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Originally published as Biophys J. BioFAST on November 2, 2007.
doi:10.1529/biophysj.107.104893
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Biophysical Journal 94:671-678 (2008)
© 2008 The Biophysical Society

Translocation of Aquaporin-Containing Vesicles to the Plasma Membrane Is Facilitated by Actomyosin Relaxation

Christoph Riethmüller *, Hans Oberleithner *, Marianne Wilhelmi *, Jonas Franz *, Eberhard Schlatter {dagger}, Jens Klokkers {dagger} and Bayram Edemir {dagger}

* Institute of Physiology II and {dagger} Department of Internal Medicine D, Experimental Nephrology, University of Münster, Munich, Germany

Correspondence: Address reprint requests to Dr. Christoph Riethmüller, Institute of Physiology II, University of Münster, Robert-Koch-Strasse 27 b, D-48149 Munich, Germany. Tel.: 0049-251-835-5323; Fax: 0049-251-835-5331; E-mail: chrth{at}uni-muenster.de.

Docking and fusion of vesicles to the plasma membrane is a fundamental process in living cells. An established model for the trafficking of vesicles is based on primary epithelial cells from the collecting duct of the nephron. Upon stimulation with the signaling peptide arginine-vasopressin (AVP), aquaporin-containing vesicles are directed to the plasma membrane. Since aquaporin 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 depolymerization of F-actin to facilitate the movement of vesicles to the membrane. Since F-actin is the major component of cytoskeletal restoring forces, AVP-stimulated cells can be expected to lose rigidity. Here, we used atomic force microscopy 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 the addition of AVP. The data demonstrate that not the depolymerization of actin but a relaxation of actomyosin interaction facilitates vesicle translocation.


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