- Record: found
- Abstract: found
- Article: not found
MEMO associated with an ErbB2 receptor phosphopeptide reveals a new phosphotyrosine motif.
Mikaël Feracci
1 ,
Cyril Pimentel ,
Olivier Bornet ,
Philippe Roche ,
Danièle Salaun ,
Ali Badache ,
Françoise Guerlesquin
Sep 02 2011
Read this article at
There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
Abstract
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.