IMR Press / FBL / Volume 16 / Issue 9 / DOI: 10.2741/3907

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Functional characterization of (pro)renin receptor in association with V-ATPase
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1 Department of Endocrinology, Metabolism, and Nephrology, Keio University School of Medicine, Tokyo, 160-8582, Japan
2 Department of Endocrinology & Anti-Aging Medicine and Internal Medicine, Keio University School of Medicine, Tokyo, 160-8582, Japan
Academic Editor:Fumiaki Suzuki
Front. Biosci. (Landmark Ed) 2011, 16(9), 3216–3223;
Published: 1 June 2011
(This article belongs to the Special Issue Handle region peptide and prorenin receptor)

The (pro)renin receptor ((P)RR) is a unique molecule that binds prorenin and renin in tissues, not only leading to their activation, but also inducing intracellular signaling. As a key player in the local renin-angiotensin system, (P)RR activation plays an important role in the development of cardiac fibrosis and proteinuria in hypertension and diabetes. Intriguingly, the fragment (P)RR is also called ATP6AP2 because it has been shown to be associated with vacuolar-type H+-ATPase (V-ATPase). The V-ATPase is a multi-subunit proton pump involved in diverse and fundamental cellular processes, including receptor-mediated endocytosis, processing of proteins and signaling molecules, membrane sorting and trafficking, and activation of lysosomal enzymes. The role of (P)RR in the function of the V-ATPase is implicated in the previous findings and vigorously investigated in the recent studies. Furthermore, the novel function of the (P)RR as an adaptor protein between the Wnt receptor complex and the V-ATPase was discovered. Thus, the (P)RR is a multi-functional molecule that shows the complex structure and behaviour. This review highlights the current insights and the future perspectives in research regarding the (P)RR and mammalian V-ATPase.

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