The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?
Littler, DR
Harrop, SJ
Goodchild, SC
Phang, JM
Mynott, AV
Jiang, L
Valenzuela, SM
Mazzanti, M
Brown, LJ
Breit, SN
Curmi, PMG
- Publication Type:
- Journal Article
- Citation:
- FEBS Letters, 2010, 584 (10), pp. 2093 - 2101
- Issue Date:
- 2010-05-01
Closed Access
Filename | Description | Size | |||
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2011000579OK.pdf | 606.95 kB | Adobe PDF |
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Littler, DR | en_US |
dc.contributor.author | Harrop, SJ | en_US |
dc.contributor.author | Goodchild, SC | en_US |
dc.contributor.author | Phang, JM | en_US |
dc.contributor.author | Mynott, AV | en_US |
dc.contributor.author |
Jiang, L https://orcid.org/0000-0002-1326-5871 |
en_US |
dc.contributor.author |
Valenzuela, SM https://orcid.org/0000-0001-5934-6047 |
en_US |
dc.contributor.author | Mazzanti, M | en_US |
dc.contributor.author | Brown, LJ | en_US |
dc.contributor.author | Breit, SN | en_US |
dc.contributor.author | Curmi, PMG | en_US |
dc.date.available | 2010-01-13 | en_US |
dc.date.issued | 2010-05-01 | en_US |
dc.identifier.citation | FEBS Letters, 2010, 584 (10), pp. 2093 - 2101 | en_US |
dc.identifier.issn | 0014-5793 | en_US |
dc.identifier.uri | http://hdl.handle.net/10453/14894 | |
dc.description.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. © 2010 Federation of European Biochemical Societies. | en_US |
dc.relation.ispartof | FEBS Letters | en_US |
dc.relation.isbasedon | 10.1016/j.febslet.2010.01.027 | en_US |
dc.subject.classification | Biochemistry & Molecular Biology | en_US |
dc.subject.mesh | Cell Membrane | en_US |
dc.subject.mesh | Cytoskeleton | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Enzymes | en_US |
dc.subject.mesh | Chloride Channels | en_US |
dc.subject.mesh | Oxidation-Reduction | en_US |
dc.subject.mesh | Hydrogen-Ion Concentration | en_US |
dc.title | The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins? | en_US |
dc.type | Journal Article | |
utslib.citation.volume | 10 | en_US |
utslib.citation.volume | 584 | en_US |
utslib.for | 0601 Biochemistry and Cell Biology | en_US |
utslib.for | 0304 Medicinal and Biomolecular Chemistry | en_US |
utslib.for | 0603 Evolutionary Biology | en_US |
pubs.embargo.period | Not known | en_US |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Mathematical and Physical Sciences | |
pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
utslib.copyright.status | closed_access | |
pubs.issue | 10 | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 584 | en_US |
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. © 2010 Federation of European Biochemical Societies.
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