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http://purl.uniprot.org/citations/16505168http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16505168http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16505168http://www.w3.org/2000/01/rdf-schema#comment"The microtubule motor cytoplasmic dynein and its activator dynactin drive vesicular transport and mitotic spindle organization. Dynactin is ubiquitously expressed in eukaryotes, but a G59S mutation in the p150Glued subunit of dynactin results in the specific degeneration of motor neurons. This mutation in the conserved cytoskeleton-associated protein, glycine-rich (CAP-Gly) domain lowers the affinity of p150Glued for microtubules and EB1. Cell lines from patients are morphologically normal but show delayed recovery after nocodazole treatment, consistent with a subtle disruption of dynein/dynactin function. The G59S mutation disrupts the folding of the CAP-Gly domain, resulting in aggregation of the p150Glued protein both in vitro and in vivo, which is accompanied by an increase in cell death in a motor neuron cell line. Overexpression of the chaperone Hsp70 inhibits aggregate formation and prevents cell death. These data support a model in which a point mutation in p150Glued causes both loss of dynein/dynactin function and gain of toxic function, which together lead to motor neuron cell death."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200511068"xsd:string
http://purl.uniprot.org/citations/16505168http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200511068"xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Ranganathan S."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Ranganathan S."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Fischbeck K.H."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Fischbeck K.H."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Tokito M.K."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Tokito M.K."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Holzbaur E.L.F."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Holzbaur E.L.F."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Caviston J.P."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Caviston J.P."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Harmison G.G."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Harmison G.G."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Sumner C.J."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Sumner C.J."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"LaMonte B.H."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"LaMonte B.H."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Levy J.R."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Levy J.R."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Ligon L.A."xsd:string
http://purl.uniprot.org/citations/16505168http://purl.uniprot.org/core/author"Ligon L.A."xsd:string