SH3 domain tyrosine phosphorylation--sites, role and evolution.

<h4>Background</h4>SH3 domains are eukaryotic protein domains that participate in a plethora of cellular processes including signal transduction, proliferation, and cellular movement. Several studies indicate that tyrosine phosphorylation could play a significant role in the regulation o...

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Autores principales:	Zuzana Tatárová, Jan Brábek, Daniel Rösel, Marian Novotný
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0cf5dc0aaebf403388325754391f61b9
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spelling	oai:doaj.org-article:0cf5dc0aaebf403388325754391f61b92021-11-18T07:18:46ZSH3 domain tyrosine phosphorylation--sites, role and evolution.1932-620310.1371/journal.pone.0036310https://doaj.org/article/0cf5dc0aaebf403388325754391f61b92012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22615764/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>SH3 domains are eukaryotic protein domains that participate in a plethora of cellular processes including signal transduction, proliferation, and cellular movement. Several studies indicate that tyrosine phosphorylation could play a significant role in the regulation of SH3 domains.<h4>Results</h4>To explore the incidence of the tyrosine phosphorylation within SH3 domains we queried the PhosphoSite Plus database of phosphorylation sites. Over 100 tyrosine phosphorylations occurring on 20 different SH3 domain positions were identified. The tyrosine corresponding to c-Src Tyr-90 was by far the most frequently identified SH3 domain phosphorylation site. A comparison of sequences around this tyrosine led to delineation of a preferred sequence motif ALYD(Y/F). This motif is present in about 15% of human SH3 domains and is structurally well conserved. We further observed that tyrosine phosphorylation is more abundant than serine or threonine phosphorylation within SH3 domains and other adaptor domains, such as SH2 or WW domains. Tyrosine phosphorylation could represent an important regulatory mechanism of adaptor domains.<h4>Conclusions</h4>While tyrosine phosphorylation typically promotes signaling protein interactions via SH2 or PTB domains, its role in SH3 domains is the opposite - it blocks or prevents interactions. The regulatory function of tyrosine phosphorylation is most likely achieved by the phosphate moiety and its charge interfering with binding of polyproline helices of SH3 domain interacting partners.Zuzana TatárováJan BrábekDaniel RöselMarian NovotnýPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 5, p e36310 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Zuzana Tatárová Jan Brábek Daniel Rösel Marian Novotný SH3 domain tyrosine phosphorylation--sites, role and evolution.
description	<h4>Background</h4>SH3 domains are eukaryotic protein domains that participate in a plethora of cellular processes including signal transduction, proliferation, and cellular movement. Several studies indicate that tyrosine phosphorylation could play a significant role in the regulation of SH3 domains.<h4>Results</h4>To explore the incidence of the tyrosine phosphorylation within SH3 domains we queried the PhosphoSite Plus database of phosphorylation sites. Over 100 tyrosine phosphorylations occurring on 20 different SH3 domain positions were identified. The tyrosine corresponding to c-Src Tyr-90 was by far the most frequently identified SH3 domain phosphorylation site. A comparison of sequences around this tyrosine led to delineation of a preferred sequence motif ALYD(Y/F). This motif is present in about 15% of human SH3 domains and is structurally well conserved. We further observed that tyrosine phosphorylation is more abundant than serine or threonine phosphorylation within SH3 domains and other adaptor domains, such as SH2 or WW domains. Tyrosine phosphorylation could represent an important regulatory mechanism of adaptor domains.<h4>Conclusions</h4>While tyrosine phosphorylation typically promotes signaling protein interactions via SH2 or PTB domains, its role in SH3 domains is the opposite - it blocks or prevents interactions. The regulatory function of tyrosine phosphorylation is most likely achieved by the phosphate moiety and its charge interfering with binding of polyproline helices of SH3 domain interacting partners.
format	article
author	Zuzana Tatárová Jan Brábek Daniel Rösel Marian Novotný
author_facet	Zuzana Tatárová Jan Brábek Daniel Rösel Marian Novotný
author_sort	Zuzana Tatárová
title	SH3 domain tyrosine phosphorylation--sites, role and evolution.
title_short	SH3 domain tyrosine phosphorylation--sites, role and evolution.
title_full	SH3 domain tyrosine phosphorylation--sites, role and evolution.
title_fullStr	SH3 domain tyrosine phosphorylation--sites, role and evolution.
title_full_unstemmed	SH3 domain tyrosine phosphorylation--sites, role and evolution.
title_sort	sh3 domain tyrosine phosphorylation--sites, role and evolution.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/0cf5dc0aaebf403388325754391f61b9
work_keys_str_mv	AT zuzanatatarova sh3domaintyrosinephosphorylationsitesroleandevolution AT janbrabek sh3domaintyrosinephosphorylationsitesroleandevolution AT danielrosel sh3domaintyrosinephosphorylationsitesroleandevolution AT mariannovotny sh3domaintyrosinephosphorylationsitesroleandevolution
_version_	1718423643377106944

SH3 domain tyrosine phosphorylation--sites, role and evolution.

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