Identification of a new NEMO/TRAF6 interface affected in incontinentia pigmenti pathology (Articolo in rivista)

Type
Label
  • Identification of a new NEMO/TRAF6 interface affected in incontinentia pigmenti pathology (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1093/hmg/ddq222 (literal)
Alternative label
  • Gautheron J.; Pescatore A.; Fusco F.; Esposito E.; Yamaoka S.; Agou F.; Ursini M.V.; Courtois G. (2010)
    Identification of a new NEMO/TRAF6 interface affected in incontinentia pigmenti pathology
    in Human molecular genetics (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Gautheron J.; Pescatore A.; Fusco F.; Esposito E.; Yamaoka S.; Agou F.; Ursini M.V.; Courtois G. (literal)
Pagina inizio
  • 3138 (literal)
Pagina fine
  • 3149 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 19 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • PMID: 20529958 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 16 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • INSERM U781, Hopital Necker-Enfants Malades and Universite´ Paris-Descartes, 75015 Paris, France, Institute of Genetics and Biophysics 'Adriano Buzzati-Traverso' (CNR), 80131 Naples, Italy, Department of Molecular Virology, Tokyo Medical and Dental University, Tokyo 113-8519, Japan and Unite´ de Biochimie Structurale et Cellulaire, Institut Pasteur, CNRS, URA 2185, 75015 Paris, France (literal)
Titolo
  • Identification of a new NEMO/TRAF6 interface affected in incontinentia pigmenti pathology (literal)
Abstract
  • NF-kappaB Essential MOdulator (NEMO) has been shown to play a critical role in NF-kappaB activation, as the regulatory subunit of IkappaB kinase. Upon cell stimulation, NEMO can be modified through phosphorylation, sumoylation or ubiquitination. In the latter case, not much is known regarding the exact function of this posttranslational modification. One of the E3 ligase responsible for K63-linked NEMO polyubiquitination is TRAF6, which participates in several signaling pathways controlling immunity, osteoclastogenesis, skin development and brain functions. We previously observed a potentially important interaction between NEMO and TRAF6. In this study, we defined in more detail the domains required for this interaction, uncovering a new binding site for TRAF6 located at the amino-terminus of NEMO and recognized by the coiled-coil domain of TRAF6. This site appears to work in concert with the previously identified NEMO ubiquitin-binding domain which binds polyubiquitinated chains, suggesting a dual mode of TRAF6 recognition. We also showed that E57K mutation of NEMO found in a mild form of the genetic disease incontinentia pigmenti, resulted in impaired TRAF6 binding and IL-1beta signaling. In contrast, activation of NF-kappaB by TNF-alpha was not affected. These data demonstrate that NEMO/TRAF6 interaction has physiological relevance and might represent a new target for therapeutic purposes. (literal)
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