Isolation and characterization of a novel HS1 SH3 domain binding protein, HS1BP3.
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.
Takemoto
Y
Y
Institute of Immunology, Syntex-Roche, 2669 Yamazaki, Noda, Chiba 278, Japan.
Furuta
M
M
Sato
M
M
Kubo
M
M
Hashimoto
Y
Y
D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001798:Blood Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000502:physiology; D002460:Cell Line; D007376:Interleukin-2 / Q000096:biosynthesis; D008213:Lymphocyte Activation; D051379:Mice; D008969:Molecular Sequence Data; D018909:src Homology Domains
D048868:Adaptor Proteins, Signal Transducing; D001798:Blood Proteins; D002352:Carrier Proteins; C061909:HCLS1 protein, human; D007376:Interleukin-2