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

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.Structured summary of protein interactionsErbB2physically interacts with MEMO by pull down (View interaction 1, 2, 3, 4, 5, 6)

► ErbB2 is associated with the most aggressive tumors.
► MEMO is a new class of phosphotyrosine binding protein that binds ErbB2.
► We present a structural model for the MEMO/PYD complex.