| Literature DB >> 16624255 |
Abstract
Trafficking of water channel aquaporin-2 (AQP2) to the apical membrane is critical to water reabsorption in renal collecting ducts and its regulation maintains body water homeostasis. However, exact molecular mechanisms which recruit AQP2 are unknown. Recent studies highlighted a key role for spatial and temporal regulation of actin dynamics in AQP2 trafficking. We have recently identified AQP2-binding proteins which directly regulate this trafficking: SPA-1, a GTPase-activating protein (GAP) for Rap1, and cytoskeletal protein actin. In addition, a multiprotein "force generator" complex which directly binds to AQP2 has been discovered. This review summarizes recent advances related to the mechanism for AQP2 trafficking.Entities:
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Year: 2006 PMID: 16624255 DOI: 10.1016/j.bbamem.2006.03.004
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002