Literature DB >> 10414301

Molecular diversity of K+ channels.

W A Coetzee1, Y Amarillo, J Chiu, A Chow, D Lau, T McCormack, H Moreno, M S Nadal, A Ozaita, D Pountney, M Saganich, E Vega-Saenz de Miera, B Rudy.   

Abstract

K+ channel principal subunits are by far the largest and most diverse of the ion channels. This diversity originates partly from the large number of genes coding for K+ channel principal subunits, but also from other processes such as alternative splicing, generating multiple mRNA transcripts from a single gene, heteromeric assembly of different principal subunits, as well as possible RNA editing and posttranslational modifications. In this chapter, we attempt to give an overview (mostly in tabular format) of the different genes coding for K+ channel principal and accessory subunits and their genealogical relationships. We discuss the possible correlation of different principal subunits with native K+ channels, the biophysical and pharmacological properties of channels formed when principal subunits are expressed in heterologous expression systems, and their patterns of tissue expression. In addition, we devote a section to describing how diversity of K+ channels can be conferred by heteromultimer formation, accessory subunits, alternative splicing, RNA editing and posttranslational modifications. We trust that this collection of facts will be of use to those attempting to compare the properties of new subunits to the properties of others already known or to those interested in a comparison between native channels and cloned candidates.

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Year:  1999        PMID: 10414301     DOI: 10.1111/j.1749-6632.1999.tb11293.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  383 in total

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8.  K(+) channel expression distinguishes subpopulations of parvalbumin- and somatostatin-containing neocortical interneurons.

Authors:  A Chow; A Erisir; C Farb; M S Nadal; A Ozaita; D Lau; E Welker; B Rudy
Journal:  J Neurosci       Date:  1999-11-01       Impact factor: 6.167

9.  Kv2 channels form delayed-rectifier potassium channels in situ.

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