Connexin43 phosphorylation: structural changes and biological effects.
Connexin43 phosphorylation: structural changes and biological effects.
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DOI:
10.1042/bj20082319
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发表时间:
2009-04-15
期刊:
影响因子:
--
通讯作者:
Lampe PD
中科院分区:
文献类型:
--
作者:
Solan JL;Lampe PD
Vertebrate gap junctions, composed of proteins from the connexin gene family, play critical roles in embryonic development, coordinated contraction of excitable cells, tissue homeostasis, 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. This 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.