2021
An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel
Urrutia J, Aguado A, Gomis-Perez C, Muguruza-Montero A, Ballesteros OR, Zhang J, Nuñez E, Malo C, Chung HJ, Leonardo A, Bergara A, Villarroel A. An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel. BMC Biology 2021, 19: 109. PMID: 34020651, PMCID: PMC8138981, DOI: 10.1186/s12915-021-01040-1.Peer-Reviewed Original ResearchConceptsKv7.2 channelsChannel functionSequences of proteinsNon-native configurationsNascent chainsProper foldingEpilepsy-causing mutationsIQ motifResponsive domainHuman diseasesHelix ANative conformationFolding routeIon channelsKCNQ2 geneMutationsNeuronal compartmentsFoldingMisfoldingProteinKey pathogenic mechanismsPathogenic variantsSilico studiesPathogenic mechanismsSide chains
2012
Surface Expression and Subunit Specific Control of Steady Protein Levels by the Kv7.2 Helix A-B Linker
Aivar P, Fernández-Orth J, Gomis-Perez C, Alberdi A, Alaimo A, Rodríguez MS, Giraldez T, Miranda P, Areso P, Villarroel A. Surface Expression and Subunit Specific Control of Steady Protein Levels by the Kv7.2 Helix A-B Linker. PLOS ONE 2012, 7: e47263. PMID: 23115641, PMCID: PMC3480381, DOI: 10.1371/journal.pone.0047263.Peer-Reviewed Original ResearchConceptsB linkerPlasma membraneHelix ATetrameric channel assemblyIntracellular C-terminusAmino acid sequenceSteady-state amountsSurface expressionSteady-state levelsProtein degradationAcid sequenceC-terminusChannel assemblyFunctional channelsIntracellular distributionProtein levelsProteinSpecific controlKv7.2Detectable impactM-currentExpressionNeuronal excitabilityMembraneIntrinsic signals