The SH3 domain of the tight junction protein ZO‐1 binds to a serine protein kinase that phosphorylates a region C‐terminal to this domain

FEBS Letters

Anderson, James M.¹  Balda, Maria S.²  Matter, Karl² 

[1] Department of Internal Medicine and Cell Biology, Yale School of Medicine, New Haven, CT, USA;Department of Cell Biology, Science III, University of Geneva, 30, Quai Ernest-Ansermet, 1211 Geneva 4, Switzerland

关键词: Tight junction;    ZO-1;    SH3 domain;    Serine protein kinase;    ZO-1;    zonula occludens-1;    ZO-2;    zonula occludens-2;    SH3;    Src homology domain 3;    GST;    glutathione S-transferase;    PDZ domain;    PSD95-Dlg A-ZO-1 homology domain;    ZAK;    ZO-1 Associated Kinase;   

DOI  :  10.1016/S0014-5793(96)01352-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

ZO-1 is a tight junction phosphoprotein partially homologous to a tumor suppressor in Drosophila. The homologous region contains an SH3 domain with an unidentified function. Using fusion proteins containing the SH3 domain and various N- and C-terminal sequences, we tested for association of a kinase with this protein domain in extracts of MDCK cells. We show that the SH3 domain of ZO-1 binds a serine protein kinase that phosphorylates a region immediately C-terminal to the SH3 domain. This kinase associates specifically with the SH3 domain of ZO-1 and appears to be also associated with junctional complexes extracted from MDCK cells.

【 授权许可】

Unknown