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Article

The chloride channel ClC-4 contributes to endosomal acidification and trafficking.

The Journal of biological chemistry - 1 Aug 2003

Mohammad-Panah Raha, Harrison Rene, Dhani Sonja, Ackerley Cameron, Huan Ling-Jun, Wang Yanchun, Bear Christine E

Abstract excerpt

Mutations in the gene coding for the chloride channel ClC-5 cause Dent's disease, a disease associated with proteinuria and renal stones. Studies in ClC-5 knockout mice suggest that this phenotype is related to defective endocytosis of low molecular weight proteins and membrane proteins by the renal proximal tubule. In this study, confocal micrographs of proximal tubules and cultured epithelial cells revealed...

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Identifiers

PMID: 12746443
DOI: 10.1074/jbc.M304357200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

The chloride channel ClC-4 contributes to endosomal acidification and trafficking.PMID 12746443Read ↗

ClC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells.Semantic proximity Read ↗

ClC transporters: discoveries and challenges in defining the mechanisms underlying function and regulation of ClC-5.Semantic proximity Read ↗

ClC-5: role in endocytosis in the proximal tubule.Semantic proximity Read ↗

A novel CLCN5 pathogenic mutation supports Dent disease with normal endosomal acidification.Semantic proximity Read ↗

TMEM9 and SEC22B interact with ClC-5 to shape renal proximal tubule function and Dent’s Disease type I pathogenesisSemantic proximity Read ↗

Receptor-mediated endocytosis and endosomal acidification is impaired in proximal tubule epithelial cells of Dent disease patients.Semantic proximity Read ↗

ClC-5 chloride channel and kidney stones: what is the link?Semantic proximity Read ↗

Heterogeneity in the processing of CLCN5 mutants related to Dent disease.Semantic proximity Read ↗

A pure chloride channel mutant of CLC-5 causes Dent's disease via insufficient V-ATPase activation.Semantic proximity Read ↗

Characterization of Dent's disease mutations of CLC-5 reveals a correlation between functional and cell biological consequences and protein structureSemantic proximity Read ↗

Functional characterization of a novel missense CLCN5 mutation causing alterations in proximal tubular endocytic machinery in Dent's disease.Semantic proximity Read ↗

ClC-5 mutations associated with Dent's disease: a major role of the dimer interface.Semantic proximity Read ↗

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