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| Item Type: | Article |
|---|---|
| Title: | A role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle |
| Creators Name: | Nedvetsky, P.I., Stefan, E., Frische, S., Santamaria, K., Wiesner, B., Valenti, G., Hammer, J.A., Nielsen, S., Goldenring, J.R., Rosenthal, W. and Klussmann, E. |
| Abstract: | 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. |
| Keywords: | AQP2 Recycling, Aquaporin, Principal Cells, Rab11, Vasopressin, Animals, Rats |
| Source: | Traffic |
| ISSN: | 1398-9219 |
| Publisher: | Blackwell Synergy |
| Volume: | 8 |
| Number: | 2 |
| Page Range: | 110-123 |
| Date: | February 2007 |
| Official Publication: | https://doi.org/10.1111/j.1600-0854.2006.00508.x |
| PubMed: | View item in PubMed |
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