Journal
FEBS LETTERS
Volume 586, Issue 19, Pages 3379-3384Publisher
WILEY
DOI: 10.1016/j.febslet.2012.07.047
Keywords
Nuclear magnetic resonance; Endocytosis; Protein-protein interaction; STAM2 UIM-SH3; Deubiquitinating enzyme; UBPY
Funding
- TGE RMN THC [Fr3050]
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To date, the signal transducing adaptor molecule 2 (STAM2) was shown to harbour two ubiquitin binding domains (UBDs) known as the VHS and UIM domains, while the SH3 domain of STAM2 was reported to interact with deubiquitinating enzymes (DUBs) like UBPY and AMSH. In the present study, NMR evidences the interaction of the STAM2 SH3 domain with ubiquitin, demonstrating that SH3 constitutes the third UBD of STAM2. Furthermore, we show that a UBPY-derived peptide can outcompete ubiquitin for SH3 binding and vice versa. These results suggest that the SH3 domain of STAM2 plays versatile roles in the context of ubiquitin mediated receptor sorting. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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