Competitive binding of UBPY and ubiquitin to the STAM2 SH3 domain revealed by NMR
Anja Lange1, Mouhamad-Baligh Ismail, Gwladys Rivière
1Université de Lyon, Université Claude Bernard Lyon1, CNRS, UMR 5280 Institut des Sciences Analytiques, Villeurbanne, France.
Abstract:
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.
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