Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.

SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and m...

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Autores principales:	Jose L Ortega Roldan, Salvador Casares, Malene Ringkjøbing Jensen, Nayra Cárdenes, Jerónimo Bravo, Martin Blackledge, Ana I Azuaga, Nico A J van Nuland
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f0dfce6381094a71b4f4d8cd64cd8eef
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spelling	oai:doaj.org-article:f0dfce6381094a71b4f4d8cd64cd8eef2021-11-18T08:55:50ZDistinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.1932-620310.1371/journal.pone.0073018https://doaj.org/article/f0dfce6381094a71b4f4d8cd64cd8eef2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039852/?tool=EBIhttps://doaj.org/toc/1932-6203SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and mutational analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C domain does not abrogate ubiquitin binding, in contrast to previous hypothesis and our findings for the first two CD2AP SH3 domains. The similar alternative binding mode of the SH3-C domains of these related adaptor proteins is characterised by a higher affinity to C-terminal extended ubiquitin molecules. We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes a new ubiquitin-binding mode involved in a different cellular function and thus changes the previously established mechanism of EGF-dependent CD2AP/CIN85 mono-ubiquitination.Jose L Ortega RoldanSalvador CasaresMalene Ringkjøbing JensenNayra CárdenesJerónimo BravoMartin BlackledgeAna I AzuagaNico A J van NulandPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e73018 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jose L Ortega Roldan Salvador Casares Malene Ringkjøbing Jensen Nayra Cárdenes Jerónimo Bravo Martin Blackledge Ana I Azuaga Nico A J van Nuland Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.
description	SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and mutational analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C domain does not abrogate ubiquitin binding, in contrast to previous hypothesis and our findings for the first two CD2AP SH3 domains. The similar alternative binding mode of the SH3-C domains of these related adaptor proteins is characterised by a higher affinity to C-terminal extended ubiquitin molecules. We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes a new ubiquitin-binding mode involved in a different cellular function and thus changes the previously established mechanism of EGF-dependent CD2AP/CIN85 mono-ubiquitination.
format	article
author	Jose L Ortega Roldan Salvador Casares Malene Ringkjøbing Jensen Nayra Cárdenes Jerónimo Bravo Martin Blackledge Ana I Azuaga Nico A J van Nuland
author_facet	Jose L Ortega Roldan Salvador Casares Malene Ringkjøbing Jensen Nayra Cárdenes Jerónimo Bravo Martin Blackledge Ana I Azuaga Nico A J van Nuland
author_sort	Jose L Ortega Roldan
title	Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.
title_short	Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.
title_full	Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.
title_fullStr	Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.
title_full_unstemmed	Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.
title_sort	distinct ubiquitin binding modes exhibited by sh3 domains: molecular determinants and functional implications.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/f0dfce6381094a71b4f4d8cd64cd8eef
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Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.

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