| First Author | Wang CC | Year | 2010 |
| Journal | Mol Cell Biol | Volume | 30 |
| Issue | 1 | Pages | 333-43 |
| PubMed ID | 19841070 | Mgi Jnum | J:156248 |
| Mgi Id | MGI:4420158 | Doi | 10.1128/MCB.00814-09 |
| Citation | Wang CC, et al. (2010) A role for VAMP8/endobrevin in surface deployment of the water channel aquaporin 2. Mol Cell Biol 30(1):333-43 |
| abstractText | 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 the depletion of VAMP8 in mice resulted in hydronephrosis. Furthermore, the level of the vasopressin-responsive water channel aquaporin 2 (AQP2) was increased by three- to fivefold in VAMP8-null mice. Forskolin and [desamino-Cys(1), D-Arg(8)]-vasopressin (DDAVP)-induced AQP2 exocytosis was impaired in VAMP8-null collecting duct cells. VAMP8 was revealed to colocalize with AQP2 on intracellular vesicles and to interact with the plasma membrane t-SNARE proteins syntaxin4 and syntaxin3, suggesting that VAMP8 mediates the regulated fusion of AQP2-positive vesicles with the plasma membrane. |
