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

Research output: Contribution to journalArticle

Authors

Colleges, School and Institutes

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.

Details

Original languageEnglish
Pages (from-to)821-3
Number of pages3
JournalBiochemistry
Volume49
Issue number5
Publication statusPublished - 9 Feb 2010