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Article

A role for CBS domain 2 in trafficking of chloride channel CLC-5.

Biochemical and biophysical research communications - 17 Oct 2003

Carr Georgina, Simmons Nicholas, Sayer John

Abstract excerpt

CLC-5 is a member of the CLC family of voltage-gated chloride channels. Mutations disrupting CLC-5 lead to Dent's disease, an X-linked renal tubular disorder, characterised by low molecular weight proteinuria, hypercalciuria, nephrocalcinosis, and renal stones. Sequence analysis of CLC-5 reveals a 746 amino acid protein with an intracellular amino-terminus, transmembrane spanning domains, and two CBS domains...

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Source

Identifiers

PMID: 14521953
DOI: 10.1016/j.bbrc.2003.09.057

Genes

CLC
CBS

Provenance

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.

Related research

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Research trail→

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A role for CBS domain 2 in trafficking of chloride channel CLC-5.PMID 14521953Read ↗

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

Novel truncating mutations in the ClC-5 chloride channel gene in patients with Dent's disease.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 ↗

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

Characterization of renal chloride channel (CLCN5) mutations in Dent's disease.Semantic proximity Read ↗

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

Functional and transport analyses of CLCN5 genetic changes identified in Dent disease patients.Semantic proximity Read ↗

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

A novel likely pathogenic CLCN5 variant in Dent’s diseaseSemantic proximity Read ↗

Novel CLCN5 mutations in patients with Dent's disease result in altered ion currents or impaired exchanger processing.Semantic proximity Read ↗

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

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