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Together, the results indicated that PI4KIIα can regulate insulin secretion independent of kinase activity.
All the above results indicated that PI4KIIα may regulate insulin secretion via protein protein interactions.
TRPM2 is also localized on lysosomes in pancreatic β cells, leading to the proposition that TRPM2-mediated lysosomal Ca2+ release may regulate insulin secretion (Lange et al., 2009).
Based on the observation that PI4KIIα can regulate insulin secretion, we then carefully analyzed the targets involved in intracellular transport, which are listed in Table 1.
Moreover, there is evidence that BMPs might regulate insulin secretion.
Both molecules can regulate insulin secretion from beta cells [5], [6].
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PROBLEM: The ATP-sensitive potassium (KATP) channel is a tiny, gated pore in the cell membrane of insulin-secreting β-cells that regulates insulin secretion.
The protein seems to participate in a higher order of metabolic regulation by interacting with Bcl-2-family members and by regulating insulin secretion.
We then questioned whether PI4KIIα directly regulates insulin secretion.
Open image in new window Fig. 3 PI4KIIα regulates insulin secretion in MIN6 cells.
Open image in new window Fig. 5 PI4KIIα regulates insulin secretion via a PKD-dependent pathway.
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