2001 Fiscal Year Final Research Report Summary
Functions and mode of action of novel regulatory systems for cell adhesion and motility
| Project/Area Number |
12680636
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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 |
Functional biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
NAKANISHI Hiroyuki Osaka University, Graduate School of Medicine, Associate Professor, 医学系研究科, 助教授 (80314318)
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| Project Period (FY) |
2000 – 2001
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| Keywords | cell adhesion / cell motility / nectin-afadin system / cadherin-catenin system / JAM-ZO-l system / frabin / Cdc42 small G protein / Rac small G protein |
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| Research Abstract |
We have found a novel regulatory system for cell adhesion. This system consists of nectin and afadin. Nectin is an immunoglobulin-like cell adhesion molecule, and afadin is an F-aotin-binding protein that connects nectin to the actin cytoskeleton.
The nectin-afadin system organizes adherens and tight jjunctions in epithelial cells.
We have also found a novel regulatory system for cell motility. This system consists of frabin and Cdc42 small G protein. Frabin is an F-actin-blnding protein that activates Cdc42. During this support from2000-to 2001, we have studied the functions and mode of action of these nectin-afadin and frabin-Cdc42 systems. The results obtained are as follows :
(1) In epithelial cells, the nectin-afadin system recruits the cadherin-catenin and JAM-ZO-lsystems to nectin-based cell-cell adhesion sites. In neurons, the nectin-afadinsystemis localized at synapses and involved information of synapses. In testis, the nectin-afadin system is involved in formation of Sertoli-spermatid junctions and essential for spermatid morphogenesis.
(2) Frabin associates with specific actin and membrane structures and activates not only Cdc42 and but also Rac small G protein in the vicinity of these structures, eventually to leading to cell motility. The F-actin-binding activity of frabin cooperatively functions with the Cdc42-activating activity in cell motility.
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Research Products
(34 results)
