| Project/Area Number |
24390081
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Yamaguchi University |
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Principal Investigator |
NAKAI Akira 山口大学, 医学(系)研究科(研究院), 教授 (60252516)
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| Co-Investigator(Kenkyū-buntansha) |
FUJIMOTO Mitsuaki 山口大学, 大学院医学系研究科, 准教授 (80359900)
HAYASHIDA Naoki 山口大学, 大学院医学系研究科, 講師 (40420517)
TAKII Ryosuke 山口大学, 大学院医学系研究科, 助教 (00419558)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥18,720,000 (Direct Cost: ¥14,400,000、Indirect Cost: ¥4,320,000)
Fiscal Year 2014: ¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
Fiscal Year 2012: ¥7,020,000 (Direct Cost: ¥5,400,000、Indirect Cost: ¥1,620,000)
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| Keywords | 神経変性疾患 / 熱ショック / 転写 / クロマチン / プロテオスタシス / リン酸化 / 蛋白質 / ホメオスタシス / 転写因子 / リン酸 |
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| Outline of Final Research Achievements |
Capacity of cellular protein homeostasis, known as proteostasis, is related with progression of age-related neurodegenerative disease and cancer. One of prominent mechanisms of the maintenance of proteostasis capacity is the heat shock response, which is regulated mainly at the level of transcription by heat shock factors (HSFs). Among mammalian HSFs, HSF4 constitutively binds to DNA under unstressed conditions. In this research project, we demonstrate a mechanism by which HSF4 activity is regulated through phosphorylation, and suggest that proteostasis capacity is regulated by a chemical modification of HSF4 under physiological conditions.
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