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

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.
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https://hal.archives-ouvertes.fr/hal-01458275
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Submitted on : Monday, February 6, 2017 - 5:49:26 PM
Last modification on : Friday, May 6, 2022 - 2:56:02 PM

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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, Wiley, 2011, 585 (17), pp.2688--92. ⟨10.1016/j.febslet.2011.07.048⟩. ⟨hal-01458275⟩

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