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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
Author(s) -
Balda Maria S.,
Anderson James M.,
Matter Karl
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01352-x
Subject(s) - sh3 domain , protein kinase domain , hamp domain , phosphoprotein , microbiology and biotechnology , egf like domain , guanylate kinase , chemistry , c raf , phosphorylation , biology , mitogen activated protein kinase kinase , protein kinase a , binding domain , proto oncogene tyrosine protein kinase src , biochemistry , binding site , gene , membrane protein , membrane , mutant
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.