Synaptotagmin IV regulates dense core vesicle (DCV) release in LbetaT2 cells.

Synaptotagmins (Syts) are calcium-binding proteins which are conserved from nematodes to humans. Fifteen Syts have been identified in mammalian species. Syt I is recognized as a Ca(2+) sensor for the synchronized release of synaptic vesicles in some types of neurons, but its role in the secretion of dense core vesicles (DCVs) remains unclear.

PKA activation bypasses the requirement for UNC-31 in the docking of dense core vesicles from C. elegans neurons.

The nematode C. elegans provides a powerful model system for exploring the molecular basis of synaptogenesis and neurotransmission. However, the lack of direct functional assays of release processes has largely prevented an in depth understanding of the mechanism of vesicular exocytosis and endocytosis in C.

Characteristics of Ca2+-exocytosis coupling in isolated mouse pancreatic beta cells.

Aim: To characterize Ca2+-stimulated exocytosis in isolated mouse pancreatic beta cells.

Methods: An improved method was described for isolation of mouse pancreatic beta cells by collagenase P. The Ca2+ channel current and the membrane capacitance were examined by using the whole-cell patch clamp recording technique.

Kir6.2DeltaC26 channel traffics to plasma membrane by constitutive exocytosis.

Adenosine triphosphate (ATP)-sensitive K+ (KATP) channels regulate many cellular functions by coupling the metabolic state of the cell to the changes in membrane potential. Truncation of C-terminal 26 amino acid residues of Kir6.2 protein (Kir6.