期刊
CELL COMMUNICATION AND ADHESION
卷 14, 期 5, 页码 211-226出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/15419060701755958
关键词
connexin43; Akt; phosphorylation; 14-3-3; Mode-1 binding; protein interactions
资金
- NCI NIH HHS [CA052098, R01 CA052098-16, R01 CA052098] Funding Source: Medline
- NCRR NIH HHS [RR16467, P20 RR016467, P20-RR016453, P20 RR016453] Funding Source: Medline
Connexin43 (Cx43) is a membrane-spanning protein that forms channels that bridge the gap between adjacent cells and this allows for the intercellular exchange of information. Cx43 is regulated by phosphorylation and by interacting proteins. Mode-1 interaction with 14-3-3 requires phosphorylation of Ser373 on Cx43 (Park et al. 2006). Akt phosphorylates and targets a number of proteins to interactions with 14-3-3. Here we demonstrate that Akt phosphorylates Cx43 on Ser373 and Ser369; antibodies recognizing Akt-phosphorylated sites or phospho-Ser rnode-1 14-3-3-binding sites recognize a protein from EGF-treated cells that migrates as Cx43, and GST-14-3-3 binds to Cx43 phosphorylated endogenously in EGF-treated cells. Confocal microscopy supports the co-localization of Cx43 with Akt and with 14-3-3 at the outer edges of gap junctional plaques. These data suggest that Akt could target Cx43 to an interaction with 14-3-3 that may play a role in the forward trafficking of Cx43 multimers and/or their incorporation into existing gap junctional plaques.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据