TY - JOUR
T1 - Molecular characterization of a swelling-induced chloride conductance regulatory protein, plCIn
AU - Krapivinsky, Grigory B.
AU - Ackerman, Michael J.
AU - Gordon, Eric A.
AU - Krapivinsky, Lyubov D.
AU - Clapham, David E.
N1 - Funding Information:
Address correspondence to D. E. C. We are indebted to Sara Manahan for her technical assistance. We thank Markus Paulmichl for the MDCK lcln fusion protein-PAX vector construct, Mark Sanders for his assistance with immunofluorescence, and Benjamin Madden and the Mayo Peptide Facility for microsequencing. This investigation was supported by National Institutes of Health grant NIDDK44025. D. E. C. is an Established Investigator of the American Heart Associabon.
PY - 1994/2/11
Y1 - 1994/2/11
N2 - Cells maintain control of their volume by the passage of KCI and water across their membranes, but the regulatory proteins are unknown. Expression in Xenopus oocytes of a novel protein, plCln, activated a chloride conductance. We have cloned analogs of plCln from rat heart and Xenopus ovary. plCln was identified as an abundant soluble cytosolic protein (∼40 kd) that does not immunolocalize with the plasma membrane. plCln was found in epithelial and cardiac cells, brain, and Xenopus oocytes, forming complexes with soluble actin and other cytosolic proteins. Monoclonal antibodies recognizing plCln blocked activation of a native hypotonicity-induced chloride conductance (ICl.swell) in Xenopus oocytes, suggesting that plCln may link actin-bound cytoskeletal elements to an unidentified volume-sensitive chloride channel. The high degree of sequence conservation and widespread expression of plCln suggest that it is an important element in cellular volume regulation.
AB - Cells maintain control of their volume by the passage of KCI and water across their membranes, but the regulatory proteins are unknown. Expression in Xenopus oocytes of a novel protein, plCln, activated a chloride conductance. We have cloned analogs of plCln from rat heart and Xenopus ovary. plCln was identified as an abundant soluble cytosolic protein (∼40 kd) that does not immunolocalize with the plasma membrane. plCln was found in epithelial and cardiac cells, brain, and Xenopus oocytes, forming complexes with soluble actin and other cytosolic proteins. Monoclonal antibodies recognizing plCln blocked activation of a native hypotonicity-induced chloride conductance (ICl.swell) in Xenopus oocytes, suggesting that plCln may link actin-bound cytoskeletal elements to an unidentified volume-sensitive chloride channel. The high degree of sequence conservation and widespread expression of plCln suggest that it is an important element in cellular volume regulation.
UR - http://www.scopus.com/inward/record.url?scp=0028144541&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028144541&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(94)90109-0
DO - 10.1016/0092-8674(94)90109-0
M3 - Article
C2 - 8313467
AN - SCOPUS:0028144541
SN - 0092-8674
VL - 76
SP - 439
EP - 448
JO - Cell
JF - Cell
IS - 3
ER -