Motonao Nakamura
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Motonao Nakamura has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
Huiping Li
Central Pharmaceutical Research Institute, Pharmaceutical Frontier Research Laboratories, Japan Tobacco Inc., Yokohama,1 Institute of Nephrology, Faculty of Medicine, Niigata University, Niigata, Japan2
1 shared publicationKen Katsuya
Central Pharmaceutical Research Institute, Pharmaceutical Frontier Research Laboratories, Japan Tobacco Inc., Yokohama,1 Institute of Nephrology, Faculty of Medicine, Niigata University, Niigata, Japan2
1 shared publicationKiyotaka Akiyama
Central Pharmaceutical Research Institute, Pharmaceutical Frontier Research Laboratories, Japan Tobacco Inc., Yokohama,1 Institute of Nephrology, Faculty of Medicine, Niigata University, Niigata, Japan2
1 shared publicationTadashi Yamamoto
Central Pharmaceutical Research Institute, Pharmaceutical Frontier Research Laboratories, Japan Tobacco Inc., Yokohama,1 Institute of Nephrology, Faculty of Medicine, Niigata University, Niigata, Japan2
1 shared publicationTakuya Orita
Central Pharmaceutical Research Institute, Pharmaceutical Frontier Research Laboratories, Japan Tobacco Inc., Yokohama,1 Institute of Nephrology, Faculty of Medicine, Niigata University, Niigata, Japan2
1 shared publicationToshio Higuchi
Central Pharmaceutical Research Institute, Pharmaceutical Frontier Research Laboratories, Japan Tobacco Inc., Yokohama, 236-0004, Japan
1 shared publication
Latest Publications
- Open Access
- 1 September 2004
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 24 (17) , 7456-7468
MUC20 Suppresses the Hepatocyte Growth Factor-Induced Grb2-Ras Pathway by Binding to a Multifunctional Docking Site of Met
A cDNA encoding a novel mucin protein, MUC20, was isolated as a gene that is up-regulated in the renal tissues of patients with immunoglobulin A nephropathy. We demonstrate here that the C terminus of MUC20 associates with the multifunctional docking site of Met without ligand activation, preventing Grb2 recruitment to Met and thus attenuating hepatocyte growth factor (HGF)-induced transient extracellular signal-regulated kinase-1 and -2 activation. Production of MUC20 reduced HGF-induced matrix metalloproteinase expression and proliferation, which require the Grb2-Ras pathway, whereas cell scattering, branching morphogenesis, and survival via the Gab1/phosphatidylinositol 3-kinase (PI3K) pathways was not affected. Thus, MUC20 reduces HGF-induced activation of the Grb2-Ras pathway but not the Gab1/PI3K pathways. We further demonstrate that the cytoplasmic domain of MUC20 has the ability to oligomerize and that the oligomerization augments its affinity for Met. Taken together, these results suggest that MUC20 is a novel regulator of the Met signaling cascade which has a role in suppression of the Grb2-Ras pathway.
- 1 September 2004
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 24 (17) , 7456-7468
Open AccessMUC20 Suppresses the Hepatocyte Growth Factor-Induced Grb2-Ras Pathway by Binding to a Multifunctional Docking Site of Met
A cDNA encoding a novel mucin protein, MUC20, was isolated as a gene that is up-regulated in the renal tissues of patients with immunoglobulin A nephropathy. We demonstrate here that the C terminus of MUC20 associates with the multifunctional docking site of Met without ligand activation, preventing Grb2 recruitment to Met and thus attenuating hepatocyte growth factor (HGF)-induced transient extracellular signal-regulated kinase-1 and -2 activation. Production of MUC20 reduced HGF-induced matrix metalloproteinase expression and proliferation, which require the Grb2-Ras pathway, whereas cell scattering, branching morphogenesis, and survival via the Gab1/phosphatidylinositol 3-kinase (PI3K) pathways was not affected. Thus, MUC20 reduces HGF-induced activation of the Grb2-Ras pathway but not the Gab1/PI3K pathways. We further demonstrate that the cytoplasmic domain of MUC20 has the ability to oligomerize and that the oligomerization augments its affinity for Met. Taken together, these results suggest that MUC20 is a novel regulator of the Met signaling cascade which has a role in suppression of the Grb2-Ras pathway.