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J. Biol. Chem., Vol. 282, Issue 10, 7232-7241, March 9, 2007
Identification of a Novel Domain at the N Terminus of Caveolin-1 That Controls Rear Polarization of the Protein and Caveolae Formation*![]() ¶ ||![]() ¶1
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When cells are migrating, caveolin-1, the principal protein component of caveolae, is excluded from the leading edge and polarized at the cell rear. The dynamic feature depends on a specific sequence motif that directs intracellular trafficking of the protein. Deletion mutation analysis revealed a putative polarization domain at the N terminus of caveolin-1, between amino acids 3260. Alanine substitution identified a minimal sequence of 10 residues (46TKEIDLVNRD55) necessary for caveolin-1 rear polarization. Interestingly, deletion of amino acids 160 did not prevent the polarization of caveolin-1 in human umbilical vein endothelial cells or wild-type mouse embryonic fibroblasts because of an interaction of Cav61178 mutant with endogenous caveolin-1. Surprisingly, expression of the depolarization mutant in caveolin-1 null cells dramatically impeded caveolae formation. Furthermore, knockdown of caveolae formation by methyl-
Received for publication, August 3, 2006 , and in revised form, December 18, 2006. * This work was supported by Grant RR016440 from the National Institutes of Health (to J. L. and D. C. F.) and the Sara and James Allen Lung Cancer Funds (to J. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. 1 To whom correspondence should be addressed: West Virginia University Health Science Center, Dept. of Physiology and Pharmacology, P. O. Box 9229, Morgantown, WV 26506-9229. Tel.: 304-293-1503; Fax: 304-293-3850; E-mail: junliu{at}hsc.wvu.edu.
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