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http://purl.uniprot.org/citations/31754032http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31754032http://www.w3.org/2000/01/rdf-schema#comment"Inositol phosphates (IPs) comprise a network of phosphorylated molecules that play multiple signaling roles in eukaryotes. IPs synthesis is believed to originate with IP3 generated from PIP2 by phospholipase C (PLC). Here, we report that in mammalian cells PLC-generated IPs are rapidly recycled to inositol, and uncover the enzymology behind an alternative "soluble" route to synthesis of IPs. Inositol tetrakisphosphate 1-kinase 1 (ITPK1)-found in Asgard archaea, social amoeba, plants, and animals-phosphorylates I(3)P1 originating from glucose-6-phosphate, and I(1)P1 generated from sphingolipids, to enable synthesis of IP6 We also found using PAGE mass assay that metabolic blockage by phosphate starvation surprisingly increased IP6 levels in a ITPK1-dependent manner, establishing a route to IP6 controlled by cellular metabolic status, that is not detectable by traditional [3H]-inositol labeling. The presence of ITPK1 in archaeal clades thought to define eukaryogenesis indicates that IPs had functional roles before the appearance of the eukaryote."xsd:string
http://purl.uniprot.org/citations/31754032http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1911431116"xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/author"Miller G.J."xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/author"Saiardi A."xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/author"Desfougeres Y."xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/author"Laha D."xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/author"Wilson M.S.C."xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/pages"24551-24561"xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/title"ITPK1 mediates the lipid-independent synthesis of inositol phosphates controlled by metabolism."xsd:string
http://purl.uniprot.org/citations/31754032http://purl.uniprot.org/core/volume"116"xsd:string
http://purl.uniprot.org/citations/31754032http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31754032
http://purl.uniprot.org/citations/31754032http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31754032
http://purl.uniprot.org/uniprot/#_B4DE87-mappedCitation-31754032http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/#_G3V4M9-mappedCitation-31754032http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/#_Q13572-mappedCitation-31754032http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/#_Q8N3Y0-mappedCitation-31754032http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/#_Q6YL32-mappedCitation-31754032http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/Q8N3Y0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/Q6YL32http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/Q13572http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/G3V4M9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31754032
http://purl.uniprot.org/uniprot/B4DE87http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31754032