IndraLab

"This suggests that the interactions of the SNARE components with Kv2.1 are abolished upon their recruitment into a full SNARE complex, which does not interact with the channel."

"Recent work demonstrating that Kv2.1 directly interacts with exocytotic SNARE proteins to modulate exocytosis xref , xref , xref raises the possibility of non-channel exocytotic function(s) of Kv2.1 in skeletal muscle regulating GLUT4 transport or function."

"Inhibition of Kv2.1 SNARE protein interaction interferes with dense core vesicle release from PC-12 cells, and overexpression enhances release via a mechanism independent of ion conduction ( xref )."

"Moreover, the physiological significance of the redox sensitivity of Kv2.1 in insulin secretion is unclear, because it has been reported that changes in Kv2.1 channels do not affect the levels of the critical pool of subplasma membrane calcium that regulates exocytosis. xref Because NADPH facilitates insulin exocytosis, xref it has been speculated that the binding of NADPH increases the association of Kv2.1 with SNARE proteins, which facilitates granule docking or priming. xref Although this is an interesting possibility, additional investigations are required to fully elucidate the relationship between NADP(H) and Kv2.1 and to assess its importance in regulating insulin secretion or other physiological phenomena."

"However, the binding of SNARE proteins to Kv2.1 could also regulate ISG exocytosis in a manner independent of electrical activity [ xref ]."

"In β-cells, these Kv2.1-SNARE complex interactions can enhance insulin secretion [ xref ]."