Literature DB >> 30789755

Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.

Dilson E Rassier1, Anna Kashina2.   

Abstract

The cytoskeleton drives many essential processes in normal physiology, and its impairments underlie many diseases, including skeletal myopathies, cancer, and heart failure, that broadly affect developed countries worldwide. Cytoskeleton regulation is a field of investigation of rapidly emerging global importance and a new venue for the development of potential therapies. This review overviews our present understanding of the posttranslational regulation of the muscle cytoskeleton through arginylation, a tRNA-dependent addition of arginine to proteins mediated by arginyltransferase 1. We focus largely on arginylation-dependent regulation of striated muscles, shown to play critical roles in facilitating muscle integrity, contractility, regulation, and strength.

Entities:  

Keywords:  actin; arginylation; muscle; myosin; posttranslational modification

Mesh:

Substances:

Year:  2019        PMID: 30789755      PMCID: PMC6580163          DOI: 10.1152/ajpcell.00500.2018

Source DB:  PubMed          Journal:  Am J Physiol Cell Physiol        ISSN: 0363-6143            Impact factor:   4.249


  61 in total

1.  An essential role of N-terminal arginylation in cardiovascular development.

Authors:  Yong Tae Kwon; Anna S Kashina; Ilia V Davydov; Rong-Gui Hu; Jee Young An; Jai Wha Seo; Fangyong Du; Alexander Varshavsky
Journal:  Science       Date:  2002-07-05       Impact factor: 47.728

2.  A SOLUBLE AMINO ACID-INCORPORATING SYSTEM FROM RAT LIVER.

Authors:  H KAJI; G D NOVELLI; A KAJI
Journal:  Biochim Biophys Acta       Date:  1963-11-22

3.  Forces measured with micro-fabricated cantilevers during actomyosin interactions produced by filaments containing different myosin isoforms and loop 1 structures.

Authors:  Albert Kalganov; Nabil Shalabi; Nedjma Zitouni; Linda Hussein Kachmar; Anne-Marie Lauzon; Dilson E Rassier
Journal:  Biochim Biophys Acta       Date:  2012-12-07

Review 4.  Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle.

Authors:  Anna Kashina
Journal:  Anat Rec (Hoboken)       Date:  2014-09       Impact factor: 2.064

Review 5.  Posttranslational Arginylation Regulates Striated Muscle Function.

Authors:  Felipe de Souza Leite; Anna Kashina; Dilson E Rassier
Journal:  Exerc Sport Sci Rev       Date:  2016-07       Impact factor: 6.230

6.  Mechanism of adenosine triphosphate hydrolysis by actomyosin.

Authors:  R W Lymn; E W Taylor
Journal:  Biochemistry       Date:  1971-12-07       Impact factor: 3.162

7.  RGS4 and RGS5 are in vivo substrates of the N-end rule pathway.

Authors:  Min Jae Lee; Takafumi Tasaki; Kayoko Moroi; Jee Young An; Sadao Kimura; Ilia V Davydov; Yong Tae Kwon
Journal:  Proc Natl Acad Sci U S A       Date:  2005-10-10       Impact factor: 11.205

8.  Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo.

Authors:  Junling Wang; Xuemei Han; Catherine C L Wong; Hong Cheng; Aaron Aslanian; Tao Xu; Paul Leavis; Heinrich Roder; Lizbeth Hedstrom; John R Yates; Anna Kashina
Journal:  Chem Biol       Date:  2014-02-13

9.  Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner.

Authors:  Brian Leei Lin; Amy Li; Ji Young Mun; Michael J Previs; Samantha Beck Previs; Stuart G Campbell; Cristobal G Dos Remedios; Pieter de P Tombe; Roger Craig; David M Warshaw; Sakthivel Sadayappan
Journal:  Sci Rep       Date:  2018-02-08       Impact factor: 4.379

10.  Target site specificity and in vivo complexity of the mammalian arginylome.

Authors:  Junling Wang; Vikas Rao Pejaver; Geoffrey P Dann; Max Y Wolf; Manolis Kellis; Yun Huang; Benjamin A Garcia; Predrag Radivojac; Anna Kashina
Journal:  Sci Rep       Date:  2018-11-01       Impact factor: 4.379

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