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

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Conner MT,Conner AC,Brown JE,Bill RM

doi

10.1021/bi902068b

subject

Has Abstract

pub_date

2010-02-09 00:00:00

pages

821-3

issue

5

eissn

0006-2960

issn

1520-4995

journal_volume

49

pub_type

杂志文章

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