PMID:17244534

Citation	Stamenova, SD, French, ME, He, Y, Francis, SA, Kramer, ZB and Hicke, L (2007) Ubiquitin binds to and regulates a subset of SH3 domains. Mol. Cell 25:273-84
Abstract	SH3 domains are modules of 50-70 amino acids that promote interactions among proteins, often participating in the assembly of large dynamic complexes. These domains bind to peptide ligands, which usually contain a core Pro-X-X-Pro (PXXP) sequence. Here we identify a class of SH3 domains that bind to ubiquitin. The yeast endocytic protein Sla1, as well as the mammalian proteins CIN85 and amphiphysin, carry ubiquitin-binding SH3 domains. Ubiquitin and peptide ligands bind to the same hydrophobic groove on the SH3 domain surface, and ubiquitin and a PXXP-containing protein fragment compete for binding to SH3 domains. We conclude that a subset of SH3 domains constitutes a distinct type of ubiquitin-binding domain and that ubiquitin binding can negatively regulate interaction of SH3 domains with canonical proline-rich ligands.
Links	PubMed PMC2713028 Online version:10.1016/j.molcel.2006.12.016
Keywords	Amino Acid Sequence; Binding Sites/genetics; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/metabolism; Cytoskeletal Proteins; Endocytosis; Humans; Ligands; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/metabolism; Sequence Homology, Amino Acid; Ubiquitin/chemistry; Ubiquitin/metabolism; src Homology Domains
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