Am J Physiol Cell Physiol AJP: Regulatory, Integrative and Comparative Physiology
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Am J Physiol Cell Physiol (January 2, 2002). doi:10.1152/ajpcell.00402.2001
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Articles in PresS, published online ahead of print January 2, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00402.2001
Submitted on August 17, 2001
Accepted on December 19, 2001

CLIC1 Inserts From the Aqueous Phase Into Phospholipid Membranes Where it Functions as an Anion Channel

Barry M Tulk1, Shefalee Kapadia1, and John C Edwards2*

1 Internal Medicine, St. Louis University, St. Louis, MO, USA
2 Renal Service, St. Louis VA Medical Center, St. Louis, MO, USA; Internal Medicine, St. Louis University, St. Louis, MO, USA

* To whom correspondence should be addressed. E-mail: John.Edwards3{at}med.va.gov.

CLIC1 is a member of the CLIC family of proteins which has been shown to demonstrate chloride channel activity when reconstituted in phospholipid vesicles. CLIC1 exists in cells both as an integral membrane protein and as a soluble cytoplasmic protein, implying that CLIC1 might cycle between membrane-inserted and soluble forms. CLIC1 was purified and detergent removed, yielding an aqueous solution of essentially pure protein. Pure CLIC1 was mixed with vesicles and chloride permeability assessed with both a chloride efflux assay and with planar lipid bilayer techniques. Soluble CLIC1 confers anion channel activity to preformed membranes that is indistinguishable from the previously reported activity resulting from reconstitution of CLIC1 into membranes by detergent dialysis. The activity is dependent on the amount of CLIC1 added, appears rapidly upon mixing of protein and lipid, is inhibited by IAA-94, NEM, and glutathione, is inactivated by heat, and shows sensitivity to both pH and to membrane lipid composition. We conclude that CLIC1 in the absence of detergent spontaneously inserts into pre-formed membranes where it can function as an anion selective channel.




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