ArticleBMC neuroscience2015
Presynaptic BK channel localization is dependent on the hierarchical organization of alpha-catulin and dystrobrevin and fine-tuned by CaV2 calcium channels.
Article in BMC neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
- Potential therapeutic targeting of BKMolecular oncology · 2026Review
- Hispidol Regulates Behavioral Responses to Ethanol through Modulation of BK Channels: A Novel Candidate for the Treatment of Alcohol Use Disorder.Molecules (Basel, Switzerland) · 2024Article
- Active Zone Trafficking of CaV2/UNC-2 Channels Is Independent of β/CCB-1 and α2δ/UNC-36 Subunits.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- CaInternational journal of molecular sciences · 2023Review
- Regulation of Neurotransmitter Release by KAdvances in neurobiology · 2023Article
- Emerging Roles of the α-Catenin Family Member α-Catulin in Development, Homeostasis and Cancer Progression.International journal of molecular sciences · 2022Review
- UNC-2 CaV2 Channel Localization at Presynaptic Active Zones Depends on UNC-10/RIM and SYD-2/Liprin-α inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Melatonin promotes sleep by activating the BK channel inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- BK channel clustering is required for normal behavioral alcohol sensitivity in C. elegans.Scientific reports · 2019Article
- Biophysical modeling of C. elegans neurons: Single ion currents and whole-cell dynamics of AWCon and RMD.PloS one · 2019Article
- BKIP-1, an auxiliary subunit critical to SLO-1 function, inhibits SLO-2 potassium channel in vivo.Scientific reports · 2017Article
- Supramolecular organization of NMDA receptors and the postsynaptic density.Current opinion in neurobiology · 2017Review
- ERG-28 controls BK channel trafficking in the ER to regulate synaptic function and alcohol response ineLife · 2017Article
- Presynaptic BK channels control transmitter release: physiological relevance and potential therapeutic implications.The Journal of physiology · 2016Review
- SLO BK Potassium Channels Couple Gap Junctions to Inhibition of Calcium Signaling in Olfactory Neuron Diversification.PLoS genetics · 2016Article
- BK Channels in the Central Nervous System.International review of neurobiology · 2016Review
- BK channels and alcohol tolerance: Insights from studies onMedicine internationalArticle
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundLarge conductance, calcium-activated BK channels regulate many important physiological processes, including smooth muscle excitation, hormone release and synaptic transmission. The biological roles of these channels hinge on their unique ability to respond synergistically to both voltage and cytosolic calcium elevations. Because calcium influx is meticulously regulated both spatially and temporally, the localization of BK channels near calcium channels is critical for their proper function. However, the mechanism underlying BK channel localization near calcium channels is not fully understood.
resultsWe show here that in C. elegans the localization of SLO-1/BK channels to presynaptic terminals, where UNC-2/CaV2 calcium channels regulate neurotransmitter release, is controlled by the hierarchical organization of CTN-1/α-catulin and DYB-1/dystrobrevin, two proteins that interact with cortical cytoskeletal proteins. CTN-1 organizes a macromolecular SLO-1 channel complex at presynaptic terminals by direct physical interaction. DYB-1 contributes to the maintenance or stabilization of the complex at presynaptic terminals by interacting with CTN-1. We also show that SLO-1 channels are functionally coupled with UNC-2 calcium channels, and that normal localization of SLO-1 to presynaptic terminals requires UNC-2. In the absence of UNC-2, SLO-1 clusters lose the localization specificity, thus accumulating inside and outside of presynaptic terminals. Moreover, CTN-1 is also similarly localized in unc-2 mutants, consistent with the direct interaction between CTN-1 and SLO-1. However, localization of UNC-2 at the presynaptic terminals is not dependent on either CTN-1 or SLO-1. Taken together, our data strongly suggest that the absence of UNC-2 indirectly influences SLO-1 localization via the reorganization of cytoskeletal proteins.
conclusionCTN-1 and DYB-1, which interact with cortical cytoskeletal proteins, are required for the presynaptic punctate localization of SLO-1 in a hierarchical manner. In addition, UNC-2 calcium channels indirectly control the fidelity of SLO-1 puncta localization at presynaptic terminals. We suggest that the absence of UNC-2 leads to the reorganization of the cytoskeletal structure that includes CTN-1, which in turn influences SLO-1 puncta localization.
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