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  • 1
    Publikationsdatum: 1997-11-05
    Beschreibung: Activation of the transcription factor nuclear factor kappa B (NF-kappaB) is controlled by sequential phosphorylation, ubiquitination, and degradation of its inhibitory subunit IkappaB. A large multiprotein complex, the IkappaB kinase (IKK) signalsome, was purified from HeLa cells and found to contain a cytokine-inducible IkappaB kinase activity that phosphorylates IkappaB-alpha and IkappaB-beta. Two components of the IKK signalsome, IKK-1 and IKK-2, were identified as closely related protein serine kinases containing leucine zipper and helix-loop-helix protein interaction motifs. Mutant versions of IKK-2 had pronounced effects on RelA nuclear translocation and NF-kappaB-dependent reporter activity, consistent with a critical role for the IKK kinases in the NF-kappaB signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercurio, F -- Zhu, H -- Murray, B W -- Shevchenko, A -- Bennett, B L -- Li, J -- Young, D B -- Barbosa, M -- Mann, M -- Manning, A -- Rao, A -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):860-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Signal Pharmaceuticals, Inc., 5555 Oberlin Drive, San Diego, CA 92121, USA. fmercuri@signalpharm.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346484" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Cell Cycle Proteins ; Cloning, Molecular ; Dual Specificity Phosphatase 1 ; Enzyme Activation ; HeLa Cells ; Helix-Loop-Helix Motifs ; Humans ; I-kappa B Kinase ; Immediate-Early Proteins/metabolism ; Leucine Zippers ; Molecular Sequence Data ; NF-kappa B/*metabolism ; *Phosphoprotein Phosphatases ; Phosphorylation ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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