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Volume 270, Number 12, Issue of March 24, 1995 pp. 6838-6842
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Caveolin Is Palmitoylated on Multiple Cysteine Residues
PALMITOYLATION IS NOT NECESSARY FOR LOCALIZATION OF CAVEOLIN TO CAVEOLAE (*)

(Received for publication, December 2, 1994; and in revised form, January 24, 1995)

Dennis J. Dietzen ,  W. Randall Hastings ,  Douglas M. Lublin (§)

From the Departments of Pathology and Internal Medicine, Division of Laboratory Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

ABSTRACT

Caveolae are subdomains of the plasma membrane which concentrate cholesterol, glycosphingolipids, and glycosylphosphatidylinositol-linked proteins. It has recently been demonstrated that specific members of the Src family of protein tyrosine kinases require palmitoylation of NH(2)-terminal cysteine residues to localize in caveolae. Here we report that caveolin, an integral membrane protein which forms part of the coat of caveolae, also incorporates palmitate through linkage to cysteine residues. Caveolin contains only three cysteine residues which are all located on the COOH-terminal side of the hydrophobic transmembrane region. Immunofluorescent staining of cells transfected with caveolin indicated that, like the NH(2) terminus, this COOH-terminal region is located on the cytoplasmic side of the plasma membrane. Studies of cysteine substitution mutants showed that all three cysteines are capable of incorporating palmitate and that the juxtamembrane Cys residue is the predominant site of palmitoylation. Simultaneous mutation of all three cysteine residues in caveolin resulted in the loss of ability to incorporate palmitate; however, this did not affect localization of the protein. Thus, palmitoylation of cysteine residues in nonmembrane spanning Src family protein tyrosine kinases has different consequences than in the transmembrane protein caveolin.

FOOTNOTES

*
This work was supported by National Institutes of Health Grant GM 41297 (to D. M. Lublin), American Cancer Society Grant BE-201 (to D. M. Lublin), and National Institutes of Health Training Grant HL 07038 (to D. J. Dietzen). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked ``advertisement'' in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§
To whom correspondence should be addressed: Dept. of Pathology, Washington University School of Medicine, 660 S. Euclid Ave., Box 8118, St. Louis, MO 63110. Tel.: 314-362-8849; Fax: 314-362-3016.

(^1)
The abbreviations used are: GPI, glycosylphosphatidylinositol; DAF, decay accelerating factor; MDCK, Madin-Darby canine kidney cells; PAGE, polyacrylamide gel electrophoresis.

(^2)
J. Kwong, D. J. Dietzen, and D. M. Lublin, unpublished observation.

©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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