ArticleJournal of cell science2021
Kv2 channel-AMIGO β-subunit assembly modulates both channel function and cell adhesion molecule surface trafficking.
Article in Journal of cell science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- AMIGO2 accelerates tumor progression by inducing a cancer stem cell-like phenotype.Scientific reports · 2025Article
- Kv2/Kv6.4 Heteromeric Potassium Channels Are Expressed in Spinal Motoneurons and Localized at C-Bouton Synapses.The European journal of neuroscience · 2025Article
- Distinct Electrophysiological Signatures Define Neuronal Subtypes in the Fasciola Cinereum.bioRxiv : the preprint server for biology · 2025Article
- A Kv2 inhibitor combination reveals native neuronal conductances consistent with Kv2/KvS heteromers.eLife · 2025Article
- An integrative approach prioritizes the orphan GPR61 genomic region in tissue-specific regulation of chronotype.Sleep advances : a journal of the Sleep Research Society · 2025Article
- 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
- Article
- Kv Channel Ancillary Subunits: Where Do We Go from Here?Physiology (Bethesda, Md.) · 2022Review
- Activity-dependent endoplasmic reticulum CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The AMIGO1 adhesion protein activates Kv2.1 voltage sensors.Biophysical journal · 2022Article
- AFrontiers in pharmacology · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Kv2 channels encode delayed rectifier currents that regulate membrane potential in many tissues. They also have a non-conducting function to form stable junctions between the endoplasmic reticulum and plasma membranes, creating membrane contact sites that mediate functions distinct from membrane excitability. Therefore, proteins that interact with Kv2.1 and Kv2.2 channels can alter conducting and/or non-conducting channel properties. One member of the AMIGO family of proteins is an auxiliary β-subunit for Kv2 channels and modulates Kv2.1 electrical activity. However, the AMIGO family has two additional members of ∼50% similarity that have not yet been characterized as Kv2 β-subunits. In this work, we show that the surface trafficking and localization of all three AMIGOs are controlled by their assembly with both Kv2 channels. Additionally, assembly of each AMIGO with either Kv2.1 or Kv2.2 hyperpolarizes the channel activation midpoint by -10 mV. However, only AMIGO2 significantly slows inactivation and deactivation, leading to a prolonged open state of Kv2 channels. The co-regulatory effects of Kv2s and AMIGOs likely fine-tune both the electrical and non-electrical properties of the cells in which they are expressed.
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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.