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Article

Interacting effects of N-terminal variation and strex exon splicing on slo potassium channel regulation by calcium, phosphorylation, and oxidation.

The Journal of biological chemistry - 26 Jul 2002

Erxleben Christian, Everhart Angela L, Romeo Charles, Florance Hannah, Bauer Mary Beth, Alcorta David A, Rossie Sandra, Shipston Michael J, Armstrong David L

Abstract excerpt

We have investigated the structural basis for the phenotype of a native rat Slo (rSlo) potassium channel (BK(Ca); KCNMA1) in a rat pituitary cell line, GH(4)C(1). Opposing regulation of these calcium- and voltage-activated potassium channels by cAMP- and cGMP-dependent protein kinases requires an alternatively spliced exon (strex) of 59 amino acids in the cytoplasmic C terminus of the pore-forming alpha subunit...

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Source

Identifiers

PMID: 12016222
DOI: 10.1074/jbc.M203087200

Genes

KCNMA1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Interacting effects of N-terminal variation and strex exon splicing on slo potassium channel regulation by calcium, phosphorylation, and oxidation.PMID 12016222Read ↗

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