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

Research output not available from this repository, contact author.

Request Changes to record.

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:	Date Event 9 February 2010 Published
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

Request changes or add full text files to a record

Repository staff actions (login required)

View Item