MCB Accepts, published online ahead of print on 19 October 2009

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Mol. Cell. Biol. doi:10.1128/MCB.00814-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

A role of VAMP8/endobrevin in surface deployment of the water channel aquaporin 2

Cheng-Chun Wang, Chee Peng Ng, Hong Shi, Hwee Chien Liew, Ke Guo, Qi Zeng, and Wanjin Hong^*

Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673, Singapore

^* To whom correspondence should be addressed. Email: mcbhwj{at}imcb.a-star.edu.sg.

The vesicle-associated-membrane-protein 8 (VAMP8) is highly expressed in the kidney, but the exact physiological and molecular functions executed by this v-SNARE protein in nephrons remain elusive. Here we show that depletion of VAMP8 in mice resulted in hydronephrosis. Furthermore, the vasopressin-responsive water channel aquaporin 2 (AQP2) was increased by three-to-five folds in VAMP8-null mice. Forskolin and [desamino-Cys¹, D-Arg⁸]-vasopressin (DDAVP)-induced AQP2 exocytosis was impaired in VAMP8-null collecting duct cells. VAMP8 was revealed to co-localize with AQP2 on intracellular vesicles and to interact with the plasma membrane t-SNARE proteins syntaxin4 and syntaxin3, suggesting that VAMP8 may mediate regulated fusion of AQP2-positive vesicles with the plasma membrane.