J. Exp. Med.
© The Rockefeller University Press
0022-1007/97/04/1387/06 $2.00
Volume 185, Number 7, April 7, 1997 1387-1392

BRIEF DEFINITIVE REPORT:
Role of Tyrosine Phosphorylation of HS1 in B Cell Antigen Receptor-mediated Apoptosis

By Yuji Yamanashi,^* Takahiro Fukuda, Hirofumi Nishizumi,^* Tetsuya Inazu,^§ Ken-ichi Higashi,^* Daisuke Kitamura, Takaomi Ishida,^* Hirohei Yamamura,^¶ Takeshi Watanabe, and Tadashi Yamamoto^*

From the ^* Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan;  Department of Molecular Immunology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-62, Japan; ^§ Department of Biochemistry, Fukui Medical School, Fukui 910-11, Japan;  Research Institute for Bioscience, Science University of Tokyo, Noda 278, Japan; and the ^¶ Department of Biochemistry, Kobe University, School of Medicine, Kobe 650, Japan

The 75-kD HS1 protein is highly tyrosine-phosphorylated during B cell antigen receptor (BCR)-mediated signaling. Owing to low expression of HS1, WEHI-231-derived M1 cells, unlike the parental cells, are insensitive to BCR-mediated apoptosis. Here, we show that BCR-associated tyrosine kinases Lyn and Syk synergistically phosphorylate HS1, and that Tyr378 and Tyr-397 of HS1 are the critical residues for its BCR-induced phosphorylation. In addition, unlike wild-type HS1, a mutant HS1 carrying the mutations Phe-378 and Phe-397 was unable to render M1 cells sensitive to apoptosis. Wild-type HS1, but not the mutant, localized to the nucleus under the synergy of Lyn and Syk. Thus, tyrosine phosphorylation of HS1 is required for BCR-induced apoptosis and nuclear translocation of HS1 may be a prerequisite for B cell apoptosis.

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