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000838399 1001_ $$0P:(DE-Juel1)156375$$aGuzman, Raul$$b0$$eCorresponding author
000838399 245__ $$aPreferential Association with ClC-3 Permits Sorting of ClC-4 into Endosomal Compartments
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000838399 520__ $$aClC-4 is an intracellular Cl--H+ exchanger, which is highly expressed in the brain and whose dysfunction has been linked to intellectual disability and epilepsy. We here studied the subcellular localization of human ClC-4 in heterologous expression systems. ClC-4 is retained in the endoplasmic reticulum (ER) upon overexpression in HEK293T cells. Co-expression with distinct ClC-3 splice variants targets ClC-4 to late endosome/lysosomes (ClC-3a and ClC-3b), recycling endosome (ClC-3c) or to the Golgi (ClC-3e). When expressed in cultured astroctyes ClC-4 sorts to endocytic compartments in WT cells, but was retained in the ER in Clcn3-/- cells. To understand the virtual absence of ER localized ClC-4 in WT cells we performed association studies by high resolution clear native gel electrophoresis (hrCNE). Whereas other CLCm channels and transporters form stable dimers, ClC-4 was mostly observed as monomer, with ClC-3-ClC-4 heterodimers being more stable than ClC-4 homodimers. We conclude that unique oligomerization properties of ClC-4 permits regulated targeting of ClC-4 to various endosomal compartments system via expression of different ClC-3 splice variants.
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000838399 7001_ $$0P:(DE-Juel1)131923$$aFranzen, Arne$$b1
000838399 7001_ $$0P:(DE-Juel1)131915$$aBungert, Stefanie$$b2
000838399 7001_ $$0P:(DE-Juel1)136837$$aFahlke, Christoph$$b3
000838399 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M117.801951$$gp. jbc.M117.801951 -$$p19055-19065$$tThe journal of biological chemistry$$v292$$x1083-351X$$y2017
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