2021
Age-dependent ataxia and neurodegeneration caused by an αII spectrin mutation with impaired regulation of its calpain sensitivity
Miazek A, Zalas M, Skrzymowska J, Bogin BA, Grzymajło K, Goszczynski TM, Levine ZA, Morrow JS, Stankewich MC. Age-dependent ataxia and neurodegeneration caused by an αII spectrin mutation with impaired regulation of its calpain sensitivity. Scientific Reports 2021, 11: 7312. PMID: 33790315, PMCID: PMC8012654, DOI: 10.1038/s41598-021-86470-1.Peer-Reviewed Original ResearchConceptsSpectrin cleavageCalpain cleavage sitesCalcium-activated proteaseGlobal neurodegenerationTraumatic encephalopathyC57BL/6J miceDendritic integrityExcessive activationNeuronal integrityProgressive ataxiaImpaired regulationCalpain activationCalpain sensitivityPhysiologic significanceNeurodegenerative diseasesNeuronal developmentCalpain proteolysisCalpain proteasesCalcium-dependent bindingAtaxiaNeurodegenerationCalpainActivated calpainSubstrate-level regulationCaM affinity
2009
Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP
Xu J, Kurup P, Zhang Y, Goebel-Goody SM, Wu PH, Hawasli AH, Baum ML, Bibb JA, Lombroso PJ. Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP. Journal Of Neuroscience 2009, 29: 9330-9343. PMID: 19625523, PMCID: PMC2737362, DOI: 10.1523/jneurosci.2212-09.2009.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsBrainCalpainCell DeathCells, CulturedCyclin-Dependent Kinase 5EndocytosisGlutamic AcidIn Vitro TechniquesMiceMice, KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Neuronsp38 Mitogen-Activated Protein KinasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateSynapsesConceptsStriatal-enriched protein tyrosine phosphataseCalpain cleavage sitesP38 activationCell deathCleavage siteExtracellular signal-regulated kinase 1/2Protein tyrosine phosphataseSignal-regulated kinase 1/2Promotes cell survivalActivation of p38Tyrosine phosphataseSubstrate bindingKinase 1/2ERK1/2 activationCalpain cleavageCell survivalNovel mechanismCalpain-mediated proteolysisReceptors coupleP38NMDAR stimulationPostsynaptic terminalsValid targetCleavage productsSTEP substrates
2007
The Phosphorylation State of GluR1 Subunits Determines the Susceptibility of AMPA Receptors to Calpain Cleavage*
Yuen EY, Liu W, Yan Z. The Phosphorylation State of GluR1 Subunits Determines the Susceptibility of AMPA Receptors to Calpain Cleavage*. Journal Of Biological Chemistry 2007, 282: 16434-16440. PMID: 17428797, DOI: 10.1074/jbc.m701283200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCalpainCells, CulturedCerebral CortexEnzyme ActivationNeuronsPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Processing, Post-TranslationalProtein SubunitsRatsRats, Sprague-DawleyReceptors, AMPATime FactorsConceptsCalpain cleavagePhosphorylation stateProteolytic cleavageDependent protein kinase IITerminal fusion proteinEffect of phosphorylationProtein phosphatase 1/2AProtein kinase IIPhosphorylation sitesProtein kinaseCalpain cleavage sitesGluR1 subunitKinase IIFusion proteinActive CaMKIIAMPAR currentsCalpain regulationCleavage siteIsoxazoleproprionic acid (AMPA) receptorSubunitsIonotropic glutamate receptorsN-methyl-D-aspartate receptorsPhysiological studiesExcitatory synaptic transmissionAMPA receptor currents
1997
Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †
Stabach P, Cianci C, Glantz S, Zhang Z, Morrow J. Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †. Biochemistry 1997, 36: 57-65. PMID: 8993318, DOI: 10.1021/bi962034i.Peer-Reviewed Original ResearchConceptsSite-directed mutagenesisAlpha II spectrinCalpain cleavage sitesCleavage siteII-spectrinHelix CRecombinant GST-fusion proteinsBona fide proteinGST fusion proteinTriple-helical motifsStrict substrate specificityFamily of Ca2Protein kinase CDynamic molecular modelingStructural repeatsProminent substrateDifferent amino acidsSubstrate specificityIntracellular proteolysisPenultimate residueCysteine proteasesKinase CMost proteasesSteroid receptor activationSpectrin
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