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The connexin43 gap junction protein is phosphorylated by protein kinase A and protein kinase C: in vivo and in vitro studies.

Abstract：

:There is general agreement that the connexin43 gap junction protein is a substrate for phosphorylation by protein kinase C but there is no similar consensus regarding the action of protein kinase A. Our previous studies demonstrated that channels formed by connexin43 were reversibly gated in response to microinjected protein kinase A and protein kinase C, but we did not determine whether these effects involved direct action on the connexin43 protein. Using a combination of in vivo metabolic labeling and in vitro phosphorylation of recombinant protein and synthetic peptides, we now find that connexin43 is a relatively poor substrate for purified protein kinase A compared to protein kinase C, but that phosphorylation can be accelerated by 8-Br-cAMP (8-bromoadenosine 3',5'-cyclic monophosphate) which also enhances connexin43 synthesis but at a much slower rate than phosphorylation. Phosphorylation of a critical amino acid, Ser364, by protein kinase A, appears to be necessary for subsequent multiple phosphorylations by protein kinase C. However, protein kinase C can phosphorylate connexin43 at a reduced level in the absence of prior phosphorylation. The results suggest that the correct regulation of channels formed by connexin43 may require sequential phosphorylations of this protein by protein kinase A and protein kinase C.

journal_name

Mol Cell Biochem

journal_title

Molecular and cellular biochemistry

authors

Shah MM,Martinez AM,Fletcher WH

doi

10.1023/a:1019902920693

keywords:

subject

Has Abstract

pub_date

2002-09-01 00:00:00

pages

57-68

issue

1-2

eissn

0300-8177

issn

1573-4919

journal_volume

238

pub_type

杂志文章

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