title: ATP-sensitive association of mortalin with the IL-1 receptor type I.
abstract: Interleukin-1 (IL-1) is a major proinflammatory cytokine mediating local and systemic responses of the immune system. Two types of IL-1 receptors are known, but only the IL-1 receptor type I initiates biological responses. Here we show that two proteins with nucleic acid binding potential and mortalin, a member of the HSP70-family, are associated with the IL-1 receptor type I irrespective of IL-1 binding. The association of mortalin with the IL-1 receptor type I is specifically reversed by ATP concentrations in the physiological range. Other nucleotides are not or much less effective. The in vitro dissociation of mortalin effects neither the receptor association nor the activity of IRAK, which initiates the IL-1-dependent phosphorylation cascade. The roles of the receptor-associated proteins are therefore discussed in the context of receptor internalisation.
authors.affiliation: Technical University of Braunschweig, Department of Biochemistry, Germany.
authors.forename: G
authors.initials: G
authors.lastname: Sacht
authors.forename: R
authors.initials: R
authors.lastname: Brigelius-Flohé
authors.forename: M
authors.initials: M
authors.lastname: Kiess
authors.forename: H
authors.initials: H
authors.lastname: Sztajer
authors.forename: L
authors.initials: L
authors.lastname: Flohé
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000818:Animals; D022762:CCAAT-Enhancer-Binding Proteins; D002352:Carrier Proteins; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007375:Interleukin-1 / Q000378:metabolism / Q000494:pharmacology; D053592:Interleukin-1 Receptor-Associated Kinases; D051379:Mice; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D009711:Nucleotides / Q000494:pharmacology; D015514:Oncogene Proteins, Fusion / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D011485:Protein Binding / Q000187:drug effects; D011494:Protein Kinases / Q000378:metabolism; D034702:RNA-Binding Protein FUS; D017472:Receptors, Interleukin-1 / Q000378:metabolism*; D053573:Receptors, Interleukin-1 Type I; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D051742:Transcription Factor CHOP; D014407:Tumor Cells, Cultured
chemical_list: D022762:CCAAT-Enhancer-Binding Proteins; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D018840:HSP70 Heat-Shock Proteins; C492001:HSPA9 protein, human; C083794:Hspa9 protein, mouse; D007375:Interleukin-1; D024101:Mitochondrial Proteins; D009687:Nuclear Proteins; D009711:Nucleotides; D015514:Oncogene Proteins, Fusion; D034702:RNA-Binding Protein FUS; D017472:Receptors, Interleukin-1; D053573:Receptors, Interleukin-1 Type I; C106030:TLS-CHOP fusion protein, human; C080352:mortalin; D051742:Transcription Factor CHOP; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D053592:Interleukin-1 Receptor-Associated Kinases