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

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Conner, Matthew T., 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, Vol.49 (No.5). pp. 821-823. doi:10.1021/bi902068b

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Official URL: http://dx.doi.org/10.1021/bi902068b

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Abstract

It is well-known that the rapid now 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 it phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Medicine > Warwick Medical School
Journal or Publication Title: Biochemistry
Publisher: American Chemical Society
ISSN: 0006-2960
Official Date: 9 February 2010
Dates:
DateEvent
9 February 2010Published
Volume: Vol.49
Number: No.5
Number of Pages: 3
Page Range: pp. 821-823
DOI: 10.1021/bi902068b
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: EDICT
Grant number: 201924

Data sourced from Thomson Reuters' Web of Knowledge

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