De-ubiquitylation is the most critical step in the ubiquitin-mediated homeostatic control of the NF-κB/IKK basal activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-11

AUTHORS

Linda Palma, Rita Crinelli, Marzia Bianchi, Mauro Magnani

ABSTRACT

The role of ubiquitylation in signal-induced activation of nuclear factor -kappaB (NF-kappaB) has been well established, while its involvement in maintaining NF-kappaB basal activity is less certain. Recent evidences demonstrate that in unstimulated cells, NF-kappaB homeostasis is actually the result of opposing forces: pro-activating activity of the IkappaB Kinase (IKK) and inhibitory activity of the Inhibitor of -kappaB (IkappaB) proteins. It is well known that endogenous de-ubiquitylating mechanisms are less effective on Ub motifs containing UbG76A. Here, we show that overexpression of a ubiquitin (Ub) G76A mutant leads to persistent activation of the IKK/NF-kappaB pathway in the absence of extra-cellular stimuli. In contrast, no effects on NF-kappaB activation were observed upon expression of UbK48R and UbK63R mutants, which are known to impair elongation of Lys(48)- and Lys(63)-linked poly-ubiquitin chains, respectively. Overall, these findings indicate that under basal conditions, the rate of de-ubiquitylation, rather than that of substrate ubiquitylation, is critical for the maintenance of appropriate levels of IKK/NF-kappaB activity. More... »

PAGES

69

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s11010-009-0146-x

    DOI

    http://dx.doi.org/10.1007/s11010-009-0146-x

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1028587826

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/19421711


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