Chloride intracellular channel proteins (CLICs) are distinct from most ion channels in that they have both soluble and integral membrane forms. CLICs are highly conserved in chordates, with six vertebrate paralogues. CLIC-like proteins are found in other metazoans. CLICs form channels in artificial bilayers in a process favoured by oxidising conditions and low pH. They are structurally plastic, with CLIC1 adopting two distinct soluble conformations. Phylogenetic and structural data indicate that CLICs are likely to have enzymatic function. The physiological role of CLICs appears to be maintenance of intracellular membranes, which is associated with tubulogenesis but may involve other substructures.

The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins? / D.R. Littler, S.J. Harrop, S.C. Goodchild, J.M. Phang, A.V. Mynott, L. Jiang, S.M. Valenzuela, M. Mazzanti, L.J. Brown, S.N. Breit, P.M. Curmi. - In: FEBS LETTERS. - ISSN 0014-5793. - 584:10(2010), pp. 2093-2101.

The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?

M. Mazzanti;
2010

Abstract

Chloride intracellular channel proteins (CLICs) are distinct from most ion channels in that they have both soluble and integral membrane forms. CLICs are highly conserved in chordates, with six vertebrate paralogues. CLIC-like proteins are found in other metazoans. CLICs form channels in artificial bilayers in a process favoured by oxidising conditions and low pH. They are structurally plastic, with CLIC1 adopting two distinct soluble conformations. Phylogenetic and structural data indicate that CLICs are likely to have enzymatic function. The physiological role of CLICs appears to be maintenance of intracellular membranes, which is associated with tubulogenesis but may involve other substructures.
Chloride intracellular channel protein ; Redox ; Membrane insertion ; Tubulogenesis ; CLIC1
Settore BIO/09 - Fisiologia
2010
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/141087
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