Abstract:
: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.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Wang CC,Ng CP,Shi H,Liew HC,Guo K,Zeng Q,Hong Wdoi
10.1128/MCB.00814-09subject
Has Abstractpub_date
2010-01-01 00:00:00pages
333-43issue
1eissn
0270-7306issn
1098-5549pii
MCB.00814-09journal_volume
30pub_type
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