The archetypal tumor promoter PMA, which promotes cancer without mutating the DNA, increases Wnt signaling by activating macropinocytosis and membrane trafficking in Xenopus embryos and tumor cells.

Modulation of the energy barrier for membrane fusion is a common mechanism by which sensors in the synapse produce supralinear calcium dependence of vesicle release and short-term synaptic potentiation.

Independent osmotic, genetic and biochemical perturbations modulate neurotransmitter release in a multiplicative manner.

The priming protein ubMunc13-2 and Synaptotagmin-7 cooperate with phorbolesters/diacylglycerol to stimulate vesicle priming in adrenal chromaffin cells, whereas phorbolesters/diacylglycerol interacting with Munc13-1 inhibit vesicle fusion, which identifies opposing functions of these two Munc13 proteins.

A near-infrared light-stimulable optogenetic platform enables remote and wireless manipulation of calcium signaling and immune responses both in vitro and in vivo to achieve tailored function.

Genetic and electrophysiology experiments provide the first direct evidence that protein kinase C is a calcium-sensing protein in post-tetanic potentiation, a form of synaptic plasticity that supports short-term memory.

Protein kinase C brings about post-tetanic potentiation - a temporary increase in synaptic strength due to increased transmitter release - via phosphorylation of a target protein, Munc18-1.

Pkc53E kinase-mediated downregulation of CSL/Su(H) activity is a direct molecular response to parasitoid wasp infestation in Drosophila, allowing the differentiation of encapsulation-active lamellocytes, thereby ensuring an appropriate immune defense.

The crystal structure of a large C-terminal fragment of Munc13-1 provides a key framework to understand how Munc13-1 mediates neurotransmitter release and presynaptic plasticity.

The α₁-adrenergic receptor augments the activity of the L-type Ca²⁺ channel Ca_V1.2 through PKC and the tyrosine kinases Pyk2 and Src and thereby synaptic plasticity.