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http://purl.uniprot.org/citations/20339000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20339000http://www.w3.org/2000/01/rdf-schema#comment"Katanin p60 (kp60), a microtubule-severing enzyme, plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. We show that a single domain isolated from the N terminus of mouse katanin p60 (kp60-NTD) binds to tubulin. The solution structure of kp60-NTD was determined by NMR. Although their sequence similarities were as low as 20%, the structure of kp60-NTD revealed a striking similarity to those of the microtubule interacting and trafficking (MIT) domains, which adopt anti-parallel three-stranded helix bundle. In particular, the arrangement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, which is a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. Mutation studies revealed that the positively charged surface formed by helices 2 and 3 binds tubulin. This binding mode resembles the interaction between the MIT domain of Vps4 and Vps2/CHMP1a, a component of endosomal sorting complexes required for transport III. Our results show that both the molecular architecture and the binding modes are conserved between two AAA-ATPases, kp60 and Vps4. A common mechanism is evolutionarily conserved between two distinct cellular events, one that drives microtubule severing and the other involving membrane skeletal reorganization."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.108365"xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Akiyama K."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Fujiwara Y."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Shirakawa M."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Tochio H."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Ikegami T."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Mase S."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Goda N."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Hiroaki H."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Tenno T."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Kuwahara Y."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/author"Iwaya N."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/pages"16822-16829"xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/title"A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization."xsd:string
http://purl.uniprot.org/citations/20339000http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20339000http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20339000
http://purl.uniprot.org/citations/20339000http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20339000
http://purl.uniprot.org/uniprot/#_E9PZI6-mappedCitation-20339000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20339000
http://purl.uniprot.org/uniprot/#_A8K7S5-mappedCitation-20339000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20339000
http://purl.uniprot.org/uniprot/#_G3UWK1-mappedCitation-20339000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20339000
http://purl.uniprot.org/uniprot/#_E9QKG2-mappedCitation-20339000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20339000