Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity.
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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 language | English |
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Pages (from-to) | 821-3 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 49 |
Issue number | 5 |
Publication status | Published - 9 Feb 2010 |