Title : Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins.

Pub. Date : 2000 Jul 21

PMID : 10801818






3 Functional Relationships(s)
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1 We screened the entire amino acid sequence of human zyxin for Mena-interacting peptides and found that, as with ActA, proline-rich sequences were the sole zyxin sequences capable of binding to Ena/vasodilator-stimulated phosphoprotein (VASP) family members in vitro. Proline vasodilator stimulated phosphoprotein Homo sapiens
2 Microinjection into cells of peptides corresponding to the first proline-rich sequence of zyxin caused the loss of Mena/VASP from focal contacts. Proline vasodilator stimulated phosphoprotein Homo sapiens
3 We conclude that zyxin and proteins that harbor similar proline-rich repeats contribute to the positioning of Mena/VASP proteins. Proline vasodilator stimulated phosphoprotein Homo sapiens