Phospho-dependent regulation of protein complex

2014 Fiscal Year Final Research Report

• Project/Area Number: 25861758
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Functional basic dentistry
• Research Institution: Kyushu University
• Principal Investigator: GAO JING 九州大学, 歯学研究科(研究院), 助教 (40585882)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: リン酸化 / SNARE / PKA / PKC

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.

Free Research Field

医歯薬学