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http://purl.uniprot.org/citations/8522584http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8522584http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8522584http://www.w3.org/2000/01/rdf-schema#comment"The functional relationship between three Dictyostelium myosin Is, myoA, myoB, and myoC, has been examined through the creation of double mutants. Two double mutants, myoA-/B- and myoB-/C-, exhibit similar conditional defects in fluid-phase pinocytosis. Double mutants grown in suspension culture are significantly impaired in their ability to take in nutrients from the medium, whereas they are almost indistinguishable from wild-type and single mutant strains when grown on a surface. The double mutants are also found to internalize gp126, a 116-kD membrane protein, at a slower rate than either the wild-type or single mutant cells. Ultrastructural analysis reveals that both double mutants possess numerous small vesicles, in contrast to the wild-type or myosin I single mutants that exhibit several large, clear vacuoles. The alterations in fluid and membrane internalization in the suspension-grown double mutants, coupled with the altered vesicular profile, suggest that these cells may be compromised during the early stages of pinocytosis, a process that has been proposed to occur via actin-based cytoskeletal rearrangements. Scanning electron microscopy and rhodamine-phalloidin staining indicates that the myosin I double mutants appear to extend a larger number of actin-filled structures, such as filopodia and crowns, than wild-type cells. Rhodamine-phalloidin staining of the F-actin cytoskeleton of these suspension-grown cells also reveals that the double mutant cells are delayed in the rearrangement of cortical actin-rich structures upon adhesion to a substrate. We propose that myoA, myoB, and myoC play roles in controlling F-actin filled membrane projections that are required for pinosome internalization in suspension."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.org/dc/terms/identifier"doi:10.1083/jcb.131.5.1205"xsd:string
http://purl.uniprot.org/citations/8522584http://purl.org/dc/terms/identifier"doi:10.1083/jcb.131.5.1205"xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Reedy M.C."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Reedy M.C."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Novak K.D."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Novak K.D."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Peterson M.D."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Peterson M.D."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Titus M.A."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/author"Titus M.A."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/pages"1205-1221"xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/pages"1205-1221"xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/title"Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/title"Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis."xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/volume"131"xsd:string
http://purl.uniprot.org/citations/8522584http://purl.uniprot.org/core/volume"131"xsd:string
http://purl.uniprot.org/citations/8522584http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8522584
http://purl.uniprot.org/citations/8522584http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8522584