Gb. Krapivinsky et al., MOLECULAR CHARACTERIZATION OF A SWELLING-INDUCED CHLORIDE CONDUCTANCEREGULATORY PROTEIN, PL(CLN), Cell, 76(3), 1994, pp. 439-448
Cells maintain control of their volume by the passage of KCl and water
across their membranes, but the regulatory proteins are unknown. Expr
ession in Xenopus oocytes of a novel protein, pl(Cln), activated a chl
oride conductance. We have cloned analogs of pl(Cln), from rat heart a
nd Xenopus ovary. pl(Cln) was identified as an abundant soluble cytoso
lic protein (similar to 40 kd) that does not immunolocalize with the p
lasma membrane. pl(Cln) was found in epithelial and cardiac cells, bra
in, and Xenopus oocytes, forming complexes with soluble actin and othe
r cytosolic proteins. Monoclonal antibodies recognizing pl(Cln) blocke
d activation of a native hypotonicity-induced chloride conductance (I-
Cl.swell) in Xenopus oocytes, suggesting that pin, may link actin-boun
d cytoskeletal elements to an unidentified volume-sensitive chloride c
hannel. The high degree of sequence conservation and widespread expres
sion of pl(Cln) suggest that it is an important element in cellular vo
lume regulation.