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

Dene R. Littler; Stephen J. Harrop; Sophia C. Goodchild; Juanita M. Phang; Andrew V. Mynott; Lele Jiang; Stella M. Valenzuela; Michele Mazzanti; Louise J. Brown; Samuel N. Breit; Paul M G Curmi

doi:10.1016/j.febslet.2010.01.027

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

Dene R. Littler, Stephen J. Harrop, Sophia C. Goodchild, Juanita M. Phang, Andrew V. Mynott, Lele Jiang, Stella M. Valenzuela, Michele Mazzanti, Louise J. Brown, Samuel N. Breit, Paul M G Curmi^*

^*Corresponding author for this work

Macquarie University Research Centre in Quantum Science and Technology

Research output: Contribution to journal › Review article › peer-review

143 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2093-2101
Number of pages	9
Journal	FEBS Letters
Volume	584
Issue number	10
DOIs	https://doi.org/10.1016/j.febslet.2010.01.027
Publication status	Published - May 2010

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

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.",

author = "Littler, {Dene R.} and Harrop, {Stephen J.} and Goodchild, {Sophia C.} and Phang, {Juanita M.} and Mynott, {Andrew V.} and Lele Jiang and Valenzuela, {Stella M.} and Michele Mazzanti and Brown, {Louise J.} and Breit, {Samuel N.} and Curmi, {Paul M G}",

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T2 - Ion channels, redox proteins, enzymes, scaffolding proteins?

AU - Littler, Dene R.

AU - Harrop, Stephen J.

AU - Goodchild, Sophia C.

AU - Phang, Juanita M.

AU - Mynott, Andrew V.

AU - Jiang, Lele

AU - Valenzuela, Stella M.

AU - Mazzanti, Michele

AU - Brown, Louise J.

AU - Breit, Samuel N.

AU - Curmi, Paul M G

PY - 2010/5

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N2 - 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.

AB - 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.

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DO - 10.1016/j.febslet.2010.01.027

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SN - 0014-5793

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SP - 2093

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JO - FEBS Letters

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

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