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J. Biol. Chem., Vol. 279, Issue 32, 33413-33420, August 6, 2004

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Syk-mediated Tyrosine Phosphorylation Is Required for the Association of Hematopoietic Lineage Cell-specific Protein 1 with Lipid Rafts and B Cell Antigen Receptor Signalosome Complex^*

Jian-Jiang Hao, Gregory B. Carey¶||, and Xi Zhan**

From the Departments of Experimental Pathology and ^¶Immunology, Holland Laboratory, American Red Cross, Rockville, Maryland 20855

Hematopoietic lineage cell-specific protein 1 (HS1) is an F-actin- and actin-related proteins 2 and 3 (Arp2/3)-binding protein that undergoes a rapid tyrosine phosphorylation upon B cell antigen receptor (BCR) activation. Density gradient centrifugation of Triton X-100 lysates from B lymphocytes demonstrated that HS1 was translocated in response to BCR cross-linking into lipid raft microdomain along with Arp2/3 complex and Wiskott-Aldrich syndrome protein. HS1-green fluorescent protein was localized in membrane patches enriched with GM1 gangliosides and BCR in the cells treated with anti-IgM antibody. Colocalization of HS1-green fluorescent protein with BCR was also correlated with tyrosine phosphorylation of HS1. Interestingly a murine HS1 mutant at the tyrosine residues Tyr³⁸⁸ and Tyr⁴⁰⁵ targeted by Syk failed to respond to BCR cross-linking for either translocation into lipid rafts or colocalization with BCR within cells. Furthermore HS1 was unable to translocate into lipid rafts in a chicken B cell line deficient in Syk. Reintroducing a Syk construct into the Syk knock-out cells recovered effectively both tyrosine phosphorylation and translocation of HS1 into lipid rafts. In contrast, translocation of HS1 into rafts was normal in a Lyn knock-out B cell line, and an HS1 mutant at the tyrosine residue Tyr²²² targeted by Lyn maintained the ability to partition into rafts upon BCR cross-linking. These data indicate that Syk plays an important role in the translocation of HS1 into lipid rafts and may be responsible for actin assembly recruitment to rafts and subsequent antigen presentations.

Received for publication, December 11, 2003 , and in revised form, May 7, 2004.

^* This work was supported by National Institutes of Health Grants R01 HL 52753-10 and R01 CA 91984-02, Department of Defense Grant DAMD 17-01-1-0125, and American Heart Association Grant 0040135N (to X. Z.). 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.

Present address: Dept. of Pathology, Greenebaum Cancer Center, University of Maryland School of Medicine, 15601 Crabbs Branch Way, Rockville, MD 20855.

^|| Present address: Dept. of Microbiology and Immunology, University of Maryland School of Medicine, 15601 Crabbs Branch Way, Rockville, MD 20855.

^** To whom correspondence should be addressed: Dept. of Pathology, Greenebaum Cancer Center, University of Maryland School of Medicine, 15601 Crabbs Branch Way, Rockville, MD 20855. Tel.: 301-738-0568; Fax: 301-517-0352; E-mail: szhan001{at}umaryland.edu.

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