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

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 Biol

authors

Wang CC,Ng CP,Shi H,Liew HC,Guo K,Zeng Q,Hong W

doi

10.1128/MCB.00814-09

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

333-43

issue

1

eissn

0270-7306

issn

1098-5549

pii

MCB.00814-09

journal_volume

30

pub_type

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