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http://purl.uniprot.org/citations/35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35575797http://www.w3.org/2000/01/rdf-schema#comment"Multivesicular bodies (MVBs) contain intralumenal vesicles that are delivered to lysosomes for degradation or released extracellularly for intercellular signaling. Here, we identified Caenorhabditis elegans filamin FLN-2 as a novel regulator of MVB biogenesis. FLN-2 co-localizes with V-ATPase subunits on MVBs, and the loss of FLN-2 affects MVB biogenesis, reducing the number of MVBs in C. elegans hypodermis. FLN-2 associates with actin filaments and is required for F-actin organization. Like fln-2(lf) mutation, inactivation of the V0 or V1 sector of V-ATPase or inhibition of actin polymerization impairs MVB biogenesis. Super-resolution imaging shows that FLN-2 docks V-ATPase-decorated MVBs onto actin filaments. FLN-2 interacts via its calponin-homology domains with F-actin and the V1-E subunit, VHA-8. Our data suggest that FLN-2 mediates the docking of MVBs on the actin cytoskeleton, which is required for MVB biogenesis."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.org/dc/terms/identifier"doi:10.1083/jcb.202201020"xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/author"Yang C."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/author"Shi L."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/author"Hao T."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/author"Jian Y."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/name"J Cell Biol"xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/pages"e202201020"xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/title"Filamin FLN-2 promotes MVB biogenesis by mediating vesicle docking on the actin cytoskeleton."xsd:string
http://purl.uniprot.org/citations/35575797http://purl.uniprot.org/core/volume"221"xsd:string
http://purl.uniprot.org/citations/35575797http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35575797
http://purl.uniprot.org/citations/35575797http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/35575797
http://purl.uniprot.org/uniprot/#_A0A0K3AVH5-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_A0A0K3AVH8-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_A0A0K3AVI4-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_A0A0K3AW96-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_A0A0K3AWA2-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_A0A0K3AYH6-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_A0A0K3AYI1-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_D0VWL6-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797
http://purl.uniprot.org/uniprot/#_D0VWL7-mappedCitation-35575797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35575797