Trafficking mechanism of water channel aquaporin-2

Biol Cell. 2005 Dec;97(12):885-92. doi: 10.1042/BC20040120.

Abstract

Targeted positioning of the water channel AQP2 (aquaporin-2) strictly regulates body water homoeostasis. Trafficking of AQP2 to the apical membrane is critical for the reabsorption of water in renal collecting ducts. In addition to the cAMP-mediated effect of vasopressin on AQP2 trafficking to the apical membrane, other signalling cascades can also induce this sorting. Recently, AQP2-binding proteins which could regulate this trafficking have been discovered; SPA-1 (signal-induced proliferation-associated gene-1), a GAP (GTPase-activating protein) for Rap1, and the cytoskeletal protein actin. This review summarizes recent advances related to the trafficking mechanisms of AQP2.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism
  • Animals
  • Aquaporin 2 / metabolism*
  • Clathrin / metabolism
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Cytoskeleton / chemistry
  • Cytoskeleton / metabolism
  • Endocytosis
  • GTPase-Activating Proteins / metabolism
  • Homeostasis
  • Humans
  • Kidney Tubules, Collecting / physiology
  • Nuclear Proteins / metabolism
  • Phosphorylation
  • Protein Transport*
  • Signal Transduction
  • Vasopressins / physiology

Substances

  • Actins
  • Aquaporin 2
  • Clathrin
  • GTPase-Activating Proteins
  • Nuclear Proteins
  • SIPA1 protein, human
  • Vasopressins
  • Cyclic AMP-Dependent Protein Kinases