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http://purl.uniprot.org/citations/11641277http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11641277http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11641277http://www.w3.org/2000/01/rdf-schema#comment"Spinal muscular atrophy (SMA) is a genetic disorder caused by mutations in the human survival of motor neuron 1 gene, SMN1. SMN protein is part of a large complex that is required for biogenesis of various small nuclear ribonucleoproteins (snRNPs). Here, we report that SMN interacts directly with the Cajal body signature protein, coilin, and that this interaction mediates recruitment of the SMN complex to Cajal bodies. Mutation or deletion of specific RG dipeptide residues within coilin inhibits the interaction both in vivo and in vitro. Interestingly, GST-pulldown experiments show that coilin also binds directly to SmB'. Competition studies show that coilin competes with SmB' for binding sites on SMN. Ectopic expression of SMN and coilin constructs in mouse embryonic fibroblasts lacking endogenous coilin confirms that recruitment of SMN and splicing snRNPs to Cajal bodies depends on the coilin C-terminal RG motif. A cardinal feature of SMA patient cells is a defect in the targeting of SMN to nuclear foci; our results uncover a role for coilin in this process."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.org/dc/terms/identifier"doi:10.1101/gad.908401"xsd:string
http://purl.uniprot.org/citations/11641277http://purl.org/dc/terms/identifier"doi:10.1101/gad.908401"xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Matera A.G."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Matera A.G."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Shpargel K.B."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Shpargel K.B."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Hebert M.D."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Hebert M.D."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Szymczyk P.W."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/author"Szymczyk P.W."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/pages"2720-2729"xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/pages"2720-2729"xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/title"Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/title"Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein."xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/11641277http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/11641277http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11641277
http://purl.uniprot.org/citations/11641277http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11641277