Specificity of reversible ADP-ribosylation and regulation of cellular processes

被引:77
作者
Crawford, Kerryanne [1 ]
Bonfiglio, Juan Jose [2 ]
Mikoc, Andreja [3 ]
Matic, Ivan [2 ]
Ahel, Ivan [1 ]
机构
[1] Univ Oxford, Sir William Dunn Sch Pathol, South Parks Rd, Oxford OX1 3RE, England
[2] Max Planck Inst Biol Ageing, Cologne, Germany
[3] Rudjer Boskovic Inst, Div Mol Biol, Zagreb, Croatia
基金
英国惠康基金; 欧盟地平线“2020”;
关键词
PARP; ADP-ribosyl transferase; ADP-ribosylation; reversible protein modification; macrodomain; PARG; ARH3; DNA damage; 39-KDA POLY(ADP-RIBOSE) GLYCOHYDROLASE; APOPTOSIS-INDUCING PROTEIN; HUMAN NEUTROPHIL PEPTIDE-1; FINGER ANTIVIRAL PROTEIN; RIBOSE ACCEPTOR SITES; DNA-DAMAGE; STRUCTURAL BASIS; OXIDATIVE STRESS; TRANSFER-RNA; RIBOSYLTRANSFERASE ART2.2;
D O I
10.1080/10409238.2017.1394265
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Proper and timely regulation of cellular processes is fundamental to the overall health and viability of organisms across all kingdoms of life. Thus, organisms have evolved multiple highly dynamic and complex biochemical signaling cascades in order to adapt and survive diverse challenges. One such method of conferring rapid adaptation is the addition or removal of reversible modifications of different chemical groups onto macromolecules which in turn induce the appropriate downstream outcome. ADP-ribosylation, the addition of ADP-ribose (ADPr) groups, represents one of these highly conserved signaling chemicals. Herein we outline the writers, erasers and readers of ADP-ribosylation and dip into the multitude of cellular processes they have been implicated in. We also review what we currently know on how specificity of activity is ensured for this important modification.
引用
收藏
页码:64 / 82
页数:19
相关论文
共 226 条
[11]   Structure of the sirtuin-linked macrodomain SAV0325 from Staphylococcus aureus [J].
Appel, C. Denise ;
Feld, Geoffrey K. ;
Wallace, Bret D. ;
Williams, R. Scott .
PROTEIN SCIENCE, 2016, 25 (09) :1682-1691
[12]   The Natural History of ADP-Ribosyltransferases and the ADP-Ribosylation System [J].
Aravind, L. ;
Zhang, Dapeng ;
de Souza, Robson F. ;
Anand, Swadha ;
Iyer, Lakshminarayan M. .
ENDOGENOUS ADP-RIBOSYLATION, 2015, 384 :3-32
[13]   Interferon-Stimulated Poly(ADP-Ribose) Polymerases Are Potent Inhibitors of Cellular Translation and Virus Replication [J].
Atasheva, Svetlana ;
Frolova, Elena I. ;
Frolov, Ilya .
JOURNAL OF VIROLOGY, 2014, 88 (04) :2116-2130
[14]   Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis [J].
Bae, JY ;
Donigian, JR ;
Hsueh, AJW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (07) :5195-5204
[15]   Activity and specificity of toxin-related mouse T cell ecto-ADP-ribosyltransferase ART2.2 depends on its association with lipid rafts [J].
Bannas, P ;
Adriouch, S ;
Kahl, S ;
Braasch, F ;
Haag, F ;
Koch-Nolte, F .
BLOOD, 2005, 105 (09) :3663-3670
[16]   Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation [J].
Barkauskaite, Eva ;
Jankevicius, Gytis ;
Ahel, Ivan .
MOLECULAR CELL, 2015, 58 (06) :935-946
[17]   Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities [J].
Barkauskaite, Eva ;
Brassington, Amy ;
Tan, Edwin S. ;
Warwicker, Jim ;
Dunstan, Mark S. ;
Banos, Benito ;
Lafite, Pierre ;
Ahel, Marijan ;
Mitchison, Timothy J. ;
Ahel, Ivan ;
Leys, David .
NATURE COMMUNICATIONS, 2013, 4
[18]  
Berger N A, 1983, Princess Takamatsu Symp, V13, P219
[19]   The Substrate Specificity of Sirtuins [J].
Bheda, Poonam ;
Jing, Hui ;
Wolberger, Cynthia ;
Lin, Hening .
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85, 2016, 85 :405-429
[20]   New Quantitative Mass Spectrometry Approaches Reveal Different ADP-ribosylation Phases Dependent On the Levels of Oxidative Stress [J].
Bilan, Vera ;
Selevsek, Nathalie ;
Kistemaker, Hans A. V. ;
Abplanalp, Jeannette ;
Feurer, Roxane ;
Filippov, Dmitri V. ;
Hottiger, Michael O. .
MOLECULAR & CELLULAR PROTEOMICS, 2017, 16 (05) :949-958