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Molecular and Cellular Biology, November 2005, p. 10087-10096, Vol. 25, No. 22
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.22.10087-10096.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Caveolin-1 Is Not Essential for Biosynthetic Apical Membrane Transport

Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany,¹ University of Heidelberg, Im Neuenheimer Feld 345, 69120 Heidelberg, Germany,² Institute of Anatomy, Medical Faculty Carl Gustav Carus, Dresden University of Technology, Fiedlerstrasse 42, 01307 Dresden, Germany³

Received 30 May 2005/ Returned for modification 10 July 2005/ Accepted 28 August 2005

Caveolin-1 has been implicated in apical transport of glycosylphosphatidylinositol (GPI)-anchored proteins and influenza virus hemagglutinin (HA). Here we have studied the role of caveolin-1 in apical membrane transport by generating caveolin-1-deficient Madin-Darby canine kidney (MDCK) cells using retrovirus-mediated RNA interference. The caveolin-1 knockdown (cav1-KD) MDCK cells were devoid of caveolae. In addition, caveolin-2 was retained in the Golgi apparatus in cav1-KD MDCK cells. However, we found no significant alterations in the apical transport kinetics of GPI-anchored proteins or HA upon depletion of caveolin-1. Similar results were obtained using embryonic fibroblasts from caveolin-1-knockout mice. Thus, we conclude that caveolin-1 does not play a major role in lipid raft-mediated biosynthetic membrane trafficking.

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