Literature DB >> 25747399

Nuclear ADP-Ribosylation and Its Role in Chromatin Plasticity, Cell Differentiation, and Epigenetics.

Michael O Hottiger1.   

Abstract

Protein ADP-ribosylation is an ancient posttranslational modification with high biochemical complexity. It alters the function of modified proteins or provides a scaffold for the recruitment of other proteins and thus regulates several cellular processes. ADP-ribosylation is governed by ADP-ribosyltransferases and a subclass of sirtuins (writers), is sensed by proteins that contain binding modules (readers) that recognize specific parts of the ADP-ribosyl posttranslational modification, and is removed by ADP-ribosylhydrolases (erasers). The large amount of experimental data generated and technical progress made in the last decade have significantly advanced our knowledge of the function of ADP-ribosylation at the molecular level. This review summarizes the current knowledge of nuclear ADP-ribosylation reactions and their role in chromatin plasticity, cell differentiation, and epigenetics and discusses current progress and future perspectives.

Entities:  

Keywords:  ADP-ribosylation; ARTD; NAD; PAR; PARP; chromatin; histone

Mesh:

Substances:

Year:  2015        PMID: 25747399     DOI: 10.1146/annurev-biochem-060614-034506

Source DB:  PubMed          Journal:  Annu Rev Biochem        ISSN: 0066-4154            Impact factor:   23.643


  97 in total

1.  Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.

Authors:  Deena M Leslie Pedrioli; Mario Leutert; Vera Bilan; Kathrin Nowak; Kapila Gunasekera; Elena Ferrari; Ralph Imhof; Lars Malmström; Michael O Hottiger
Journal:  EMBO Rep       Date:  2018-06-28       Impact factor: 8.807

2.  Catalytic-Independent Functions of PARP-1 Determine Sox2 Pioneer Activity at Intractable Genomic Loci.

Authors:  Ziying Liu; W Lee Kraus
Journal:  Mol Cell       Date:  2017-02-16       Impact factor: 17.970

3.  ELTA: Enzymatic Labeling of Terminal ADP-Ribose.

Authors:  Yoshinari Ando; Elad Elkayam; Robert Lyle McPherson; Morgan Dasovich; Shang-Jung Cheng; Jim Voorneveld; Dmitri V Filippov; Shao-En Ong; Leemor Joshua-Tor; Anthony K L Leung
Journal:  Mol Cell       Date:  2019-01-31       Impact factor: 17.970

Review 4.  Insight into the machinery that oils chromatin dynamics.

Authors:  Roni H G Wright; Narcis Fernandez-Fuentes; Baldomero Oliva; Miguel Beato
Journal:  Nucleus       Date:  2016-11-28       Impact factor: 4.197

5.  Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9.

Authors:  Chun-Song Yang; Kasey Jividen; Adam Spencer; Natalia Dworak; Li Ni; Luke T Oostdyk; Mandovi Chatterjee; Beata Kuśmider; Brian Reon; Mahmut Parlak; Vera Gorbunova; Tarek Abbas; Erin Jeffery; Nicholas E Sherman; Bryce M Paschal
Journal:  Mol Cell       Date:  2017-05-18       Impact factor: 17.970

Review 6.  Approaches for the study of epigenetic modifications in the inner ear and related tissues.

Authors:  Bradley J Walters; Brandon C Cox
Journal:  Hear Res       Date:  2019-01-12       Impact factor: 3.208

7.  Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1.

Authors:  Konstantin N Naumenko; Mariya V Sukhanova; Loic Hamon; Tatyana A Kurgina; Elizaveta E Alemasova; Mikhail M Kutuzov; David Pastré; Olga I Lavrik
Journal:  Biomolecules       Date:  2020-09-16

8.  Label-Free Quantitative Proteomic Reveals Differentially Expressed Proteins in Aeromonas-Immunostimulated Leukocytes of Lampetra japonica.

Authors:  Yingying Li; Wenying Zhang; Yu Zuo; Ting Zhu; Yue Pang; Tiesong Li; Qingwei Li
Journal:  Curr Microbiol       Date:  2018-03-14       Impact factor: 2.188

9.  Analyzing structure-function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLa PARP1 knock-out cells.

Authors:  Lisa Rank; Sebastian Veith; Eva C Gwosch; Janine Demgenski; Magdalena Ganz; Marjolijn C Jongmans; Christopher Vogel; Arthur Fischbach; Stefanie Buerger; Jan M F Fischer; Tabea Zubel; Anna Stier; Christina Renner; Michael Schmalz; Sascha Beneke; Marcus Groettrup; Roland P Kuiper; Alexander Bürkle; Elisa Ferrando-May; Aswin Mangerich
Journal:  Nucleic Acids Res       Date:  2016-09-29       Impact factor: 16.971

10.  AI26 inhibits the ADP-ribosylhydrolase ARH3 and suppresses DNA damage repair.

Authors:  Xiuhua Liu; Rong Xie; Lily L Yu; Shih-Hsun Chen; Xiaoyun Yang; Anup K Singh; Hongzhi Li; Chen Wu; Xiaochun Yu
Journal:  J Biol Chem       Date:  2020-08-04       Impact factor: 5.157

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