ArticleMolecular biology of the cell2018
Remodeling neuronal ER-PM junctions is a conserved nonconducting function of Kv2 plasma membrane ion channels.
Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Kv2/Kv6.4 Heteromeric Potassium Channels Are Expressed in Spinal Motoneurons and Localized at C-Bouton Synapses.The European journal of neuroscience · 2025Article
- External strain on the plasma membrane is relayed to the endoplasmic reticulum by membrane contact sites and alters cellular energetics.Science advances · 2025Article
- A Kv2 inhibitor combination reveals native neuronal conductances consistent with Kv2/KvS heteromers.eLife · 2025Article
- Regulation of Kv2.1 Channels by Kv9.1 Variants.Biomedicines · 2025Article
- The Electrically Silent Kv5.1 Subunit Forms Heteromeric Kv2 Channels in Cortical Neurons and Confers Distinct Functional Properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Glucocorticoids Rapidly Modulate CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell-cell contacts.The Journal of cell biology · 2024Article
- Downregulation of the silent potassium channel Kv8.1 increases motor neuron vulnerability in amyotrophic lateral sclerosis.Brain communications · 2024Article
- The formation of KCommunications biology · 2023Article
- Neuronal ER-plasma membrane junctions couple excitation to CaNature communications · 2023Article
- The formation of KResearch square · 2023Article
- Endoplasmic Reticulum-Plasma Membrane Junctions as Sites of Depolarization-Induced CaAnnual review of physiology · 2023Review
- ER-PM Junctions on GABAergic Interneurons Are Organized by Neuregulin 2/VAP Interactions and Regulated by NMDA Receptors.International journal of molecular sciences · 2023Article
- Non-conducting functions of ion channels: The case of integrin-ion channel complexes.Channels (Austin, Tex.) · 2022Review
- Increased KCells · 2022Article
- Pentameric assembly of the Kv2.1 tetramerization domain.Acta crystallographica. Section D, Structural biology · 2022Article
- The AMIGO1 adhesion protein activates Kv2.1 voltage sensors.Biophysical journal · 2022Article
- Role of the endoplasmic reticulum in synaptic transmission.Current opinion in neurobiology · 2022Review
- Phosphoinositide transport and metabolism at membrane contact sites.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2022Review
- High spatial density is associated with non-conducting Kv channels from two families.Biophysical journal · 2022Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The endoplasmic reticulum (ER) and plasma membrane (PM) form junctions crucial to ion and lipid signaling and homeostasis. The Kv2.1 ion channel is localized at ER-PM junctions in brain neurons and is unique among PM proteins in its ability to remodel these specialized membrane contact sites. Here, we show that this function is conserved between Kv2.1 and Kv2.2, which differ in their biophysical properties, modulation, and cellular expression. Kv2.2 ER-PM junctions are present at sites deficient in the actin cytoskeleton, and disruption of the actin cytoskeleton affects their spatial organization. Kv2.2-containing ER-PM junctions overlap with those formed by canonical ER-PM tethers. The ability of Kv2 channels to remodel ER-PM junctions is unchanged by point mutations that eliminate their ion conduction but eliminated by point mutations within the Kv2-specific proximal restriction and clustering (PRC) domain that do not impact their ion channel function. The highly conserved PRC domain is sufficient to transfer the ER-PM junction-remodeling function to another PM protein. Last, brain neurons in Kv2 double-knockout mice have altered ER-PM junctions. Together, these findings demonstrate a conserved in vivo function for Kv2 family members in remodeling neuronal ER-PM junctions that is distinct from their canonical role as ion-conducting channels shaping neuronal excitability.
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