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http://purl.uniprot.org/citations/30601698http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30601698http://www.w3.org/2000/01/rdf-schema#comment"During podosome formation, distinct phosphatidylinositol 3,4,5-trisphosphate lipid (PI(3,4,5)P3) production and F-actin polymerization take place at integrin-mediated adhesions. Membrane-associated actin regulation factors, such as myosin-1, serve as key molecules to link phosphatidylinositol signals to podosome assembly. Here, we report that long-tailed myosin-1e (Myo1e) is enriched at the ventral layer of the podosome core in a PI(3,4,5)P3-dependent manner. The combination of TH1 and TH2 (TH12) of Myo1e tail domains contains the essential motif for PI(3,4,5)P3-dependent membrane association and ventral localization at the podosome. TH12 KR2A (K772A and R782A) becomes dissociated from the plasma membrane. While F-actin polymerizations are initialized from the ventral layer of the podosome, TH12 precedes the recruitment of N-WASP and Arp2/3 in the initial phase of podosome formation. Overexpression of TH12, not TH12 KR2A, impedes PI(3,4,5)P3 signaling, restrains F-actin polymerization, and inhibits podosome formation. TH12 also suppresses gelatin degradation and migration speed of invadopodia-forming A375 melanoma cells. Thus, TH12 domain of Myo1e serves as a regulatory component to connect phosphatidylinositol signaling to F-actin polymerization at the podosome."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e18-06-0398"xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/author"Feng Z."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/author"Krendel M."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/author"Cao F."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/author"Yu C.H."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/author"Sit B."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/name"Mol Biol Cell"xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/pages"622-635"xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/title"Tail domains of myosin-1e regulate phosphatidylinositol signaling and F-actin polymerization at the ventral layer of podosomes."xsd:string
http://purl.uniprot.org/citations/30601698http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/30601698http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30601698
http://purl.uniprot.org/citations/30601698http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30601698
http://purl.uniprot.org/uniprot/#_E9Q634-mappedCitation-30601698http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30601698
http://purl.uniprot.org/uniprot/#_Q12965-mappedCitation-30601698http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30601698
http://purl.uniprot.org/uniprot/#_Q3TLJ4-mappedCitation-30601698http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30601698
http://purl.uniprot.org/uniprot/#_Q4KMR3-mappedCitation-30601698http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30601698
http://purl.uniprot.org/uniprot/#_Q8C123-mappedCitation-30601698http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30601698
http://purl.uniprot.org/uniprot/Q3TLJ4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30601698
http://purl.uniprot.org/uniprot/Q8C123http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30601698
http://purl.uniprot.org/uniprot/Q12965http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30601698