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http://purl.uniprot.org/citations/11809832http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11809832http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11809832http://www.w3.org/2000/01/rdf-schema#comment"Actin-depolymerizing factor (ADF)/cofilins are essential regulators of actin filament turnover. Several ADF/cofilin isoforms are found in multicellular organisms, but their biological differences have remained unclear. Herein, we show that three ADF/cofilins exist in mouse and most likely in all other mammalian species. Northern blot and in situ hybridization analyses demonstrate that cofilin-1 is expressed in most cell types of embryos and adult mice. Cofilin-2 is expressed in muscle cells and ADF is restricted to epithelia and endothelia. Although the three mouse ADF/cofilins do not show actin isoform specificity, they all depolymerize platelet actin filaments more efficiently than muscle actin. Furthermore, these ADF/cofilins are biochemically different. The epithelial-specific ADF is the most efficient in turning over actin filaments and promotes a stronger pH-dependent actin filament disassembly than the two other isoforms. The muscle-specific cofilin-2 has a weaker actin filament depolymerization activity and displays a 5-10-fold higher affinity for ATP-actin monomers than cofilin-1 and ADF. In steady-state assays, cofilin-2 also promotes filament assembly rather than disassembly. Taken together, these data suggest that the three biochemically distinct mammalian ADF/cofilin isoforms evolved to fulfill specific requirements for actin filament dynamics in different cell types."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.org/dc/terms/identifier"doi:10.1091/mbc.01-07-0331"xsd:string
http://purl.uniprot.org/citations/11809832http://purl.org/dc/terms/identifier"doi:10.1091/mbc.01-07-0331"xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Lappalainen P."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Lappalainen P."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Partanen J."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Partanen J."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Ojala P.J."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Ojala P.J."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Thesleff I."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Thesleff I."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Vartiainen M.K."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Vartiainen M.K."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Mustonen T."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Mustonen T."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Mattila P.K."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/author"Mattila P.K."xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/pages"183-194"xsd:string
http://purl.uniprot.org/citations/11809832http://purl.uniprot.org/core/pages"183-194"xsd:string