Research
- NIH/NINDS [NS067525]
- NIDA [DA000266]
- FQRNT
Poly(ADP-ribosyl)ation is a posttranslational modification catalyzed by the poly(ADPribose) polymerases (PARPs). These enzymes covalently modify glutamic, aspartic and lysine amino acid side chains of acceptor proteins by the sequential addition of ADP-ribose (ADPr) units. The poly(ADP-ribose) (pADPr) polymers formed alter the physico-chemical characteristics of the substrate with functional consequences on its biological activities. Recently, non-covalent binding to pADPr has emerged as a key mechanism to modulate and coordinate several intracellular pathways including the DNA damage response, protein stability and cell death. In this review, we describe the basis of non-covalent binding to pADPr that has led to the emerging concept of pADPr-responsive signaling pathways. This review emphasizes the structural elements and the modular strategies developed by pADPr-binding proteins to exert a fine-tuned control of a variety of pathways. Poly(ADP-ribosyl)ation reactions are highly regulated processes, both spatially and temporally, for which at least four specialized pADPr-binding modules accommodate different pADPr structures and reprogram protein functions. In this review, we highlight the role of well-characterized and newly discovered pADPr-binding modules in a diverse set of physiological functions. (C) 2013 Elsevier Ltd. All rights reserved.
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