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Sep 2011 FEBS letters

MEMO associated with an ErbB2 receptor phosphopeptide reveals a new phosphotyrosine motif.


Feracci M, Pimentel C, Bornet O, Roche P, Salaun D, Badache A, Guerlesquin F


Tyrosine 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.

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