ArticleThe Journal of biological chemistry2012
An electrostatic switch controls palmitoylation of the large conductance voltage- and calcium-activated potassium (BK) channel.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Topology-Driven Discovery of Transmembrane ProteinbioRxiv : the preprint server for biology · 2024Article
- Regulating neuronal excitability: The role ofPNAS nexus · 2024Article
- Palmitoylation of Voltage-Gated Ion Channels.International journal of molecular sciences · 2022Review
- A sticky situation: regulation and function of protein palmitoylation with a spotlight on the axon and axon initial segment.Neuronal signaling · 2021Review
- Distinct lipid bilayer compositions have general and protein-specific effects on K+ channel function.The Journal of general physiology · 2021Article
- Site-specific deacylation by ABHD17a controls BK channel splice variant activity.The Journal of biological chemistry · 2020Article
- A polybasic motif in alternatively spliced KChIP2 isoforms prevents CaThe Journal of biological chemistry · 2019Article
- Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-mediated myotube formation.Nature communications · 2018Article
- Understanding the rules governing NCX1 palmitoylation.Channels (Austin, Tex.) · 2017Article
- Global, site-specific analysis of neuronal protein S-acylation.Scientific reports · 2017Article
- Distinct domains of the β1-subunit cytosolic N terminus control surface expression and functional properties of large-conductance calcium-activated potassium (BK) channels.The Journal of biological chemistry · 2017Article
- Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane.eLife · 2017Article
- Fluorogenic Green-Inside Red-Outside (GIRO) Labeling Approach Reveals Adenylyl Cyclase-Dependent Control of BKα Surface Expression.Bioconjugate chemistry · 2015Article
- The physiology of protein S-acylation.Physiological reviews · 2015Review
- Ion channel regulation by protein S-acylation.The Journal of general physiology · 2014Review
- S-acylation dependent post-translational cross-talk regulates large conductance calcium- and voltage- activated potassium (BK) channels.Frontiers in physiology · 2014Review
- Regulation of large conductance calcium- and voltage-activated potassium (BK) channels by S-palmitoylation.Biochemical Society transactions · 2013Article
- A BK (Slo1) channel journey from molecule to physiology.Channels (Austin, Tex.)Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein palmitoylation is a major dynamic posttranslational regulator of protein function. However, mechanisms that control palmitoylation are poorly understood. In many proteins, palmitoylation occurs at cysteine residues juxtaposed to membrane-anchoring domains such as transmembrane helices, sites of irreversible lipid modification, or hydrophobic and/or polybasic domains. In particular, polybasic domains represent an attractive mechanism to dynamically control protein palmitoylation, as the function of these domains can be dramatically influenced by protein phosphorylation. Here we demonstrate that a polybasic domain immediately upstream of palmitoylated cysteine residues within an alternatively spliced insert in the C terminus of the large conductance calcium- and voltage-activated potassium channel is an important determinant of channel palmitoylation and function. Mutation of basic amino acids to acidic residues within the polybasic domain results in inhibition of channel palmitoylation and a significant right-shift in channel half maximal voltage for activation. Importantly, protein kinase A-dependent phosphorylation of a single serine residue within the core of the polybasic domain, which results in channel inhibition, also reduces channel palmitoylation. These data demonstrate the key role of the polybasic domain in controlling stress-regulated exon palmitoylation and suggests that phosphorylation controls the domain by acting as an electrostatic switch.
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Registered trials
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.