Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity

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Abstract

It is well-known that the rapid flow of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). However, the mechanisms that allow cells to quickly respond to a changing osmotic environment are less well established. Using GFP-AQP fusion proteins expressed in HEK293 cells, we demonstrate the reversible manipulation of cellular trafficking of AQP1. AQP1 trafficking was mediated by the tonicity of the cell environment in a specific PKC- and microtubule-dependent manner. This suggests that the increased level of water transport following osmotic change may be due a phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.

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Original languageEnglish
Pages (from-to)821-823
Number of pages3
JournalBiochemistry
Volume49
Issue number5
DOIs
Publication statusPublished - 9 Feb 2010

    Keywords

  • cell, membrane proteins, aquaporins, GFP-AQP fusion proteins, HEK293 cells, manipulation, cellular trafficking of AQP1

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