Functional reconstitution of mammalian ‘chloride intracellular channels’ CLIC1, CLIC4 and CLIC5 reveals differential regulation by cytoskeletal actin

@article{Singh2007FunctionalRO,
  title={Functional reconstitution of mammalian ‘chloride intracellular channels’ CLIC1, CLIC4 and CLIC5 reveals differential regulation by cytoskeletal actin},
  author={H Singh and Michael A. Cousin and R Head Ashley},
  journal={The FEBS Journal},
  year={2007},
  volume={274}
}
Chloride intracellular channels (CLICs) are soluble, signal peptide‐less proteins that are distantly related to Ω‐type glutathione‐S‐transferases. Although some CLICs bypass the classical secretory pathway and autoinsert into cell membranes to form ion channels, their cellular roles remain unclear. Many CLICs are strongly associated with cytoskeletal proteins, but the role of these associations is not known. In this study, we incorporated purified, recombinant mammalian CLIC1, CLIC4 and (for… 
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Emerging biological roles of Cl− intracellular channel proteins
TLDR
Emerging evidence points to a role of CLIC proteins in actin dynamics and membrane trafficking and the lessons learned from gene-targeting studies are discussed.
Interaction of Human Chloride Intracellular Channel Protein 1 (CLIC1) with Lipid Bilayers: A Fluorescence Study.
TLDR
It is shown that fluorescence spectroscopy can be used to establish the interaction and position of CLIC1 in a lipid bilayer and support the current model of an oxidation-driven interaction of CLic1 with lipid bilayers and also propose a membrane anchoring role for Trp35.
Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein
TLDR
It is found that indanyloxyacetic acid-94 (IAA-94), a blocker of CLICs, delays the growth of Escherichia coli and SspA, the E. coli stringent starvation protein A, shares sequence and structural homology with CL ICs and forms functional ion channels.
CLIC 4 translocation 25 Spatiotemporal regulation of CLIC 4 , a novel player in the G α 13-RhoA signaling pathway
TLDR
The results show that CLIC4 is regulated by G 13-linked RhoA pathway to be targeted to G13-coupled receptor complexes at the plasma membrane, and they suggest thatCLIC4 binds an as-yet-unknown substrate in a manner analogous to GST-substrate interaction.
Investigating Sterol and Redox Regulation of the Ion Channel Activity of CLIC1 Using Tethered Bilayer Membranes
TLDR
It is shown that membrane sterols play an essential role in CLIC1’s acrobatic switching from a globular soluble form to an integral membrane form, promoting greater ion channel conductance in membranes, and that redox play a role in the ion channel activity of CLic1.
Transmembrane extension and oligomerization of the CLIC1 chloride intracellular channel protein upon membrane interaction.
TLDR
Fitting the data to symmetric oligomer models of the CLIC1 transmembrane form indicates that the structure is large and most consistent with a model comprising approximately six to eight subunits.
Data supporting characterization of CLIC1, CLIC4, CLIC5 and DmCLIC antibodies and localization of CLICs in endoplasmic reticulum of cardiomyocytes
Regulation of the Membrane Insertion and Conductance Activity of the Metamorphic Chloride Intracellular Channel Protein CLIC1 by Cholesterol
TLDR
The observed cholesterol dependent behaviour of CLIC1 is highly reminiscent of the cholesterol-dependent-cytolysin family of bacterial pore-forming proteins, suggesting common regulatory mechanisms for spontaneous protein insertion into the membrane bilayer.
Both CLIC4 and CLIC5A activate ERM proteins in glomerular endothelium.
TLDR
The findings indicate that CLIC4/CLIC5A-mediated ERM activation is required for maintenance of the glomerular capillary architecture.
The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?
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References

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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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