Subunit-dependent assembly of inward-rectifier K+ channels

E. Glowatzki, G. Fakler, U. Brandle, U. Rexhausen, H. P. Zenner, J. P. Ruppersberg, B. Fakler

Research output: Contribution to journalArticle

Abstract

Inward-rectifier, G-protein-regulated and ATP-dependent K+ channels form a novel gene family of related proteins which share two transmembrane segments as a common structural feature. These K+ channels are only distantly related to the voltage-gated Shaker-type K+ channels comprising six extensively studied in the past, little is known about subunit assembly of inward-rectifier K+ channels. Differential sensitivity of inward-rectifier K+ channels to voltage-dependent pore block by spermine was used to analyse subunit assembly. It is shown that inward-rectifier K+ channel proteins are composed of four subunits whose assembly obeys the rules of a binomial distribution. 'Strong' and 'mild' inward-rectifier K+ channel subunits (BIR10 and ROMK1) which are co-expressed in individual auditory hair cells form hetero-tetramers. Distribution of these hetero-tetramers, however, is not binomial. Hetero- and homo-oligomeric channels form with similar probabilities resulting in independent channel populations with distinct functional properties.

Original languageEnglish (US)
Pages (from-to)251-261
Number of pages11
JournalProceedings of the Royal Society B: Biological Sciences
Volume261
Issue number1361
DOIs
StatePublished - Jan 1 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Environmental Science(all)
  • Agricultural and Biological Sciences(all)

Fingerprint Dive into the research topics of 'Subunit-dependent assembly of inward-rectifier K<sup>+</sup> channels'. Together they form a unique fingerprint.

  • Cite this

    Glowatzki, E., Fakler, G., Brandle, U., Rexhausen, U., Zenner, H. P., Ruppersberg, J. P., & Fakler, B. (1995). Subunit-dependent assembly of inward-rectifier K+ channels. Proceedings of the Royal Society B: Biological Sciences, 261(1361), 251-261. https://doi.org/10.1098/rspb.1995.0145