Literature DB >> 21784066

Posttranslational arginylation as a global biological regulator.

Sougata Saha1, Anna Kashina.   

Abstract

Posttranslational modifications constitute a major field of emerging biological significance as mounting evidence demonstrates their key role in multiple physiological processes. Following in the footsteps of protein phosphorylation studies, new modifications are being shown to regulate protein properties and functions in vivo. Among such modifications, an important role belongs to protein arginylation - posttranslational tRNA-mediated addition of arginine, to proteins by arginyltransferase, ATE1. Recent studies show that arginylation is essential for embryogenesis in many organisms and that it regulates such important processes as heart development, angiogenesis, and tissue morphogenesis in mammals. This review summarizes the key data in the protein arginylation field since its original discovery to date.
Copyright © 2011 Elsevier Inc. All rights reserved.

Entities:  

Mesh:

Substances:

Year:  2011        PMID: 21784066      PMCID: PMC3171647          DOI: 10.1016/j.ydbio.2011.06.043

Source DB:  PubMed          Journal:  Dev Biol        ISSN: 0012-1606            Impact factor:   3.582


  97 in total

1.  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

2.  The posttranslational arginylation of proteins in different regions of the rat brain.

Authors:  M E Hallak; G Bongiovanni; H S Barra
Journal:  J Neurochem       Date:  1991-11       Impact factor: 5.372

3.  Evidence that oxidized proteins are substrates for N-terminal arginylation.

Authors:  N Zhang; R Donnelly; N A Ingoglia
Journal:  Neurochem Res       Date:  1998-11       Impact factor: 3.996

4.  Non-rebosomal incorporation of arginine into a specific protein by a cell-free extract of parathyroid tissue.

Authors:  B Kemper; J F Habener
Journal:  Biochim Biophys Acta       Date:  1974-05-17

5.  Further studies on the soluble amino acid incorporating system from rat liver.

Authors:  H Kaji
Journal:  Biochemistry       Date:  1968-11       Impact factor: 3.162

6.  Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm.

Authors:  R L Soffer; H Horinishi
Journal:  J Mol Biol       Date:  1969-07-14       Impact factor: 5.469

7.  Complete purification of arginyl-tRNA:protein arginyltransferase from hog kidney and production of its antibody.

Authors:  M Kato; Y Nozawa
Journal:  Anal Biochem       Date:  1984-12       Impact factor: 3.365

8.  Universality and structure of the N-end rule.

Authors:  D K Gonda; A Bachmair; I Wünning; J W Tobias; W S Lane; A Varshavsky
Journal:  J Biol Chem       Date:  1989-10-05       Impact factor: 5.157

9.  Inactivation of arginyl-tRNA protein transferase by a bifunctional arsenoxide: identification of residues proximal to the arsenoxide site.

Authors:  J Li; C M Pickart
Journal:  Biochemistry       Date:  1995-01-10       Impact factor: 3.162

10.  Conditional Tek promoter-driven deletion of arginyltransferase in the germ line causes defects in gametogenesis and early embryonic lethality in mice.

Authors:  Nicolae Adrian Leu; Satoshi Kurosaka; Anna Kashina
Journal:  PLoS One       Date:  2009-11-05       Impact factor: 3.240

View more
  36 in total

1.  Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats.

Authors:  Christopher S Brower; Connor E Rosen; Richard H Jones; Brandon C Wadas; Konstantin I Piatkov; Alexander Varshavsky
Journal:  Proc Natl Acad Sci U S A       Date:  2014-11-04       Impact factor: 11.205

Review 2.  A finer tuning of G-protein signaling through regulated control of RGS proteins.

Authors:  Jacob Kach; Nan Sethakorn; Nickolai O Dulin
Journal:  Am J Physiol Heart Circ Physiol       Date:  2012-04-27       Impact factor: 4.733

3.  tRNAArg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.

Authors:  Irem Avcilar-Kucukgoze; Howard Gamper; Christine Polte; Zoya Ignatova; Ralph Kraetzner; Michael Shtutman; Ya-Ming Hou; Dawei W Dong; Anna Kashina
Journal:  Cell Chem Biol       Date:  2020-06-16       Impact factor: 8.116

4.  Nanotechnology-mediated crossing of two impermeable membranes to modulate the stars of the neurovascular unit for neuroprotection.

Authors:  Bapurao Surnar; Uttara Basu; Bhabatosh Banik; Anis Ahmad; Brian Marples; Nagesh Kolishetti; Shanta Dhar
Journal:  Proc Natl Acad Sci U S A       Date:  2018-12-10       Impact factor: 11.205

Review 5.  Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.

Authors:  Dilson E Rassier; Anna Kashina
Journal:  Am J Physiol Cell Physiol       Date:  2019-02-21       Impact factor: 4.249

Review 6.  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

7.  Post-translational arginylation as a novel regulator of platelet function.

Authors:  Markus Bender; Hervé Falet
Journal:  Haematologica       Date:  2014-03       Impact factor: 9.941

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.  Disruption of the ATE1 and SLC12A1 Genes by Balanced Translocation in a Boy with Non-Syndromic Hearing Loss.

Authors:  B Vona; C Neuner; N El Hajj; E Schneider; R Farcas; V Beyer; U Zechner; A Keilmann; M Poot; O Bartsch; I Nanda; T Haaf
Journal:  Mol Syndromol       Date:  2013-10-04

10.  Loss of ATE1-mediated arginylation leads to impaired platelet myosin phosphorylation, clot retraction, and in vivo thrombosis formation.

Authors:  Lurong Lian; Aae Suzuki; Vincent Hayes; Sougata Saha; Xuemei Han; Tao Xu; John R Yates; Mortimer Poncz; Anna Kashina; Charles S Abrams
Journal:  Haematologica       Date:  2013-11-29       Impact factor: 9.941

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.