Phospho-dependent regulation of protein complex
| Project/Area Number |
25861758
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional basic dentistry
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| Research Institution | Kyushu University |
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Principal Investigator |
GAO JING 九州大学, 歯学研究科(研究院), 助教 (40585882)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | リン酸化 / SNARE / PKA / PKC / タンパク質複合体 / SNAP-２５ / 開口分泌 |
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| Outline of Final Research Achievements |
In the current study, we investigated the phospho-regulation of exocytosis and the role of PRIP in the modulation of exocytosis. The formation of sodium dodecyl sulfate (SDS)-resistant SNARE complex was decreased by the phosphorylation of Thr 138 of SNAP-25 by PKA in advance. In contrast, increased formation of SNARE complex were seen when Ser 187 of SNAP-25 was phosphorylated by PKC instead. The noradrenaline secretion from PC12 cells was regulated by the modulation of phosphorylation of SNAP-25 by PKA and PKC. On the other hand, we found that C2 domain of PRIP-1 bound t-SNARE proteins as well as SNARE accessory protein, synaptotagmine-1 C2 domain in a calcium-dependent manner. These results suggest that phosphorylation of SNAP-25 by PKC or PKA is differentially involved in exocytosis in PC12 cells by regulating the formation of SNARE complex in the different patterns,which confirmed the notion that protein phosphorylation is involved in regulation of exocytosis.
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Report
(3 results)
Research Products
(10 results)
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[Journal Article] Signaling pathway for adiponectin expression in adipocytes by osteocalcin.2015
Author(s)
Otani, T., Mizokami, A., Hayashi, Y., Gao, J., Mori, Y., Nakamura, S., Takeuchi, H. and Hirata, M.
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Journal Title
Cellular Signalling
Volume: 27
Issue: 3
Pages: 532-544
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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