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http://purl.uniprot.org/citations/29615809http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29615809http://www.w3.org/2000/01/rdf-schema#comment"TAGLN is an actin-binding protein family that comprises three isoforms with theorized roles in smooth muscle differentiation, tumour development, lymphocyte activation, and brain chemistry. However, their fundamental characteristics in regulation of the actin-based cytoskeleton are not fully understood. Here we show that TAGLN2 (including TAGLN1 and TAGLN3) extensively nucleates G-actin polymerization under low-salt conditions, where polymerization would be completely suppressed. The calponin homology domain and actin-binding loop are essential to mechanically connect two adjacent G-actins, thereby mediating multimeric interactions. However, TAGLN2 blocked the Arp2/3 complex binding to actin filaments under physiological salt conditions, thereby inhibiting branched actin nucleation. In HeLa and T cells, TAGLN2 enhanced filopodium-like membrane protrusion. Collectively, the dual functional nature of TAGLN2-G-actin polymerization and Arp2/3 complex inhibition-may account for the mechanisms of filopodia development at the edge of Arp2/3-rich lamellipodia in various cell types."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.org/dc/terms/identifier"doi:10.1038/s41598-018-23816-2"xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Lee S."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Kim C.H."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Lee K.S."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Kim H.R."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Lee H.S."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Jung H.S."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Jun Y."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Kwon M.S."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Mun J.Y."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Jin M.S."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Jun C.D."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Piragyte I."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Na B.R."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Hyun Y.M."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Kim B.N.R."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/author"Mun Y."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/name"Sci Rep"xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/pages"5503"xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/title"TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions."xsd:string
http://purl.uniprot.org/citations/29615809http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/29615809http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29615809