Literature DB >> 20387642

[Tyrosine nitration as regulatory post-translational modification of proteins].

Ia B Blium, Iu A Krasylenko, A I Iemets'.   

Abstract

Review highlights new pathways of signal transduction from nitric oxide (NO) that is a recognized secondary messenger in regulatory cascades of phylogenetically distant species. Indirect (via Ca2+ and cGMP) and direct (protein S-nitrosylation and tyrosine nitration) pathways of NO signal transduction are presented. S-nitrosyation as new paradigm in signal transduction and protein functions regulations is discussed. The importance of animal and plant protein tyrosine nitration in vivo and the potential regulatory significance of this posttranslational modification are emphasized. Also review describes tree mechanisms of protein tyrosine nitration: via peroxynitrite, peroxydase and haem-peroxidase. Particular attention is paid to cytoskeleton proteins tyrosine nitration, particularly tubulines, because microtubules are involved into modulation of signal transduction from various messengers.

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Year:  2009        PMID: 20387642

Source DB:  PubMed          Journal:  Ukr Biokhim Zh (1999)


  2 in total

1.  Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease.

Authors:  Tejaswita M Karve; Amrita K Cheema
Journal:  J Amino Acids       Date:  2011-07-21

2.  Tubulin tyrosine nitration regulates microtubule organization in plant cells.

Authors:  Yaroslav B Blume; Yuliya A Krasylenko; Oleh M Demchuk; Alla I Yemets
Journal:  Front Plant Sci       Date:  2013-12-26       Impact factor: 5.753

  2 in total

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