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A Role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle.

Authors: Nedvetsky, PI  Stefan, E  Frische, S  Santamaria, K  Wiesner, B  Valenti, G  Hammer JA, 3RD  Nielsen, S  Goldenring, JR  Rosenthal, W  Klussmann, E 
Citation: Nedvetsky PI, etal., Traffic. 2007 Feb;8(2):110-23. Epub 2006 Dec 6.
Pubmed: (View Article at PubMed) PMID:17156409
DOI: Full-text: DOI:10.1111/j.1600-0854.2006.00508.x

Arginine-vasopressin (AVP) regulates water reabsorption in renal collecting duct principal cells. Its binding to Gs-coupled vasopressin V2 receptors increases cyclic AMP (cAMP) and subsequently elicits the redistribution of the water channel aquaporin-2 (AQP2) from intracellular vesicles into the plasma membrane (AQP2 shuttle), thereby facilitating water reabsorption from primary urine. The AQP2 shuttle is a paradigm for cAMP-dependent exocytic processes. Using sections of rat kidney, the AQP2-expressing cell line CD8, and primary principal cells, we studied the role of the motor protein myosin Vb, its vesicular receptor Rab11, and the myosin Vb- and Rab11-binding protein Rab11-FIP2 in the AQP2 shuttle. Myosin Vb colocalized with AQP2 intracellularly in resting and at the plasma membrane in AVP-treated cells. Rab11 was found on AQP2-bearing vesicles. A dominant-negative myosin Vb tail construct and Rab11-FIP2 lacking the C2 domain (Rab11-FIP2-DeltaC2), which disrupt recycling, caused condensation of AQP2 in a Rab11-positive compartment and abolished the AQP2 shuttle. This effect was dependent on binding of myosin Vb tail and Rab11-FIP2-DeltaC2 to Rab11. In summary, we identified myosin Vb as a motor protein involved in AQP2 recycling and show that myosin Vb- and Rab11-FIP2-dependent recycling of AQP2 is an integral part of the AQP2 shuttle.

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RGD Object Information
RGD ID: 2312655
Created: 2009-08-27
Species: All species
Last Modified: 2009-08-27
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.