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XB-ART-51239
Biophys J 2014 Sep 02;1075:1105-1116. doi: 10.1016/j.bpj.2014.07.040.
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GlialCAM, a CLC-2 Cl(-) channel subunit, activates the slow gate of CLC chloride channels.

Jeworutzki E , Lagostena L , Elorza-Vidal X , López-Hernández T , Estévez R , Pusch M .


Abstract
GlialCAM, a glial cell adhesion molecule mutated in megalencephalic leukoencephalopathy with subcortical cysts, targets the CLC-2 Cl(-) channel to cell contacts in glia and activates CLC-2 currents in vitro and in vivo. We found that GlialCAM clusters all CLC channels at cell contacts in vitro and thus studied GlialCAM interaction with CLC channels to investigate the mechanism of functional activation. GlialCAM slowed deactivation kinetics of CLC-Ka/barttin channels and increased CLC-0 currents opening the common gate and slowing its deactivation. No functional effect was seen for common gate deficient CLC-0 mutants. Similarly, GlialCAM targets the common gate deficient CLC-2 mutant E211V/H816A to cell contacts, without altering its function. Thus, GlialCAM is able to interact with all CLC channels tested, targeting them to cell junctions and activating them by stabilizing the open configuration of the common gate. These results are important to better understand the physiological role of GlialCAM/CLC-2 interaction.

PubMed ID: 25185546
PMC ID: PMC4156679
Article link: Biophys J
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: bsnd clcn5


Article Images: [+] show captions
References [+] :
Accardi, Fast and slow gating relaxations in the muscle chloride channel CLC-1. 2000, Pubmed, Xenbase