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PMID: 7628441 Published · ppublish English Journal Article

LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck.

The EMBO journal ·Vol. 14 ·No. 14 ·1995-07-17 ·Pages 3403-14

Takemoto Y, Furuta M, Li XK, Strong-Sparks WJ, Hashimoto Y

Abstract

The Lck tyrosine kinase molecule plays an essential role in T cell activation and T cell development. Using the expression cloning technique, we have isolated a gene that encodes a molecule, LckBP1, able to associate with murine Lck. Analysis of full-length LckBP1 cDNA indicates at least four potentially important segments: a four tandem 37 amino acid repeat motif with a potential helix-turn-helix DNA binding motif; a proline-rich region; a proline-glutamate repeat; and an SH3 domain. These four regions are very similar to the human haematopoietic-specific protein 1 (HS1). Deletion mutant analysis of LckBP1 revealed two proline-rich regions that permit association with Lck SH3. One region contains prolines conserved among HS1 and cortactin, and the other region contains a potential MAP kinase recognition site. In vivo association between Lck and LckBP1 was confirmed by immunoprecipitation of lysates from a pre-T cell line and adult thymocytes using antibodies specific for Lck and LckBP1. LckBP1 is tyrosine phosphorylated after T-cell receptor stimulation. The SH3 domain and the potential helix-turn-helix motif in LckBP1 suggest that this molecule may associate with various molecules and function as a DNA binding molecule. The data also suggest that LckBP1 mediates intracellular signalling through Lck in T cells.

Related Genes
MeSH Terms
3T3 Cells Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Base Sequence Binding Sites Cell Line Cloning, Molecular DNA, Complementary DNA-Binding Proteins/chemistry,metabolism Hematopoietic Stem Cells/metabolism Humans Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Mice Mice, Inbred BALB C Molecular Sequence Data Peptides/metabolism Proline/metabolism Proline-Rich Protein Domains Protein Conformation Protein-Tyrosine Kinases/metabolism Receptors, Antigen, T-Cell/metabolism Sequence Homology, Amino Acid Signal Transduction T-Lymphocytes/metabolism
Chemicals
Adaptor Proteins, Signal Transducing DNA, Complementary DNA-Binding Proteins Hcls1 protein, mouse Peptides Receptors, Antigen, T-Cell Proline Protein-Tyrosine Kinases Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Takemoto Y
Institute of Immunology, Syntex-Roche, Chiba, Japan.
Furuta M
Li X K
Strong-Sparks W J
Hashimoto Y
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1995-07-17
Pages
3403-14
Language
English
Region
England
NLM ID
8208664
PMCID
PMC394407
Subset
IM
Databases
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