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J. Biol. Chem., Vol. 277, Issue 5, 3371-3379, February 1, 2002
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From the Caveolae are flask-shaped invaginations at the
plasma membrane that constitute a subclass of detergent-resistant
membrane domains enriched in cholesterol and sphingolipids and that
express caveolin, a caveolar coat protein. Autocrine motility factor
receptor (AMF-R) is stably localized to caveolae, and the cholesterol
extracting reagent, methyl-
Caveolin-1 Is a Negative Regulator of Caveolae-mediated
Endocytosis to the Endoplasmic Reticulum*
§,,
Department of Pathology and Cell Biology,
Université de Montréal, Montreal, Quebec H3C 3J7, Canada
and the ¶ Department of Pharmacology, Hebrew University of
Jerusalem, Jerusalem 91120, Israel
-cyclodextrin, inhibits its
internalization to the endoplasmic reticulum implicating caveolae
in this distinct receptor-mediated endocytic pathway. Curiously, the
rate of methyl--cyclodextrin-sensitive endocytosis of AMF-R to the
endoplasmic reticulum is increased in ras- and
abl-transformed NIH-3T3 cells that express
significantly reduced levels of caveolin and few caveolae.
Overexpression of the dynamin K44A dominant negative mutant via an
adenovirus expression system induces caveolar invaginations sensitive
to methyl--cyclodextrin extraction in the transformed cells without
increasing caveolin expression. Dynamin K44A expression further
inhibits AMF-R-mediated endocytosis to the endoplasmic reticulum in
untransformed and transformed NIH-3T3 cells. Adenoviral expression of
caveolin-1 also induces caveolae in the transformed NIH-3T3 cells and
reduces AMF-R-mediated endocytosis to the endoplasmic reticulum to
levels observed in untransformed NIH-3T3 cells. Cholesterol-rich
detergent-resistant membrane domains or glycolipid rafts therefore
invaginate independently of caveolin-1 expression to form
endocytosis-competent caveolar vesicles via rapid
dynamin-dependent detachment from the plasma membrane.
Caveolin-1 stabilizes the plasma membrane association of caveolae and
thereby acts as a negative regulator of the caveolae-mediated endocytosis of AMF-R to the endoplasmic reticulum.
*
This study was supported in part by a grant from the
Canadian Institutes for Health Research (CIHR).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a CIHR Investigator award. To whom correspondence
should be addressed: Dépt. de Pathologie et Biologie Cellulaire, Université de Montréal, C. P. 6128, Succursale A,
Montréal, Québec H3C 3J7, Canada. Tel.: 514-343-6291; Fax:
514-343-2459; E-mail: ivan.robert.nabi@umontreal.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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