Chloride Intracellular Channel Protein 2: Difference between revisions

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CLIC proteins are a new class of soluble and membrane-bound proteins that have been grouped together on the basis of their sequence similarity. The proteins were named CLIC because the first members of this family to be characterized formed intracellular chloride channels. <ref>PMID:9339381</ref>  They display broad tissue and cellular distribution. They have been implicated in kidney function, cell division, and bone resorption. (Brett A. Cromer  and al, 2007 1) They differ from the other classes of chloride ion channels in primary structure and in the transmembrane regions of the tertiary structure. Since the first member of CLIC, p64 (CLIC5), was discovered in bovine kidney, several members of the CLIC family have been found in other tissues from many species, including NCC27 (CLIC1), CLIC2, CLIC3, mtCLIC (CLIC4), and parchorin (CLIC6). (X. Meng and al, 2009) With the exception of p64 and parchorin, these proteins contain a conserved region of approximately 240 residues. (Brett A. Cromer and al, 2007 2)
CLIC proteins are a new class of soluble and membrane-bound proteins that have been grouped together on the basis of their sequence similarity. The proteins were named CLIC because the first members of this family to be characterized formed intracellular chloride channels. <ref>PMID:9339381</ref>  They display broad tissue and cellular distribution. They have been implicated in kidney function, cell division, and bone resorption. <ref>PMID:18007051</ref> They differ from the other classes of chloride ion channels in primary structure and in the transmembrane regions of the tertiary structure. Since the first member of CLIC, p64 (CLIC5), was discovered in bovine kidney, several members of the CLIC family have been found in other tissues from many species, including NCC27 (CLIC1), CLIC2, CLIC3, mtCLIC (CLIC4), and parchorin (CLIC6). (X. Meng and al, 2009) With the exception of p64 and parchorin, these proteins contain a conserved region of approximately 240 residues. (Brett A. Cromer and al, 2007 2)
CLIC proteins can localize to distinct cellular membranes, including the nuclear membrane, lysosomal membranes, mitochondria, Golgi membranes, cell–cell junctions, and the plasma membrane. (Brett A. Cromer and al, 2007 1)
CLIC proteins can localize to distinct cellular membranes, including the nuclear membrane, lysosomal membranes, mitochondria, Golgi membranes, cell–cell junctions, and the plasma membrane. (Brett A. Cromer and al, 2007 1)
The CLIC proteins show sequence homology with members of the glutathione-S-transferase (GST) superfamily.
The CLIC proteins show sequence homology with members of the glutathione-S-transferase (GST) superfamily.
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Proteins. 2008 Apr. PMID: 18186468  
Proteins. 2008 Apr. PMID: 18186468  


'''Expression, purification, crystallization and preliminary X-ray diffraction analysis of chloride intracellular channel 2 (CLIC2).'''
 
Cromer BA, Gorman MA, Hansen G, Adams JJ, Coggan M, Board PG, Parker MW.
 
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1.PMID: 18007051


'''Structure of the Janus protein human CLIC2'''
'''Structure of the Janus protein human CLIC2'''
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Berryman M, Bretscher A.
Berryman M, Bretscher A.


Mol Biol Cell. 2000 May.PMID: 10793131  
Mol Biol Cell. 2000 May.PMID: 10793131
 
'''Genomic structure of a novel chloride channel gene, CLIC2, in Xq28.
'''
Heiss NS, Poustka A.
 
Genomics. 1997 Oct 1.PMID: 9339381
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