Peer-review started: August 12, 2016
First decision: September 30, 2016
Revised: October 12, 2016
Accepted: November 1, 2016
Article in press: November 2, 2016
Published online: January 6, 2017
Processing time: 138 Days and 7 Hours
Dent’s disease is an X-linked renal tubulopathy characterized by low molecular weight proteinuria, hypercalciuria and progressive renal failure. Disease aetiology is associated with mutations in the CLCN5 gene coding for the electrogenic 2Cl-/H+ antiporter chloride channel 5 (CLC-5), which is expressed in the apical endosomes of renal proximal tubules with the vacuolar type H+-ATPase (V-ATPase). Initially identified as a member of the CLC family of Cl- channels, CLC-5 was presumed to provide Cl- shunt into the endosomal lumen to dissipate H+ accumulation by V-ATPase, thereby facilitating efficient endosomal acidification. However, recent findings showing that CLC-5 is in fact not a Cl- channel but a 2Cl-/H+ antiporter challenged this classical shunt model, leading to a renewed and intense debate on its physiological roles. Cl- accumulation via CLC-5 is predicted to play a critical role in endocytosis, as illustrated in mice carrying an artificial Cl- channel mutation E211A that developed defective endocytosis but normal endosomal acidification. Conversely, a recent functional analysis of a newly identified disease-causing Cl- channel mutation E211Q in a patient with typical Dent’s disease confirmed the functional coupling between V-ATPase and CLC-5 in endosomal acidification, lending support to the classical shunt model. In this editorial, we will address the current recognition of the physiological role of CLC-5 with a specific focus on the functional coupling of V-ATPase and CLC-5.
Core tip: Chloride channel 5 (CLC-5) mutations cause Dent’s disease, which is characterized by renal proximal tubulopathy due to defective endocytosis. Recent revelations that CLC-5 is a 2Cl-/H+ antiporter and not a Cl- channel challenged the classical model proposing CLC-5 as a Cl- shunt to facilitate V-ATPase-mediated endosomal acidification. Therefore, physiological roles of CLC-5 and its interaction with V-ATPase in endosomal acidification and/or endocytosis are intensely debated. Recent functional analysis of a novel pure Cl- channel mutant from a Dent’s disease patient indicated a possible functional coupling between V-ATPase and CLC-5 not only in endosomal acidification but also at the plasma membrane.