Open AccessTyrosine 284 phosphorylation is required for ClC-3 chloride channel activation in vascular smooth muscle cells
Author(s) -
Xiaoguang Wang,
Jing Tao,
Mingming Ma,
YongBo Tang,
JiaGuo Zhou,
YongYuan Guan
Publication year - 2013
Publication title -
cardiovascular research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.774
H-Index - 219
eISSN - 1755-3245
pISSN - 0008-6363
DOI - 10.1093/cvr/cvt063
Subject(s) - phosphorylation , tyrosine phosphorylation , tyrosine , vascular smooth muscle , chloride channel , microbiology and biotechnology , protein tyrosine phosphatase , chemistry , intracellular , signal transduction , smooth muscle , biochemistry , biology , endocrinology
The ClC-3 chloride channel (and current, ICl,ClC-3) plays an important role in cell volume regulation, proliferation, and apoptosis in vascular smooth muscle cells, and is a potential target for prevention of vascular remodelling and stroke. However, modulation of ICl,ClC-3 by intercellular signalling is not fully understood. Although it has been suggested that tyrosine phosphorylation is required for ICl,ClC-3 activation, the potential tyrosine residues in the ClC-3 protein are not clear. In the present study, the critical tyrosine residues in ClC-3 protein were investigated.
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