1999 Fiscal Year Final Research Report Summary
Role of G-Protein of Rap1 in Oncogenesis
| Project/Area Number |
10670969
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Hematology
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| Research Institution | JIKEI UNIVERSITY SCHOOL OF MEDICINE |
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Principal Investigator |
KURAISHI Yasunobu JIKEI UNIVERSITY SCHOOL OF MEDICINE,HEMATOLOGY AND ONCOLOGY, ASSOCIATE PROFESSOR, 医学部, 助教授 (30112824)
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| Co-Investigator(Kenkyū-buntansha) |
ICHIBA Tamotsu JIKEI UNIVERSITY SCHOOL OF MEDICINE,HEMATOLOGY AND ONCOLOGY,RESEARCH ASSISTANT, 医学部, 助手 (10307407)
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| Project Period (FY) |
1998 – 1999
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| Keywords | GUANINE NUCLEOTIDE EXCHANGE FACTOR / LOW MOLECULAR G-PROTEIN / ENZYME ACTIVITY / TYROSINE PHOSPHORYLATION |
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| Research Abstract |
Although Rap 1 is a member of Ras-family G-protein, it shows a unique character that it can antagonize Ras induced transformation. We previously analyzed the regulation of C3G-Rap 1 pathway.
In the present research, we found that C3G was tyrosine phosphorylated on its tyrosine 504 in the presence of adaptor protein, Crk. We demonstrated that tyrosine phosphorylation of C3G correlate well with its catalytic activation for Rap 1. The up-regulation of C3G by Crk was not observed when its tyrosine was substituted to phenylalanine. Furthermore, C3G was tyrosine phosphorylated in 3Y1 cell lines transfected with Crk or Src, but not Ras. We also found that amino-terminal transfected of C3G shows the elevated exchange activity, that is, amino-terminal region of C3G negatively regulated its catalytic activity.
We plan to identity proteins which can bind to C3G using two-hybrid method, and clarify its role in signal transduction.
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