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...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039852/?tool=EBI |
| _version_ | 1818742614756687872 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-18T02:15:19Z |
| format | Article |
| id | doaj.art-f0dfce6381094a71b4f4d8cd64cd8eef |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-18T02:15:19Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-f0dfce6381094a71b4f4d8cd64cd8eef2022-12-21T21:24:24ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0189e7301810.1371/journal.pone.0073018Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.Jose L Ortega RoldanSalvador CasaresMalene Ringkjøbing JensenNayra CárdenesJerónimo BravoMartin BlackledgeAna I AzuagaNico A J van NulandSH3 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.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039852/?tool=EBI |
| spellingShingle | 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. PLoS ONE |
| title | 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_short | 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 |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039852/?tool=EBI |
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