MembraneinducedalterationsofstructureandsignaltransductionmechanisminthePIP3-bindingdomains
Project/Area Number |
22570191
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Cell biology
|
Research Institution | University of Hyogo |
Principal Investigator |
TUZI Satoru 兵庫県立大学, 大学院・生命理学研究科, 准教授 (60227387)
|
Co-Investigator(Kenkyū-buntansha) |
YAGISAWA Hitoshi 兵庫県立大学, 大学院・生命理学研究科, 准教授 (40192380)
|
Project Period (FY) |
2010 – 2012
|
Project Status |
Completed (Fiscal Year 2012)
|
Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2010: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | 細胞内情報伝達 / 固体NMR 分光法 / PH ドメイン / 分光法 / シグナル伝達 / 膜表在性蛋白質 / 脂質二重膜 / 生物物理 / PHドメイン / SWAP-70 / PIP3 / 固体NMR / 膜結合性蛋白質 / 二次構造 |
Research Abstract |
Conformations of the pleckstrin homology (PH) domain in solutionand at the membrane surface were examined by using solid-state NMR, circular dichroism(CD) and fluorescence spectroscopy. The PH domains form one of the largest domainfamilies known to regulate membrane association of host proteins. Drastic conformationalalterations including a transition of the secondary structure were detected for themembrane-bound PH domain of a signal transduction protein SWAP-70. Theseconformational alterations induced at the membrane surface are suggested to regulatefunctions of SWAP-70, such as intracellular relocalization in response to the cellularsignaling.
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Report
(4 results)
Research Products
(20 results)