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http://purl.uniprot.org/citations/20026655http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20026655http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20026655http://www.w3.org/2000/01/rdf-schema#comment"Knockdown of the actin-severing protein actin-depolymerizing factor (ADF)/cofilin inhibited export of an exogenously expressed soluble secretory protein from Golgi membranes in Drosophila melanogaster and mammalian tissue culture cells. A stable isotope labeling by amino acids in cell culture mass spectrometry-based protein profiling revealed that a large number of endogenous secretory proteins in mammalian cells were not secreted upon ADF/cofilin knockdown. Although many secretory proteins were retained, a Golgi-resident protein and a lysosomal hydrolase were aberrantly secreted upon ADF/cofilin knockdown. Overall, our findings indicate that inactivation of ADF/cofilin perturbed the sorting of a subset of both soluble and integral membrane proteins at the trans-Golgi network (TGN). We suggest that ADF/cofilin-dependent actin trimming generates a sorting domain at the TGN, which filters secretory cargo for export, and that uncontrolled growth of this domain causes missorting of proteins. This type of actin-dependent compartmentalization and filtering of secretory cargo at the TGN by ADF/cofilin could explain sorting of proteins that are destined to the cell surface."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200908040"xsd:string
http://purl.uniprot.org/citations/20026655http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200908040"xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Molina H."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Molina H."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Duran J.M."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Duran J.M."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Malhotra V."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Malhotra V."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Alleaume A.M."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Alleaume A.M."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Egorov M."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Egorov M."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Forlanelli E."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Forlanelli E."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Polishchuk R."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"Polishchuk R."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"von Blume J."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/author"von Blume J."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/20026655http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string