Membrane trafficking of Aquaporin 1 is mediated by Protein Kinase C via microtubules and regulated by tonicity.

CONNER, Matthew, CONNER, Alex C., BROWN, James E. P. and BILL, Roslyn M. (2010). Membrane trafficking of Aquaporin 1 is mediated by Protein Kinase C via microtubules and regulated by tonicity. Biochemistry, 49 (5), 821-823.

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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.

Item Type:	Article
Research Institute, Centre or Group:	Biomedical Research Centre
Identification Number:	10.1021/bi902068b
Depositing User:	Rebecca Jones
Date Deposited:	01 Mar 2012 10:09
Last Modified:	01 Mar 2012 10:09
URI:	http://shura.shu.ac.uk/id/eprint/4872

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