Identification of a novel Ezrin‐binding site in syndecan‐2 cytoplasmic domain

FEBS Letters

Berndt, Christine¹  Roy, Christian²  Mangeat, Paul²  Reina, Manuel¹  Granés, Francesc¹  Vilaró, Senén¹ 

[1] Department of Cellular Biology, Faculty of Biology, University of Barcelona, Barcelona, Spain;Departement Biologie Santé, CNRS URA 1856, Université Montpellier II, Montpellier, France

关键词: Syndecan;    Ezrin/Radixin/Moesin proteins;    Protein interaction;    ERM;    Ezrin/Radixin/Moesin;    ICAM;    intercellular adhesion molecule;    NHE3;    Na+/H+ exchanger 3;    GST;    glutathione S-transferase;   

DOI  :  10.1016/S0014-5793(03)00712-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

ERM (Ezrin/Radixin/Moesin) proteins are crosslinkers between plasma membrane proteins and the actin cytoskeleton, thereby involved in the formation of cell adhesion sites. Earlier work showed that Ezrin links syndecan-2 to the actin cytoskeleton. Here we provide evidence that the Ezrin N-terminal domain binds to the syndecan-2 cytoplasmic domain with an estimated K _D of 0.71 μM and without the requirement of other proteins. We also studied the regions in the syndecan-2 cytoplasmic domain implicated in the binding to Ezrin. By truncating the syndecan-2 cytoplasmic domain and by oligopeptide competition assays we show that the Ezrin-binding sequence is not located in the positively charged juxtamembrane region (RMRKK), but in the neighboring sequence DEGSYD. We therefore conclude that the consensus sequence for Ezrin binding is unique among membrane proteins, suggesting a distinct regulation.

【 授权许可】

Unknown