| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Research Abstract |
In the current study, we investigated the involvement of phospholipase C-related but catalytically inactive protein (PRIP), which was firstly identified in our laboratory, in the regulation of the function of protein kinases and phosphatases, especially in the phospho-dependent modulation of exocytosis. We found that PRIP directly interacted with the catalytic subunits of two distinct phosphatases (PP1 and PP2A) in a mutually exclusive manner and the interactions are regulated by phosphorylation of PRIP itself. Moreover,phospho-SNAP-25 (synaptosome-associated protein of 25kDa), a component of SNARE complex, was dephosphorylated by protein phosphatase-1, whose activity was regulated by PRIP. Noradrenalin secretionin PC12 cells was also modulated b y PRI P, which was correlated with the phospho-states of SNAP-25.Collectively, these results suggest that PRIP is involved in the regulation of the phospho-states of SNAP-25 by modulating the activity of PP1, thus regulating exocytosis.
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