MEMO associated with an ErbB2 receptor phosphopeptide reveals a new phosphotyrosine motif
- Feracci, Mikaël
- Pimentel, Cyril
- Bornet, Olivier
- Roche, Philippe
- Salaun, Danièle
- Badache, Ali
- Guerlesquin, Françoise
Publication date
September 2011
DOI Publisher
Federation of European Biochemical Societies. Published by Elsevier B.V.Abstract
AbstractTyrosine phosphorylations are essential in signal transduction. Recently, a new type of phosphotyrosine binding protein, MEMO (Mediator of ErbB2-driven cell motility), has been reported to bind specifically to an ErbB2-derived phosphorylated peptide encompassing Tyr-1227 (PYD). Structural and functional analyses of variants of this peptide revealed the minimum sequence required for MEMO recognition. Using a docking approach we have generated a structural model for MEMO/PYD complex and compare this new phosphotyrosine motif to SH2 and PTB phosphotyrosine motives.Structured summary of protein interactionsErbB2 physically interacts with MEMO by pull down (View interaction 1, 2, 3, 4, 5, 6
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