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Laboratory of Physiology, Catholic University of Leuven, Campus Gasthuisberg, B-3000 Leuven, Belgium
We used the whole cell
patch-clamp technique in calf pulmonary endothelial (CPAE) cells to
investigate the effect of wild-type and mutant c-Src tyrosine kinase on
ICl,swell, the swelling-induced Cl
current through volume-regulated anion channels (VRAC). Transient transfection of wild-type c-Src in CPAE cells did not significantly affect ICl,swell. However, transfection of c-Src
with a Ser3Cys mutation that introduces a dual acylation
signal and targets c-Src to lipid rafts and caveolae strongly repressed
hypotonicity-induced ICl,swell in CPAE cells.
Kinase activity was dispensable for the inhibition of
ICl,swell, since kinase-deficient c-Src
Ser3Cys either with an inactivating point mutation in the
kinase domain or with the entire kinase domain deleted still suppressed
VRAC activity. Again, the Ser3Cys mutation was required to
obtain maximal inhibition by the kinase-deleted c-Src. In contrast, the
inhibitory effect was completely lost when the Src homology domains 2 and 3 were deleted in c-Src. We therefore conclude that c-Src-mediated
inhibition of VRAC requires compartmentalization of c-Src to caveolae
and that the Src homology domains 2 and/or 3 are necessary and
sufficient for inhibition.
anion channel; caveola; tyrosine kinase; cell volume; volume-regulated anion channel
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