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The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein

A glutamic acid deletion (ΔE) in the AAA+ protein torsinA causes DYT1 dystonia. Although the majority of torsinA resides within the endoplasmic reticulum (ER), torsinA binds a substrate in the lumen of the nuclear envelope (NE), and the ΔE mutation enhances this interaction. Using a novel cell-based...

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Autores principales: Goodchild, Rose E., Dauer, William T.
Formato: Artigo
Lenguaje:Inglês
Publicado: The Rockefeller University Press 2005
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC2171781/
https://ncbi.nlm.nih.gov/pubmed/15767459
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1083/jcb.200411026
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