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Originally published In Press as doi:10.1074/jbc.M005826200 on October 16, 2000

J. Biol. Chem., Vol. 276, Issue 3, 1780-1788, January 19, 2001
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c-Src Regulates the Interaction between Connexin-43 and ZO-1 in Cardiac Myocytes*

Toshihiko ToyofukuDagger §||, Yoshiki Akamatsu||, Hong Zhang, Tsunehiko Kuzuya, Michihiko Tada, and Masatsugu HoriDagger

From the Dagger  Department of Internal Medicine and Therapeutics and the  Department of Pathology and Pathophysiology, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871, Japan

Connexin-43 is known to interact directly with ZO-1 in cardiac myocytes, but little is known about the role of ZO-1 in connexin-43 function. In cardiac myocytes, constitutively active c-Src inhibited endogenous interaction between connexin-43 and ZO-1 by binding to connexin-43. In HEK293 cells, by contrast, a connexin-43 mutant lacking the Src phosphorylation site (Tyr265) interacted with ZO-1 despite cotransfection of a constitutively active c-Src. Moreover, in vitro binding assays using recombinant proteins synthesized from regions of connexin-43 and ZO-1 showed that the tyrosine-phosphorylated C terminus of connexin-43 interacts with the c-Src SH2 domain in parallel with the loss of its interaction with ZO-1. Cell surface biotinylation revealed that, by phosphorylating Tyr265, constitutively active c-Src reduces total and cell surface connexin-43 down to the levels seen in cells expressing a mutant connexin-43 lacking the ZO-1 binding domain. Finally, electrophysiological analysis showed that both the tyrosine phosphorylation site and the ZO-1-binding domain of connexin-43 were involved in the regulation of gap junctional function. We therefore conclude that c-Src regulates the interaction between connexin-43 and ZO-1 through tyrosine phosphorylation and through the binding of its SH2 domain to connexin-43.

* This work was supported by grants-in-aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| These authors contributed equally to this work.

§ To whom correspondence should be addressed: Dept. of Internal Medicine and Therapeutics, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-3273; Fax: 81-6-6879-3279; E-mail: toyofuku@mr-path.med.osaka-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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