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Membranes 2016, 6(1), 15; doi:10.3390/membranes6010015

Cholesterol Promotes Interaction of the Protein CLIC1 with Phospholipid Monolayers at the Air–Water Interface

1
School of Life Sciences, University of Technology Sydney, Sydney, New South Wales 2007, Australia
2
Bragg Institute, Australian Nuclear Science and Technology Organisation (ANSTO), New South Wales 2234, Australia
*
Author to whom correspondence should be addressed.
Received: 22 December 2015 / Revised: 27 January 2016 / Accepted: 29 January 2016 / Published: 11 February 2016
(This article belongs to the Special Issue Membranes and Ion Channels)
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Abstract

CLIC1 is a Chloride Intracellular Ion Channel protein that exists either in a soluble state in the cytoplasm or as a membrane bound protein. Members of the CLIC family are largely soluble proteins that possess the intriguing property of spontaneous insertion into phospholipid bilayers to form integral membrane ion channels. The regulatory role of cholesterol in the ion-channel activity of CLIC1 in tethered lipid bilayers was previously assessed using impedance spectroscopy. Here we extend this investigation by evaluating the influence of cholesterol on the spontaneous membrane insertion of CLIC1 into Langmuir film monolayers prepared using 1-palmitoyl-2-oleoylphosphatidylcholine, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-ethanolamine and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine alone or in combination with cholesterol. The spontaneous membrane insertion of CLIC1 was shown to be dependent on the presence of cholesterol in the membrane. Furthermore, pre-incubation of CLIC1 with cholesterol prior to its addition to the Langmuir film, showed no membrane insertion even in monolayers containing cholesterol, suggesting the formation of a CLIC1-cholesterol pre-complex. Our results therefore suggest that CLIC1 membrane interaction involves CLIC1 binding to cholesterol located in the membrane for its initial docking followed by insertion. Subsequent structural rearrangements of the protein would likely also be required along with oligomerisation to form functional ion channels. View Full-Text
Keywords: CLIC1; membrane insertion; cholesterol; Langmuir monolayer film; phospholipids; POPC; POPE; POPS CLIC1; membrane insertion; cholesterol; Langmuir monolayer film; phospholipids; POPC; POPE; POPS
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Hossain, K.R.; Al Khamici, H.; Holt, S.A.; Valenzuela, S.M. Cholesterol Promotes Interaction of the Protein CLIC1 with Phospholipid Monolayers at the Air–Water Interface. Membranes 2016, 6, 15.

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