| Project/Area Number |
16390073
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | Tokyo Medical and Dental University |
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Principal Investigator |
HATA Yutaka Tokyo Medical and Dental University, Graduate School of Medicine, Professor, 大学院・医歯学総合研究科, 教授 (80313237)
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| Co-Investigator(Kenkyū-buntansha) |
HIRABAYASHI Susumu Tokyo Medical and Dental University, Graduate School of Medicine, Assistant Professor, 大学院・医歯学総合研究科, 助手 (80376730)
IIDA Junko Tokyo Medical and Dental University, Graduate School of Medicine, Assistant Professor, 大学院・医歯学総合研究科, 助手 (80376805)
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| Project Period (FY) |
2004 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥15,100,000 (Direct Cost: ¥15,100,000)
Fiscal Year 2005: ¥5,800,000 (Direct Cost: ¥5,800,000)
Fiscal Year 2004: ¥9,300,000 (Direct Cost: ¥9,300,000)
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| Keywords | epithelial cell junction / neural synapse / cell adhesion / cell polarity / 細胞骨格 / シグナル伝達 |
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| Research Abstract |
Multicellular organisms develop functional domains such as epithelial cell junctions, neural synapses and lipid rafts on plasma membranes, which are important for the efficient intercellular signal transductions. These domains are composed of distinct protein components that interact with each other in manifold ways. Scaffold proteins have emerged as key molecules underlying basal molecular architectures of cell junctions. Scaffold proteins have multiple modules that bind a wide variety of proteins and facilitate the interactions among these ligands. As more than one ligands bind to the same module, some components can interact with a scaffold protein simultaneously, whereas others can not. Thereby, the combination of proteins assembled by a scaffold protein should alter depending on the cellular context. We currently examine which proteins are assembled by scaffold proteins at various stages of the maturation of cell junctions.
1) We have reported that synaptic scaffold molecule (S-SCAM) is involved in the accumulation of synaptic cell adhesion molecule named neuroligin. S-SCAM appears to provide a scaffold to activate a small GTP-binding protein implicated in the regulation of the cytoskeleton in neural dendritic spines.
2) Membrane-associated guanylate kinase with inverted organization (MAGI)-1 is an epithelial isoform of S-SCAM. We have recently revealed in the immunoelectron microscope the localization of MAGI-1 at slit diaphragm in kidney. MAGI-1 interacts with nephrin, a cell adhesion molecule that is an essential component of slit diaphragm.
3) Junctional adhesion molecule (JAM) 4 was identified as a ligand for MAGI-1. We have identified Ligand-of-Numb X (LNX) 1 as a novel JAM4-binding partner and analyzed the effect of LNX1 on endocytosis of JAM4.
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