Membrane Trafficking of Aquaporin 1 Is Mediated by Protein Kinase C via Microtubules and Regulated by Tonicity

被引：47

作者：

Conner, Matthew T. ^{[1
]}

Conner, Alex C. ^{[2
]}

Brown, James E. P. ^{[1
]}

Bill, Roslyn M. ^{[1
]}

机构：

[1] Aston Univ, Birmingham B4 7ET, W Midlands, England

[2] Univ Warwick, Warsaw Med Sch, Coventry CV4 7AL, W Midlands, England

来源：

BIOCHEMISTRY | 2010年 / 49卷 / 05期

关键词：

PLASMA-MEMBRANE; WATER PERMEABILITY; CHANNEL; TRANSLOCATION; RESOLUTION; TRANSPORT; MICE;

D O I：

10.1021/bi902068b

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：821 / 823

页数：3

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