Overview
- Peptide DLGGKRLGIEDAAGLGGPDGK(C), corresponding to amino acid residues 184-204 of rat KV3.2 (Accession P22462). Intracellular, N-terminal part.
- Rat brain membranes (1:200). Mouse sciatic nerve lysate (Sobko, A. et al. (1998) J. Neurosci. 18, 10398.).
- Western blot analysis of rat brain membranes:1. Anti-KV3.2 (KCNC2) Antibody (#APC-011), (1:200).
2. Anti-KV3.2 (KCNC2) Antibody, preincubated with Kv3.2/KCNC2 Blocking Peptide (#BLP-PC011).
- CHO transfected cells (Lewis, A. et al. (2004) J. Biol. Chem. 279, 7884.).
- Rat brain sections. Human pancreatic islets (Yan, L. et al. (2004) Diabetes 53, 597.).
KV3.2 is a member of the voltage-gated K+ channel superfamily. Together with the related proteins KV3.1, KV3.3 and KV3.4 they constitute the Shaw type subfamily family.1
As with all KV channels, KV3.2 possesses the signature structure of the voltage-dependent K+ channels: six membrane-spanning domains with intracellular N- and C-termini. The functional KV channel is a tetramer that can either be a homomer or a heteromer of KV3 subunits.
KV3 subfamily members inactivate very rapidly and therefore are thought to play a role in the repolarization of action potentials and to facilitate repetitive high frequency firing.2,3
KV3.2 is highly expressed in the brain but has been also detected in peripheral organs such as pancreas and mesenteric artery.
KV3.2 and KV3.1 are highly enriched in neurons that fire at high frequencies, such as fast-spiking interneurons of the cortex and hippocampus and neurons in the globus pallidus. Their unusually rapid activation and deactivation rates allow channels containing KV3.2 and KV3.1 subunits to repolarize action potentials quickly thus minimizing the rate of recovery of sodium channel inactivation.2,3