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J. Biol. Chem., Vol. 279, Issue 30, 31973-31982, July 23, 2004
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¶



From the
Laboratory of Immunogenetics, NIAID, National Institutes of Health, Rockville, Maryland 20852, the
Department of Medicine and Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, and the ||Memorial Sloan Kettering Cancer Center, Radiochemistry Core Facility, New York, New York 10021
Signaling through the B cell antigen receptor (BCR) is amplified and prolonged by coligation of the BCR to the CD19/CD21/CD81 coreceptor complex. Coligation is induced during immune responses by the simultaneous binding of complement-tagged antigens to the complement receptor, CD21, and to the BCR. Enhanced signaling is due in part to the ability of the CD19/CD21/CD81 complex to stabilize the BCR in sphingolipid- and cholesterol-rich membrane microdomains termed lipid rafts. The tetraspanin CD81 is essential for the raft-stabilizing function of the coreceptor. Here we show that coligation of the BCR and the CD19/CD21/CD81 complex leads to selective, rapid, and reversible palmitoylation of CD81 and that palmitoylation is necessary for the raft stabilizing function of the CD19/CD21/CD81 complex. Inducible palmitoylation may represent a novel mechanism by which tetraspanins function to facilitate lipid raft-dependent receptor signaling.
Received for publication, April 21, 2004 , and in revised form, May 24, 2004.
* 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.
¶ Current address: Molecular Inflammation Section, NIAMS, NIH, Bethesda, MD 20892.
** Current address: M. D. Anderson Cancer Center, Houston, TX 77030.

To whom correspondence should be addressed: Laboratory of Immunogenetics, NIAID/NIH/Twinbrook II, 12441 Parklawn Dr., Rm. 200B, MSC 8180, Rockville, MD 20852. Tel.: 301-496-9589; Fax: 301-402-0259; E-mail: spierce{at}nih.gov.
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