ArticlePloS one2013
Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Association of CD2AP neuronal deposits with Braak neurofibrillary stage in Alzheimer's disease.Brain pathology (Zurich, Switzerland) · 2022Article
- Regulation of CYLD activity and specificity by phosphorylation and ubiquitin-binding CAP-Gly domains.Cell reports · 2021Article
- Article
- (S)Pinning down protein interactions by NMR.Protein science : a publication of the Protein Society · 2017Review
- Bin1 and CD2AP polarise the endocytic generation of beta-amyloid.EMBO reports · 2017Article
- Differential Recognition Preferences of the Three Src Homology 3 (SH3) Domains from the Adaptor CD2-associated Protein (CD2AP) and Direct Association with Ras and Rab Interactor 3 (RIN3).The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors at 6 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
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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Registered trials
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