Vertebrate gap junctions, composed of proteins from the connexin gene family, play critical roles in embryonic development, co-ordinated contraction of excitable cells, tissue homoeostasis, normal cell growth and differentiation. Phosphorylation of connexin43, the most abundant and ubiquitously expressed connexin, has been implicated in the regulation of gap junctional communication at several stages of the connexin ‘life cycle’, including hemichannel oligomerization, export of the protein to the plasma membrane, hemichannel activity, gap junction assembly, gap junction channel gating and connexin degradation. Consistent with a short (1–5 h) protein half-life, connexin43 phosphorylation is dynamic and changes in response to activation of many different kinases. The present review assesses our current understanding of the effects of phosphorylation on connexin43 structure and function that in turn regulate gap junction biology, with an emphasis on events occurring in heart and skin.
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Review Article|
March 27 2009
Connexin43 phosphorylation: structural changes and biological effects
Joell L. Solan;
Joell L. Solan
1Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, M5C800 Box 19024, Seattle, WA 98109, U.S.A.
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Paul D. Lampe
Paul D. Lampe
1
1Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, M5C800 Box 19024, Seattle, WA 98109, U.S.A.
1To whom correspondence should be addressed (email plampe@fhcrc.org).
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Publisher: Portland Press Ltd
Received:
December 03 2008
Revision Received:
February 02 2009
Accepted:
February 11 2009
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 419 (2): 261–272.
Article history
Received:
December 03 2008
Revision Received:
February 02 2009
Accepted:
February 11 2009
Citation
Joell L. Solan, Paul D. Lampe; Connexin43 phosphorylation: structural changes and biological effects. Biochem J 15 April 2009; 419 (2): 261–272. doi: https://doi.org/10.1042/BJ20082319
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