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

Abstract : 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.
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https://hal.univ-grenoble-alpes.fr/hal-01321627
Contributeur : Frank Thomas <>
Soumis le : jeudi 26 mai 2016 - 09:55:26
Dernière modification le : mardi 6 octobre 2020 - 16:12:09

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Jose L Ortega Roldan, Salvador Casares, Malene Ringkjøbing Jensen, Nayra Cárdenes, Jerónimo Bravo, et al.. Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.. PLoS ONE, Public Library of Science, 2013, 8 (9), pp.e73018. ⟨10.1371/journal.pone.0073018⟩. ⟨hal-01321627⟩

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