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

Matthew T. Conner, Alex C. Conner, James Brown, Roslyn M. Bill

Research output: Contribution to journalArticle

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.
LanguageEnglish
Pages821-823
Number of pages3
JournalBiochemistry
Volume49
Issue number5
DOIs
Publication statusPublished - 9 Feb 2010

Fingerprint

Aquaporin 1
Aquaporins
Microtubules
Protein Kinase C
Membranes
Phosphorylation
Flow of water
Membrane Proteins
Fusion reactions
Water
HEK293 Cells
Proteins

Keywords

  • cell
  • membrane proteins
  • aquaporins
  • GFP-AQP fusion proteins
  • HEK293 cells
  • manipulation
  • cellular trafficking of AQP1

Cite this

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Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity. / Conner, Matthew T.; Conner, Alex C.; Brown, James; Bill, Roslyn M.

In: Biochemistry, Vol. 49, No. 5, 09.02.2010, p. 821-823.

Research output: Contribution to journalArticle

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