Biochemical characterization of the native Kv2.1 potassium channel

Jean Ju Chung, Min Li

Research output: Contribution to journalArticle

Abstract

Functional diversity of potassium channels in both prokaryotic and eukaryotic cells suggests multiple levels of regulation. Posttranslational regulation includes differential subunit assembly of homologous pore-forming subunits. In addition, a variety of modulatory subunits may interact with the pore complex either statically or dynamically. Kv2.1 is a delayed rectifier potassium channel isolated by expression cloning. The native polypeptide has not been purified, hence composition of the Kv2.1 channel complexes was not well understood. Here we report a biochemical characterization of Kv2.1 channel complexes from both recombinant cell lines and native rat brain. The channel complexes behave as large macromolecular complexes with an apparent oligomeric size of 650 kDa as judged by gel filtration chromatography. The molecular complexes have distinct biochemical populations detectable by a panel of antibodies. This is indicative of functional heterogeneity. Despite mRNA distribution in a variety of tissues, the native Kv2.1 polypeptides are more abundantly found in brain and have predominantly Kv2.1 subunits but not homologous Kv2.2 subunits. The proteins precipitated by anti-Kv2.1 and their physiological relevance are of interest for further investigation.

Original languageEnglish (US)
Pages (from-to)3743-3755
Number of pages13
JournalFEBS Journal
Volume272
Issue number14
DOIs
StatePublished - Jul 2005

Fingerprint

Shab Potassium Channels
Brain
Delayed Rectifier Potassium Channels
Prokaryotic Cells
Macromolecular Substances
Peptides
Cloning
Potassium Channels
Eukaryotic Cells
Chromatography
Gel Chromatography
Rats
Organism Cloning
Gels
Cells
Tissue
Cell Line
Messenger RNA
Antibodies
Chemical analysis

Keywords

  • Channels
  • Oligomerization
  • Potassium
  • Proteomics
  • Purification

ASJC Scopus subject areas

  • Biochemistry

Cite this

Biochemical characterization of the native Kv2.1 potassium channel. / Chung, Jean Ju; Li, Min.

In: FEBS Journal, Vol. 272, No. 14, 07.2005, p. 3743-3755.

Research output: Contribution to journalArticle

Chung, Jean Ju ; Li, Min. / Biochemical characterization of the native Kv2.1 potassium channel. In: FEBS Journal. 2005 ; Vol. 272, No. 14. pp. 3743-3755.
@article{d79b86750fa24a82be63dba2381a33b7,
title = "Biochemical characterization of the native Kv2.1 potassium channel",
abstract = "Functional diversity of potassium channels in both prokaryotic and eukaryotic cells suggests multiple levels of regulation. Posttranslational regulation includes differential subunit assembly of homologous pore-forming subunits. In addition, a variety of modulatory subunits may interact with the pore complex either statically or dynamically. Kv2.1 is a delayed rectifier potassium channel isolated by expression cloning. The native polypeptide has not been purified, hence composition of the Kv2.1 channel complexes was not well understood. Here we report a biochemical characterization of Kv2.1 channel complexes from both recombinant cell lines and native rat brain. The channel complexes behave as large macromolecular complexes with an apparent oligomeric size of 650 kDa as judged by gel filtration chromatography. The molecular complexes have distinct biochemical populations detectable by a panel of antibodies. This is indicative of functional heterogeneity. Despite mRNA distribution in a variety of tissues, the native Kv2.1 polypeptides are more abundantly found in brain and have predominantly Kv2.1 subunits but not homologous Kv2.2 subunits. The proteins precipitated by anti-Kv2.1 and their physiological relevance are of interest for further investigation.",
keywords = "Channels, Oligomerization, Potassium, Proteomics, Purification",
author = "Chung, {Jean Ju} and Min Li",
year = "2005",
month = "7",
doi = "10.1111/j.1742-4658.2005.04802.x",
language = "English (US)",
volume = "272",
pages = "3743--3755",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "14",

}

TY - JOUR

T1 - Biochemical characterization of the native Kv2.1 potassium channel

AU - Chung, Jean Ju

AU - Li, Min

PY - 2005/7

Y1 - 2005/7

N2 - Functional diversity of potassium channels in both prokaryotic and eukaryotic cells suggests multiple levels of regulation. Posttranslational regulation includes differential subunit assembly of homologous pore-forming subunits. In addition, a variety of modulatory subunits may interact with the pore complex either statically or dynamically. Kv2.1 is a delayed rectifier potassium channel isolated by expression cloning. The native polypeptide has not been purified, hence composition of the Kv2.1 channel complexes was not well understood. Here we report a biochemical characterization of Kv2.1 channel complexes from both recombinant cell lines and native rat brain. The channel complexes behave as large macromolecular complexes with an apparent oligomeric size of 650 kDa as judged by gel filtration chromatography. The molecular complexes have distinct biochemical populations detectable by a panel of antibodies. This is indicative of functional heterogeneity. Despite mRNA distribution in a variety of tissues, the native Kv2.1 polypeptides are more abundantly found in brain and have predominantly Kv2.1 subunits but not homologous Kv2.2 subunits. The proteins precipitated by anti-Kv2.1 and their physiological relevance are of interest for further investigation.

AB - Functional diversity of potassium channels in both prokaryotic and eukaryotic cells suggests multiple levels of regulation. Posttranslational regulation includes differential subunit assembly of homologous pore-forming subunits. In addition, a variety of modulatory subunits may interact with the pore complex either statically or dynamically. Kv2.1 is a delayed rectifier potassium channel isolated by expression cloning. The native polypeptide has not been purified, hence composition of the Kv2.1 channel complexes was not well understood. Here we report a biochemical characterization of Kv2.1 channel complexes from both recombinant cell lines and native rat brain. The channel complexes behave as large macromolecular complexes with an apparent oligomeric size of 650 kDa as judged by gel filtration chromatography. The molecular complexes have distinct biochemical populations detectable by a panel of antibodies. This is indicative of functional heterogeneity. Despite mRNA distribution in a variety of tissues, the native Kv2.1 polypeptides are more abundantly found in brain and have predominantly Kv2.1 subunits but not homologous Kv2.2 subunits. The proteins precipitated by anti-Kv2.1 and their physiological relevance are of interest for further investigation.

KW - Channels

KW - Oligomerization

KW - Potassium

KW - Proteomics

KW - Purification

UR - http://www.scopus.com/inward/record.url?scp=22544444516&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=22544444516&partnerID=8YFLogxK

U2 - 10.1111/j.1742-4658.2005.04802.x

DO - 10.1111/j.1742-4658.2005.04802.x

M3 - Article

C2 - 16008572

AN - SCOPUS:22544444516

VL - 272

SP - 3743

EP - 3755

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 14

ER -