Functional characterization of (pro)renin receptor in association with V-ATPase

Front Biosci (Landmark Ed). 2011 Jun 1;16(9):3216-23. doi: 10.2741/3907.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Animals
  • Embryonic Development / physiology
  • Female
  • Gene Expression
  • Humans
  • Male
  • Models, Molecular
  • Pregnancy
  • Prorenin Receptor
  • Protein Interaction Domains and Motifs
  • Receptors, Cell Surface / chemistry
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / metabolism*
  • Signal Transduction
  • Tissue Distribution
  • Vacuolar Proton-Translocating ATPases / chemistry
  • Vacuolar Proton-Translocating ATPases / genetics
  • Vacuolar Proton-Translocating ATPases / metabolism*

Substances

  • ATP6AP1 protein, human
  • ATP6AP2 protein, human
  • Atp6ap1 protein, mouse
  • Receptors, Cell Surface
  • Vacuolar Proton-Translocating ATPases
  • Prorenin Receptor