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FEBS Lett. 2011 Sep 2;585(17):2688-92. doi: 10.1016/j.febslet.2011.07.048. Epub 2011 Aug 10.

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

Author information

1
UPR3243-CNRS, Marseille, France.

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.

PMID:
21840311
DOI:
10.1016/j.febslet.2011.07.048
[Indexed for MEDLINE]
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