Kv1.1 Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Kv1.1 is a voltage-gated potassium channel essential for neuronal excitability and synaptic transmission.
| Property |
Value |
| Protein Name |
Kv1.1 |
| Gene |
KCNA1 |
| UniProt ID |
P09488 |
| Molecular Weight |
~58 kDa |
| Subcellular Localization |
Neuronal membrane, axon initial segment |
| Protein Family |
Voltage-gated potassium channels (Shaker-like) |
Kv1.1 contains:
- 6 transmembrane segments
- Tetrameric assembly
- Cytoplasmic N- and C-termini with interaction domains
Kv1.1 regulates:
- Action potential repolarization
- Resting membrane potential
- Neurotransmitter release
- Repetitive firing properties
Mutations cause brief episodes of ataxia with myokymia (muscle rippling).
Channel hyperfunction causes continuous muscle activity.
Altered excitability can contribute to seizures.
| Approach |
Status |
Notes |
| Carbamazepine |
Approved |
Reduces neuronal excitability |
| Acetazolamide |
Approved |
Prevents episodes |
- Browne DL, et al. Episodic ataxia/myokymia syndrome. Nat Genet. 1994;8(2):136-40. PMID:7842010
The study of Kv1.1 Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
- Jan LY, et al. "Voltage-gated potassium channels." Annu Rev Neurosci. 1991;14:199-227. PMID:1840554
- Gutman GA, et al. "International Union of Pharmacology. LII. Nomenclature and molecular relationships of potassium channels." Pharmacol Rev. 2005;57(4):473-508. PMID:16382104
- Chandy KG, et al. "Voltage-gated potassium channels." Physiol Rev. 2021;101(3):1413-1481. PMID:33719549
- Alexander SP, et al. "The Concise Guide to Pharmacology 2021/22." Br J Pharmacol. 2021;178(Suppl 1):S1-S136. PMID:34537901
- Varga Z, et al. "Kv1 channel function in neurons." J Neurosci. 2004;24(39):8475-8479. PMID:15456830
Kv1.1 is a transmembrane protein of 655 amino acids with a molecular weight of ~71 kDa. Each subunit contains:
- N-terminus: Tetramerization domain (T1) for subunit assembly
- S1-S6 segments: Six transmembrane helices forming the voltage-sensing and pore domains
- P-loop: Between S5 and S6, forms the selectivity filter (GYG)
- C-terminus: Postsynaptic density and interaction domains
The crystal structure of Kv channels reveals:
- Symmetric tetrameric assembly around a central pore
- Voltage sensor domain (S1-S4) separated from the pore domain (S5-S6)
- Gate formed by the S6 helix bundle crossing at the intracellular mouth
¶ Channel Assembly and Trafficking
Kv1.1 assembles with:
- Kv1.2, Kv1.4: Form heteromeric channels with distinct properties
- Kvβ subunits: Cytoplasmic beta subunits that modify gating
- KChiP proteins: Cytoplasmic calcium sensors that enhance surface expression
- PSD-93/DLG1: Scaffolding proteins that anchor channels at synapses
Proper trafficking to the membrane requires assembly with beta subunits and correct folding in the ER.
| Property |
Value |
| Single channel conductance |
10-12 pS |
| Activation threshold |
-40 mV |
| Peak activation |
+20 mV |
| Deactivation time constant |
20-50 ms |
| Inactivation |
N-type and C-type |
- Dominant-negative mutations reduce channel function
- Results in neuronal hyperexcitability
- Causes epilepsy and ataxia
- Some mutations enhance channel activity
- May affect cardiac function
- Altered excitability patterns
Current research focuses on:
- Structure-function studies: Cryo-EM of Kv1.1 complexes
- Channelopathies: Genotype-phenotype correlations in EA1
- Drug discovery: Selective modulators for neurological disorders
- Gene therapy: Viral vector delivery of wild-type channels
Last updated: 2026-03-04