Molecular cloning and characterization of Kv6.3, a novel modulatory subunit for voltage-gated K + channel Kv2.1

• Published in: FEBS letters Vol. 512; no. 1; pp. 230 - 234
• Main Authors: Sano, Yorikata, Mochizuki, Shinobu, Miyake, Akira, Kitada, Chika, Inamura, Kohei, Yokoi, Hiromichi, Nozawa, Katsura, Matsushime, Hitoshi, Furuichi, Kiyoshi
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 13.02.2002
• Subjects: Amino Acid Sequence; Cloning, Molecular; Delayed Rectifier Potassium Channels; Electric Conductivity; Humans; Ion Channel Gating; Kv2.1; Kv6.3; Modulatory subunit; Molecular Sequence Data; Potassium Channels - classification; Potassium Channels - genetics; Potassium Channels - metabolism; Potassium Channels, Voltage-Gated; Protein Subunits; Sequence Homology, Amino Acid; Shab Potassium Channels; Tissue Distribution; Voltage-gated K + channel; PBS, phosphate-buffered saline; Voltage-gated K + channel; Modulatory subunit; Kv6.3; CDS, coding sequence; PCR, polymerase chain reaction; RACE, rapid amplification of cDNA ends; RT, reverse transcriptase; Kv2.1; EST, expressed sequence tag; GAPDH, glyceraldehyde-3-phosphate dehydrogenase
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(02)02267-6

We report identification and characterization of Kv6.3, a novel member of the voltage-gated K + channel. Reverse transcriptase-polymerase chain reaction analysis indicated that Kv6.3 was highly expressed in the brain. Electrophysiological studies indicated that homomultimeric Kv6.3 did not yield a functional voltage-gated ion channel. When Kv6.3 and Kv2.1 were co-expressed, the heteromultimeric channels displayed the decreased rate of deactivation compared to the homomultimeric Kv2.1 channels. Immunoprecipitation studies indicated that Kv6.3 bound with Kv2.1 in co-transfected cells. These results indicate that Kv6.3 is a novel member of the voltage-gated K + channel which functions as a modulatory subunit.