1995 Fiscal Year Final Research Report Summary
Ras- and protein kinase- mediated signal transduction
| Project/Area Number |
06454177
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
KAIBUCHI Kozo Nara Institute of Science and Technology, Division of Signal Transduction, Professor, バイオサイエンス研究科, 教授 (00169377)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAFUKU Masato Nara Institute of Science and Technology, Division of Signal Transduction, Assis, バイオサイエンス研究科, 助教授 (80202216)
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| Project Period (FY) |
1994 – 1995
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| Keywords | Small GTPase / Protein kinase / Cytoskeleton / Cell Adhesion |
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| Research Abstract |
The small GTPase Ras is implicated in the regulation of various cell functions such as gene expression and cell proliferation. Here, we purified a Ras-interacting protein and identified it as AF-6. AF-6 has a GLGF/Dlg homology repeat (DHR) motif and shows a high degree of sequence similarity with Drosophila Canoe. The recombinant AF-6 and Canoe specifically interacted with GTP・Ras. The known Ras target c-Raf-l inhibited the interaction of AF-6 with GTP・Ras. These results indicate that AF-6 and Canoe are putative targets for Ras.
The small GTPase Rho has been implicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers and focal contacts. Upon stimulation, GDP・Rho is believed to be converted to GTP・Rho then binds specific targets to mediate downstream signaling. Here we found that GTP・Rho. GTP・Rho directly bound and activated two types of serine/threonine kinases. One is protein kinase N (PKN), of which C-terminal catalytic domain is homologous to that of protein kinase C.PKN was autophosphorylated in Swiss 3T3 cells upon stimulation by LPA and this autophosphorylation was blocked by treatment with Botulinum C3 exoenzyme. The other is novel protein kinase with Mr of about 164 kDa, which we have molecular cloned and designated as Rho-kinase. These finding indicates that upon stimulation GTP・Rho seems to interact with unique subsets of protein kinases.
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[Publications] Kuroda, S., Shimizu, K., Yamamori, B., Matsuda S., Imazumi, K., Kaibuchi, K., and Takai, Y.: "Purification and characterization of REKS from Xenopus eggs-Identification of REKS as a Ras-dependent mitogen-activated kinase kinase kinase." J.Biol.Chem.270. 2460-2465 (1995)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Yamamoto, T., Matsui, T., Nakafuku, M., Iwamatsu, A., and Kaibuchi, K.: "A novel GTPase-activating protein for R-ras, R-Ras GAP." J.Biol.Chem.270. 30557-30561 (1995)
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「研究成果報告書概要(欧文)」より
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[Publications] Gotoh, T., Hattori, S., Nakamura, S., Kitayama, H., Noda, M., Takai, Y., Kaibuchi, K., Matsui, H., Hatase, O., Takahashi, H., Kurata, T., Matsuda, M.: "Identification of Rapl as atarget for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G." Mol.Cell.Biol.15. 6746-6753 (1995)
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[Publications] Miyazaki, M., Kaibuchi, K., Shirataki, H., Kohno, H., Ueyama, T., Nishikawa, J., and Takai, Y.: "Rabphilin-3A binds to a Mr 115,000 polypeptide in phosphatidylserine- and Ca2+-dependent manner." Mol.Brain Res.28. 29-36 (1995)
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[Publications] Amano, K., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., Kaibuchi, K.: "Identification of a putative target for Rho as a serine-threonine kinase protein kinase N." Science. 271. 648-651 (1996)
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「研究成果報告書概要(欧文)」より
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[Publications] Kuriyama, M., Harada, N., Kuroda, S., Yamamoto, T., Nakafuku, M., Iwamatsu, A., Yamamoto, D., Prasad, R., Croce, C., Canaani, E., and Kaibuchi, K.: "Identification of AF-6 and Canoe as putative targets for Ras." J.Biol.Chem.271. 607-610 (1996)
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「研究成果報告書概要(欧文)」より
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[Publications] Matsui, T., Amano, M., Yamamoto, T., Chihara, K., Nakafuku, M., Ito, M., Nakano, T., Okawa, K., Iwamatsu, A., and Kaibuchi, K.: "Rho-associated kinase, a novel serine/threonine kinase, as a putative target for the small GTP-binding protein Rho." EMBO J.(in press).
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