MEMO associated with an ErbB2 receptor phosphopeptide reveals a new phosphotyrosine motif. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue FEBS Letters Année : 2011

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

Résumé

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.

Dates et versions

hal-01458275 , version 1 (06-02-2017)

Identifiants

Citer

Mikael Feracci, Cyril Pimentel, Olivier Bornet, Philippe Roche, Danièle Salaün, et al.. MEMO associated with an ErbB2 receptor phosphopeptide reveals a new phosphotyrosine motif.. FEBS Letters, 2011, 585 (17), pp.2688--92. ⟨10.1016/j.febslet.2011.07.048⟩. ⟨hal-01458275⟩
83 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Mastodon Facebook X LinkedIn More