Non-conducting function of the Kv2.1 channel enables it to recruit vesicles for release in neuroendocrine and nerve cells.

Regulation of exocytosis by voltage-gated K(+) channels has classically been viewed as inhibition mediated by K(+) fluxes. We recently identified a new role for Kv2.1 in facilitating vesicle release from neuroendocrine cells, which is independent of K(+) flux.

Syntaxin modulates Kv1.1 through dual action on channel surface expression and conductance.

The Kv1.1 channel that is expressed throughout the central and peripheral nervous system is known to interact with syntaxin 1A, a member of the exocytosis machinery protein complex. This interaction was previously shown to increase the macroscopic currents of the presynaptic Kv1.

Voltage-gated potassium channel as a facilitator of exocytosis.

Voltage-gated ion channels are well characterized for their function in excitability signals. Accumulating studies, however, have established an ion-independent function for the major classes of ion channels in cellular signaling. During the last few years we established a novel role for Kv2.

K+ channel facilitation of exocytosis by dynamic interaction with syntaxin.

Kv channels inhibit release indirectly by hyperpolarizing membrane potential, but the significance of Kv channel interaction with the secretory apparatus is not known. The Kv2.1 channel is commonly expressed in the soma and dendrites of neurons, where it could influence the release of neuropeptides and neurotrophins, and in neuroendocrine cells, where it could influence hormone release.