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.

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1021/bi902068b
Link to published version:: 10.1021/bi902068b

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

Actions (login required)

View Item

Downloads

Downloads per month over past year

View more statistics