The DOI matches its Crossref record; 56 of the 57 references it cites were found in a registry or an index.
MiRP2 Forms Potassium Channels in Skeletal Muscle with Kv3.4 and Is Associated with Periodic Paralysis
Open accessAbstract
The subthreshold, voltage-gated potassium channel of skeletal muscle is shown to contain MinK-related peptide 2 (MiRP2) and the pore-forming subunit Kv3.4. MiRP2-Kv3.4 channels differ from Kv3.4 channels in unitary conductance, voltage-dependent activation, recovery from inactivation, steady-state open probability, and block by a peptide toxin. Thus, MiRP2-Kv3.4 channels set resting membrane potential (RMP) and do not produce afterhyperpolarization or cumulative inactivation to limit action potential frequency. A missense mutation is identified in the gene for MiRP2 (KCNE3) in two families with periodic paralysis and found to segregate with the disease. Mutant MiRP2-Kv3.4 complexes exhibit reduced current density and diminished capacity to set RMP. Thus, MiRP2 operates with a classical potassium channel subunit to govern skeletal muscle function and pathophysiology.
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“The MiRP2-Kv3.4 mutation reduces potassium efflux, resulting in hypokalemia. This condition decreases muscle membrane excitability, leading to muscle weakness and paralysis [19].”
From Thyrotoxic Hypokalemic Periodic Paralysis: Pathophysiological Mechanisms (2025) · cites this paper as [19]
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Cites
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MiRP1 Forms IKr Potassium Channels with HERG and Is Associated with Cardiac Arrhythmia
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Self-citationModulation of A-type potassium channels by a family of calcium sensors
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Nerbonne, J. M., & Kass, R. S. (2005) · Physiological Reviews · doi:10.1152/physrev.00002.2005 · Cited by 1,104
Plaster, N. M., Tawil, R., Tristani‐Firouzi, M., Canún, S., Bendahhou, S., Tsunoda, A., Donaldson, M. R., Iannaccone, S. T., Brunt, E. R. P., Barohn, R. J., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00342-7 · Cited by 993
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Voltage-gated potassium channels as therapeutic targets
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Metadata
- Authors
- Abbott, G. W., Butler, M. H., Bendahhou, S., Dalakas, M. C., Ptacek, L. J., & Goldstein, S. A. N.
- Affiliations
- Yale University (US)
- National Institutes of Health (US)
- Corresponding author
- Goldstein, Steve A.N
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 104
- Issue
- 2
- Pages
- 217-231
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2069886131
- Cited by
- 294
- References
- 57
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 4 · 2019: 6 · 2018: 4 · 2017: 4 · 2016: 7 · 2015: 5 · 2014: 9 · 2013: 11 · 2012: 5
- FWCI
- 11.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- National Center for Research Resources (MO1-RR-00064, M01RR000064)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Keywords
- KCNE3, Kv3.4, voltage-gated potassium channels, skeletal muscle, periodic paralysis, resting membrane potential, single-channel conductance, channel inactivation
- MeSH terms
- Animals, Cell Line, Cell Membrane, Chromosome Mapping, Chromosomes, Human, Pair 11, Cnidarian Venoms, Electrophysiology, Female, Cricetinae, Humans, Immunohistochemistry, Male, Membrane Potentials, Oocytes, Paralyses, Familial Periodic, Pedigree, Xenopus laevis, Potassium Channels, Patch-Clamp Techniques, Muscle, Skeletal, Mutation, Missense, Protein Subunits, Potassium Channels, Voltage-Gated, Xenopus Proteins, Mice, Rats, Shaw Potassium Channels
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