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International Immunology, Vol. 11, No. 12, 1957-1964, December 1999
© 1999 Japanese Society for Immunology

Isolation and characterization of a novel HS1 SH3 domain binding protein, HS1BP3

Yoshihiro Takemoto1,3, Masaaki Furuta1,3, Mitsuru Sato1,3, Masato Kubo2 and Yasuhiro Hashimoto1,3

1 Institute of Immunology, Syntex-Roche, 2669 Yamazaki, Noda, Chiba 278, Japan.
2 Science University of Tokyo, 2669 Yamazaki Noda, Chiba 278, Japan

Correspondence to: Y. Takemoto, Tsukuba Research Laboratories, Glaxo Wellcome K.K., 43, Wadai, Tsukuba-shi, Ibaraki 300-4247, Japan

We have isolated a novel gene, HS1BP3, which encodes an HS1 binding protein. Analysis of HS1BP3 cDNA indicates several potentially important segments, including a PX domain, a leucine zipper, immunoreceptor tyrosine-based inhibitory motif-like motifs and proline-rich regions. HS1BP3 associates with HS1 proteins in vivo as confirmed by immunoprecipitation in B and T cell lines. HS1BP3 preferentially associates with the HS1 SH3 domains rather than with other SH3 molecules, suggesting a role of HS1BP3 as an HS1 signaling mediator. Overexpression of mutant HS1BP3 protein in T cell lines results in decreased IL-2 production. Our data suggest a novel role for HS1BP3 in lymphocyte activation.

Keywords: HS1, HS1BP3, IL-2, Lck, PX domain, tyrosine kinase

3 Present address: Tsukuba Research Laboratories, Glaxo Wellcome K.K., 43, Wadai, Tsukuba-shi, Ibaraki 300-4247, Japan

Transmitting editor: M. Taniguchi


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