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- W2151062696 abstract "Trafficking of water channel aquaporin-2 (AQP2) to the apical membrane and its vasopressin and protein kinase A (PKA)-dependent regulation in renal collecting ducts is critical for body water homeostasis. We previously identified an AQP2 binding protein complex including actin and tropomyosin-5b (TM5b). We show that dynamic interactions between AQP2 and the actin cytoskeleton are critical for initiating AQP2 apical targeting. Specific binding of AQP2 to G-actin in reconstituted liposomes is negatively regulated by PKA phosphorylation. Dual color fluorescence cross-correlation spectroscopy reveals local AQP2 interaction with G-actin in live epithelial cells at single-molecule resolution. Cyclic adenosine monophosphate signaling and AQP2 phosphorylation release AQP2 from G-actin. In turn, AQP2 phosphorylation increases its affinity to TM5b, resulting in reduction of TM5b bound to F-actin, subsequently inducing F-actin destabilization. RNA interference-mediated knockdown and overexpression of TM5b confirm its inhibitory role in apical trafficking of AQP2. These findings indicate a novel mechanism of channel protein trafficking, in which the channel protein itself critically regulates local actin reorganization to initiate its movement." @default.
- W2151062696 created "2016-06-24" @default.
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- W2151062696 date "2008-08-04" @default.
- W2151062696 modified "2023-10-01" @default.
- W2151062696 title "Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking" @default.
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- W2151062696 doi "https://doi.org/10.1083/jcb.200709177" @default.
- W2151062696 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2500142" @default.
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