1993 Fiscal Year Final Research Report Summary
Mechanism of Signal Transduction by Nonreceptor Protein-tyrosine Kinases
| Project/Area Number |
04670150
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Sapporo Medical University |
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Principal Investigator |
SASAKI Terukatsu Sapporo Medical University, Cancer Research Institute, Professor, 医学部・付属癌研究所 (00045494)
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| Co-Investigator(Kenkyū-buntansha) |
NAGURA Kazuko Sapporo Medical University, Cancer Research Institute, Research Associate, 医学部・付属癌研究所, 技師
ISHINO Masaho Sapporo Medical University, Cancer Research Institute, Instructor, 医学部・付属癌研究所, 助手 (30232325)
SASAKI Hiroko Sapporo Medical University, Cancer Research Institute, Assistant Professor, 医学部・付属癌研究所, 講師 (60045424)
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| Project Period (FY) |
1992 – 1993
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| Keywords | Src homology 3 domain / protein-tyrosine kinase / tyrosine-phosphorylation / GST fusion protein |
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| Research Abstract |
1. The Src homology 3 domain (SH3) is a protein domain involved in the assembly of proteins participating in the signal transduction by protein-tyrosine kinases. A cDNA clone encoding a new protein ligand to the SH3 domain of Fyn PTK was isolated. The clone was identified by screening mouse embryo cDNA library with Fyn・SH3/GST fusion protein as a probe. The new SH3 ligand protein is also expressed in adult brain. The protein contains two proline-rich sequences with a specificity in binding to Fyn and Src SH3 domains, a new SH3 domain, and potential ligand sequences for SH2 domains. Antibody specific to the newly identified protein immunoprecipitated and immunoblotted a protein from the teratocarcinoma cell lysate and from the lysate of COS-7 cells transfected with the cloned cDNA.The protein was tyrosine-phosphorylated by Fyn expressed from cotransfected fyn cDNA in COS-7 cells. 2. A 70-kDa protein with high affinity to Fyn SH3 was found in the Jurkat cell lysate by affinity binding to Fyn SH3/GST fusion protein. The protein was eluted from SDS-PAGE gels, digested with trypsin, and the peptides were separated. The results of gas-phase microsequencing of the peptides indicated that the protein is closely related to GAP-binding phosphoprotein, p62. The SH3 domains are known to bind to proline-rich sequences. The proline-rich sequences in p62 were expressed as GST fusion proteins and the binding of the GST fusion proteins to various SH3/GST fusion proteins were examined. The results indicate that each proline-rich sequence has a specific affinity to a subset of SH3 domains.
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Research Products
(15 results)
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[Publications] Adachi,M.,Sekiya,M.,shino,M.,Sasaki,H.,Hinoda,Y.,Imai,K.& Yachi,A.: "Induction of protein-tyrosine phosphatase LC-PTP by IL-2 in human T cells." Febs Lett.338. 47-52 (1994)
Description
「研究成果報告書概要(和文)」より
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[Publications] Adachi, M., Sekiya, M., Ishino, M., Sasaki, H., Hinoda, Y., Imai, K.and Yachi, A.: "Induction of protein-tyrosine phosphatase LC-PTP by IL-2 in human T cells" FEBS Lett.338. 47-52 (1994)
Description
「研究成果報告書概要(欧文)」より
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