ArticleNeuroscience2007
Alternatively spliced C-terminal domains regulate the surface expression of large conductance calcium-activated potassium channels.
Article in Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Paraoxonase 3 regulates the pore-forming α subunit of the large-conductance KBiochimica et biophysica acta. Molecular cell research · 2025Article
- Article
- CaMolecules (Basel, Switzerland) · 2023Review
- Ion channels and channelopathies in glomeruli.Physiological reviews · 2023Review
- Identification of the Large-Conductance CaMolecules (Basel, Switzerland) · 2021Article
- Down-Regulation of CaInternational journal of molecular sciences · 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
- Fluorogenic Green-Inside Red-Outside (GIRO) Labeling Approach Reveals Adenylyl Cyclase-Dependent Control of BKα Surface Expression.Bioconjugate chemistry · 2015Article
- Podocytes … What's Under Yours? (Podocytes and Foot Processes and How They Change in Nephropathy).Frontiers in endocrinology · 2015Review
- Cell type-specific spatial and functional coupling between mammalian brain Kv2.1 K+ channels and ryanodine receptors.The Journal of comparative neurology · 2014Article
- MaxiK channel and cell signalling.Pflugers Archiv : European journal of physiology · 2014Review
- S-acylation dependent post-translational cross-talk regulates large conductance calcium- and voltage- activated potassium (BK) channels.Frontiers in physiology · 2014Review
- Intrinsic disorder in the BK channel and its interactome.PloS one · 2014Article
- Article
- Functional insights into modulation of BKCa channel activity to alter myometrial contractility.Frontiers in physiology · 2014Review
- Palmitoylation of the β4-subunit regulates surface expression of large conductance calcium-activated potassium channel splice variants.The Journal of biological chemistry · 2013Article
- Identification and quantification of full-length BK channel variants in the developing mouse cochlea.Journal of neuroscience research · 2011Article
- Neuronal fast activating and meningeal silent modulatory BK channel splice variants cloned from rat.Pflugers Archiv : European journal of physiology · 2011Article
- Cloning and distribution of Ca2+-activated K+ channels in lobster Panulirus interruptus.Neuroscience · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The Slo1 gene, also known as KCNMA1, encodes the pore-forming subunits of large-conductance Ca2+-activated K+ (BK(Ca)) channels. Products of this gene are widely expressed in vertebrate tissues, and occur in a large number (>or=20) of alternatively spliced variants that vary in their gating properties, susceptibility to modulation, and trafficking to the plasma membrane. Motifs in the large cytoplasmic C-terminal are especially important in determining the functional properties of BK(Ca) channels. Here we report that chick ciliary ganglion neurons express transcripts and proteins of two Slo1 splice variants that differ at the extreme C-terminal. We refer to these variants as VEDEC and QEDRL (or QEERL for the orthologous mammalian versions), after the five terminal amino acid residues in each isoform. Individual ciliary ganglion neurons preferentially express these variants in different subcellular compartments. Moreover, QEERL channels show markedly higher levels of constitutive expression on the plasma membrane than VEDEC channels in HEK293T and NG108-15 cells. However, growth factor treatment can stimulate surface expression of VEDEC channels to levels comparable to those seen with QEERL. In addition, we show that co-expression of a soluble protein composed of VEDEC C-terminal tail residues markedly increases cell surface expression of full-length VEDEC channels, suggesting that this region binds to proteins that cause retention of the these channels in intracellular stores.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.