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Title

Distinct Ubiquitin Binding Modes Exhibited by SH3 Domains: Molecular Determinants and Functional Implications

AuthorsOrtega Roldan, Jose L.; Casares, Salvador; Jensen, Malene Ringkjøbing; Cárdenes, Nayra; Bravo, Jerónimo ; Blackledge, Martin; Azuaga, Ana I.; van Nuland, Nico A. J.
Issue Date11-Sep-2013
PublisherPublic Library of Science
CitationPLoS ONE 8(9): e73018. (2013)
AbstractSH3 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.
Description14 páginas, 6 figuras. En material suplementario: 3 figuras, 2 tablas
Publisher version (URL)http://dx.doi.org/10.1371/journal.pone.0073018
URIhttp://hdl.handle.net/10261/82349
DOI10.1371/journal.pone.0073018
E-ISSN1932-6203
Appears in Collections:(IBV) Artículos
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