Open Close
Reference
Citation
Littler, D.R., Harrop, S.J., Goodchild, S.C., Phang, J.M., Mynott, A.V., Jiang, L., Valenzuela, S.M., Mazzanti, M., Brown, L.J., Breit, S.N., Curmi, P.M. (2010). The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?  FEBS Lett. 584(10): 2093--2101.
FlyBase ID
FBrf0232068
Publication Type
Review
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.

PubMed ID
PubMed Central ID
Associated Information
Comments
Associated Files
Other Information
Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    FEBS Lett.
    Title
    FEBS Letters
    Publication Year
    1968-
    ISBN/ISSN
    0014-5793
    Data From Reference
    Gene Groups (1)
    Genes (1)