RRC ID 35737
Author Takemoto Y, Furuta M, Sato M, Kubo M, Hashimoto Y.
Title Isolation and characterization of a novel HS1 SH3 domain binding protein, HS1BP3.
Journal Int Immunol
Abstract 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.
Volume 11(12)
Pages 1957-64
Published 1999-12-1
DOI 10.1093/intimm/11.12.1957
PMID 10590261
MeSH Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Base Sequence Blood Proteins / metabolism* Carrier Proteins / chemistry Carrier Proteins / isolation & purification* Carrier Proteins / physiology Cell Line Interleukin-2 / biosynthesis Lymphocyte Activation Mice Molecular Sequence Data src Homology Domains*
IF 3.519
Times Cited 22
WOS Category IMMUNOLOGY
Resource
DNA material pCAGGS-HS1BP3 (RDB02142) DHA-HS1BP3 (RDB02143) D-HA-HS1BP3-C2 (RDB02144) D-Myc-HS1BP3 (RDB02145) D-Myc-HS1BP3-C2 (RDB02146) GST-HS1BP3-C5 (RDB02149) GST-HS1BP3 (RDB02150) GST-HS1BP3-C2 (RDB02151).
Human and Animal Cells HeLa(RCB0007) NIH3T3