Structure, G protein activation, and functional relevance of the cardiac G protein-gated K+ channel, IKACh

K Wickman; G Krapivinsky; S Corey; M Kennedy; J Nemec; I Medina; D E Clapham

doi:10.1111/j.1749-6632.1999.tb11300.x

Structure, G protein activation, and functional relevance of the cardiac G protein-gated K+ channel, IKACh

Ann N Y Acad Sci. 1999 Apr 30:868:386-98. doi: 10.1111/j.1749-6632.1999.tb11300.x.

Authors

K Wickman¹, G Krapivinsky, S Corey, M Kennedy, J Nemec, I Medina, D E Clapham

Affiliation

¹ Department of Cardiology, Howard Hughes Medical Institute, Harvard Medical School, Children's Hospital, Boston, Massachusetts 02115, USA.

PMID: 10414308
DOI: 10.1111/j.1749-6632.1999.tb11300.x

Abstract

The muscarinic-gated atrial potassium channel IKACh has been well characterized functionally, and has been an excellent model system for studying G protein/effector interactions. Complementary DNAs encoding the composite subunits of IKACh have been identified, allowing direct probing of structural and functional features of the channel. Here, we highlight recent approaches taken in our laboratory to determine the oligomeric structure of native cardiac IKACh, the mechanism of activation of IKACh by G proteins, and the relevance of IKACh to cardiac physiology.

MeSH terms

Amino Acid Sequence
Animals
Cattle
Cross-Linking Reagents / chemistry
Electrocardiography
Electrophysiology
G Protein-Coupled Inwardly-Rectifying Potassium Channels
GTP-Binding Proteins / metabolism*
Heart Atria / metabolism*
Heart Rate
Mice
Molecular Sequence Data
Peptide Fragments / pharmacology
Potassium Channels / chemistry
Potassium Channels / physiology*
Potassium Channels, Inwardly Rectifying*
Protein Conformation
Vagus Nerve / physiology

Substances

Cross-Linking Reagents
G Protein-Coupled Inwardly-Rectifying Potassium Channels
Peptide Fragments
Potassium Channels
Potassium Channels, Inwardly Rectifying
GTP-Binding Proteins