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A single in-frame deletion of a codon for a glutamic acid residue within the TOR1A gene is linked to the autosomal-dominant movement disorder DYT1 dystonia, a condition characterized by involuntary muscle contractions that cause abnormal posture. This gene encodes the protein torsinA, and the functions of both wild-type and mutant (ΔE-torsinA) forms remain poorly understood. Previous studies based on overexpression systems indicated that wild-type torsinA resides mainly in the endoplasmic reticulum but that ΔE-torsinA is localized to the nuclear envelope or intracellular inclusions. This mutation-associated mis-localization has been proposed to underlie at least a part of the pathophysiology of DYT1 dystonia. However, the subcellular localization of torsinA has not been extensively studied when expressed at the endogenous level. Here we report an immunocytochemical analysis of torsinA proteins in cultured mouse neurons from a ΔE-torsinA knock-in model of DYT1 dystonia, where torsinA proteins are not upregulated. In all examined neurons of wild-type, heterozygous and homozygous mice, torsinA signal was found mainly near the Golgi apparatus, and only weakly in the endoplasmic reticulum and nuclear envelope. These results suggest that, in the absence of overexpression, torsinA proteins are localized near the Golgi apparatus and may influence cellular function involving the organelle. KEYWORDS DYT1 dystonia; endogenous protein; endoplasmic reticulum; Golgi apparatus; immunocytochemistry; neuron; nuclear envelope; overexpression; torsinA. ABBREVIATIONS DIC, differential interference contrast; ER, endoplasmic reticulum; GFP, green fluorescent protein; GM130, Golgi matrix protein of 130 kDa; GRP78/BiP, glucose-regulated protein of 78 kDa / binding immunoglobulin protein; LED, light-emitting diode; MEM, Minimum Essential Medium; NPC, nuclear pore complex; PBS, phosphate-buffered saline; PDI, protein disulfide isomerase; ROI, region of interest; ΔE, deletion of a single GAG codon in the TOR1A or Tor1a gene.
A single in-frame deletion of a codon for a glutamic acid residue within the TOR1A gene is linked to the autosomal-dominant movement disorder DYT1 dystonia, a condition characterized by involuntary muscle contractions that cause abnormal posture. This gene encodes the protein torsinA, and the functions of both wild-type and mutant (ΔE-torsinA) forms remain poorly understood. Previous studies based on overexpression systems indicated that wild-type torsinA resides mainly in the endoplasmic reticulum but that ΔE-torsinA is localized to the nuclear envelope or intracellular inclusions. This mutation-associated mis-localization has been proposed to underlie at least a part of the pathophysiology of DYT1 dystonia. However, the subcellular localization of torsinA has not been extensively studied when expressed at the endogenous level. Here we report an immunocytochemical analysis of torsinA proteins in cultured mouse neurons from a ΔE-torsinA knock-in model of DYT1 dystonia, where torsinA proteins are not upregulated. In all examined neurons of wild-type, heterozygous and homozygous mice, torsinA signal was found mainly near the Golgi apparatus, and only weakly in the endoplasmic reticulum and nuclear envelope. These results suggest that, in the absence of overexpression, torsinA proteins are localized near the Golgi apparatus and may influence cellular function involving the organelle. KEYWORDS DYT1 dystonia; endogenous protein; endoplasmic reticulum; Golgi apparatus; immunocytochemistry; neuron; nuclear envelope; overexpression; torsinA. ABBREVIATIONS DIC, differential interference contrast; ER, endoplasmic reticulum; GFP, green fluorescent protein; GM130, Golgi matrix protein of 130 kDa; GRP78/BiP, glucose-regulated protein of 78 kDa / binding immunoglobulin protein; LED, light-emitting diode; MEM, Minimum Essential Medium; NPC, nuclear pore complex; PBS, phosphate-buffered saline; PDI, protein disulfide isomerase; ROI, region of interest; ΔE, deletion of a single GAG codon in the TOR1A or Tor1a gene.
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