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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 ISSN 0006-2960.
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Official URL: http://dx.doi.org/10.1021/bi902068b
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 | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School | ||||
Journal or Publication Title: | Biochemistry | ||||
Publisher: | American Chemical Society | ||||
ISSN: | 0006-2960 | ||||
Official Date: | 9 February 2010 | ||||
Dates: |
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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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