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Biophys. J. BioFAST: First Published November 2, 2007. doi:10.1529/biophysj.107.104893
© 2007 by the Biophysical Society.

A more recent version of this article appeared on January 15, 2008.
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CELL BIOPHYSICS

TRANSLOCATION OF AQUAPORIN-CONTAINING VESICLES TO THE PLASMA MEMBRANE IS FACILITATED BY ACTOMYOSIN RELAXATION

Christoph P Riethmuller 1*, Hans Oberleithner 1, Marianne Wilhelmi 1, Jonas Franz 1, Eberhard Schlatter 1, Jens Klokkers 1 and Bayram Edemir 1

1 University of Munster

* To whom correspondence should be addressed. E-mail: chrth{at}uni-muenster.de.

Submitted on January 19, 2007
Revised on February 25, 2007
Accepted on 16 July 2007


  Abstract
Docking and fusion of vesicles to the plasma membrane is a fundamental process in living cells. An established model for trafficking of vesicles bases on primary epithelial cells from the collecting duct of the nephron (IMCD cells). Upon stimulation with the signaling peptide arginine-vasopressin (AVP), aquaporin (AQP) containing vesicles are directed to the plasma membrane. Since AQP selectively enhances the water-permeability of plasma membranes, this process helps to balance the water content of the organism. A mechanism has been suggested involving local depolymerisation of F-actin to facilitate the movement of vesicles to the membrane (1). Since F-actin is the major component of cytoskeletal restoring forces, AVP-stimulated cells can be expected to lose rigidity. Here, we used AFM force-mapping to test whether AVP alters cell stiffness. The Young's Modulus of living epithelial cells at 37°C was continuously monitored yielding a 51% decrease of Young's Modulus after addition of AVP. The data demonstrate that not depolymerisation of actin, but a relaxation of actomyosin interaction facilitates vesicle translocation.

Key Words: AFM, Aquaporin, Elasticity, Epithelial cells, Force Mapping, Kidney




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Copyright © 2007 by the Biophysical Society.