Competitive binding of UBPY and ubiquitin to the STAM2 SH3 domain revealed by NMR

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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FEBS Letters, Wiley, 2012, 586 (19), pp.3379-3384. 〈10.1016/j.febslet.2012.07.047〉
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https://hal.archives-ouvertes.fr/hal-00819142
Contributeur : Agnès Bussy <>
Soumis le : mardi 30 avril 2013 - 11:22:39
Dernière modification le : samedi 5 décembre 2015 - 01:49:58

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Anja Lange, Mouhamad-Baligh Ismail, Gwladys Rivière, Maggy Hologne, Denis Lacabanne, et al.. Competitive binding of UBPY and ubiquitin to the STAM2 SH3 domain revealed by NMR. FEBS Letters, Wiley, 2012, 586 (19), pp.3379-3384. 〈10.1016/j.febslet.2012.07.047〉. 〈hal-00819142〉

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