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    TRAF6-mediated ubiquitination of NEMO requires p62/sequestosome-1

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    Version of Record-Open Access (930.7Kb)
    Date
    2014-03
    Author
    Zotti, Tiziana
    Scudiero, Ivan
    Settembre, Pio
    Ferravante, Angela
    Mazzone, Pellegrino
    D'Andrea, Luca
    Reale, Carla
    Vito, Pasquale
    Stilo, Romania
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    Abstract
    The atypical protein kinase C-interacting protein p62/sequestosome-1 (p62) has emerged as a crucial molecule in a variety of cellular functions due to its involvement in various signaling mechanisms. p62 has been implicated in the activation of NF-?B in TNF?-stimulated cells and has been shown to be activated in response to interleukin-1? (IL-1?). Here we demonstrate that p62 interacts with NEMO, the regulatory subunit of the complex responsible for activation of NF-?B transcription factor. Depletion of p62 obtained through a short interfering RNA targeting p62 mRNA abrogated TRAF6 capacity to promote NEMO ubiquitination and severely impairs NF-?B activation following IL-1? stimulation.Together, these results indicate that p62 is an important intermediary in the NF-?B activation pathways implemented through non-degradative ubiquitination events.
    DOI/handle
    http://dx.doi.org/10.1016/j.molimm.2013.10.015
    http://hdl.handle.net/10576/4265
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    • Biological & Environmental Sciences [‎200 ‎ items ]

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