These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Cdc2-mediated phosphorylation of the gap junction protein, connexin43, during mitosis.
    Author: Kanemitsu MY, Jiang W, Eckhart W.
    Journal: Cell Growth Differ; 1998 Jan; 9(1):13-21. PubMed ID: 9438384.
    Abstract:
    As cells enter mitosis, gap junctional communication with neighboring cells decreases (H. Xie et al., J. Cell Biol., 137: 203-210, 1997). Phosphorylation of the gap junction protein, connexin43 (Cx43), has been implicated in reducing junctional permeability. Cx43 contains p34cdc2 phosphorylation consensus sites in its COOH-terminal region. Accordingly, we examined the role of p34cdc2/cyclin B in Cx43 phosphorylation. Purified p34cdc2/cyclin B, or p34cdc2/cyclin B complex immunoprecipitated from mitotic cells, phosphorylated GSTCx43 in vitro. The synthetic peptide, SDPYHATTGPLSPSKDCGSPK, corresponding to amino acids 241-264 of Cx43, was also phosphorylated by p34cdc2/cyclin B in vitro. Sites phosphorylated in vitro were phosphorylated in vivo. Butyrolactone I, an inhibitor of cdc2 kinase, inhibited increases in Cx43 phosphorylation during mitosis. We conclude that phosphorylation of Cx43 by p34cdc2/cyclin B may contribute to the increased Cx43 phosphorylation and reduced gap junctional communication observed during mitosis.
    [Abstract] [Full Text] [Related] [New Search]