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http://purl.uniprot.org/citations/21990363http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21990363http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21990363http://www.w3.org/2000/01/rdf-schema#comment"The enzyme carnitine palmitoyltransferase 1 (CPT1), which is anchored in the outer mitochondrial membrane (OMM), controls the rate-limiting step in fatty acid β-oxidation in mammalian tissues. It is inhibited by malonyl-CoA, the first intermediate of fatty acid synthesis, and it responds to OMM curvature and lipid characteristics, which reflect long term nutrient/hormone availability. Here, we show that the N-terminal regulatory domain (N) of CPT1A can adopt two complex amphiphilic structural states, termed Nα and Nβ, that interchange in a switch-like manner in response to offered binding surface curvature. Structure-based site-directed mutageneses of native CPT1A suggest Nα to be inhibitory and Nβ to be noninhibitory, with the relative Nα/Nβ ratio setting the prevalent malonyl-CoA sensitivity of the enzyme. Based on the amphiphilic nature of N and molecular modeling, we propose malonyl-CoA sensitivity to be coupled to the properties of the OMM by Nα-OMM associations that alter the Nα/Nβ ratio. For enzymes residing at the membrane-water interface, this constitutes an integrative regulatory mechanism of exceptional sophistication."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.306951"xsd:string
http://purl.uniprot.org/citations/21990363http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.306951"xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Ulmer T.S."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Ulmer T.S."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Estolt-Povedano S."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Estolt-Povedano S."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Rao J.N."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Rao J.N."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Warren G.Z."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Warren G.Z."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Zammit V.A."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/author"Zammit V.A."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/pages"42545-42554"xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/pages"42545-42554"xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/title"An environment-dependent structural switch underlies the regulation of carnitine palmitoyltransferase 1A."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/title"An environment-dependent structural switch underlies the regulation of carnitine palmitoyltransferase 1A."xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/21990363http://purl.uniprot.org/core/volume"286"xsd:string