ArticleFEBS letters2007
Differential trafficking of carboxyl isoforms of Ca2+-gated (Slo1) potassium channels.
Article in FEBS letters, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
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- Ion channels and channelopathies in glomeruli.Physiological reviews · 2023Review
- Pharmacological modulation of mitochondrial ion channels.British journal of pharmacology · 2019Review
- Colonic Potassium Absorption and Secretion in Health and Disease.Comprehensive Physiology · 2018Review
- The mitochondrial BKMitochondrion · 2017Article
- Tagging of Endogenous BK Channels with a Fluorogen-Activating Peptide Reveals β4-Mediated Control of Channel Clustering in Cerebellum.Frontiers in cellular neuroscience · 2017Article
- MaxiK channel interactome reveals its interaction with GABA transporter 3 and heat shock protein 60 in the mammalian brain.Neuroscience · 2016Article
- An unexpected journey: conceptual evolution of mechanoregulated potassium transport in the distal nephron.American journal of physiology. Cell physiology · 2016Review
- BK Channels in the Central Nervous System.International review of neurobiology · 2016Review
- Evidence for a KATP Channel in Rough Endoplasmic Reticulum (rerKATP Channel) of Rat Hepatocytes.PloS one · 2015Article
- Mitochondrial BKCa channel.Frontiers in physiology · 2015Review
- A splice variant of the two-pore domain potassium channel TREK-1 with only one pore domain reduces the surface expression of full-length TREK-1 channels.Pflugers Archiv : European journal of physiology · 2014Article
- MaxiK channel and cell signalling.Pflugers Archiv : European journal of physiology · 2014Review
- Functional insights into modulation of BKCa channel activity to alter myometrial contractility.Frontiers in physiology · 2014Review
- MitoBK(Ca) is encoded by the Kcnma1 gene, and a splicing sequence defines its mitochondrial location.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Palmitoylation of the β4-subunit regulates surface expression of large conductance calcium-activated potassium channel splice variants.The Journal of biological chemistry · 2013Article
- Role of the BK channel (KCa1.1) during activation of electrogenic K+ secretion in guinea pig distal colon.American journal of physiology. Gastrointestinal and liver physiology · 2012Article
- Intracellular BK(Ca) (iBK(Ca)) channels.The Journal of physiology · 2012Review
- Identification and quantification of full-length BK channel variants in the developing mouse cochlea.Journal of neuroscience research · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The pore-forming subunit of the large-conductance Ca(2+)-dependent K(+) (Slo1) channel is encoded by one gene. However, the functional properties of Slo1 channels are diverse in part because of their numerous regulatory mechanisms including posttranslational modification and alternative splicing. In particular, multiple splice variants of the pore-forming subunit have been reported but their significance is only beginning to be elucidated. Here we examined the cell biological properties of the three common C-terminal isoforms that differ in the last 8 (Slo1_ERL and Slo1_VYR) or 61 residues (Slo1_DEC). We found that Slo1_DEC, the longest isoform, shows dramatically reduced surface expression compared to that of Slo1_ERL or Slo1_VYR. Immunocytochemistry revealed that a large fraction of Slo1_DEC remains localized in endoplasmic reticulum (ER). Using a GST fusion protein containing the Slo1_DEC-specific sequence, affinity purification was carried out to isolate interacting proteins. The identified proteins include protein phosphatase 2A (PP2A-A), actin, and tubulin. The PP2A-A interaction is specific to Slo1_DEC and causes a significant reduction of phosphorylation in Slo1_DEC but not Slo1_ERL or Slo1_VYR. The results together support the notion that Slo1_DEC nucleates isoform-specific protein complexes and possesses a cis element(s) for regulating trafficking of the Slo1 channels.
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