hUBC9 associates with MEKK1 and type I TNF-α receptor and stimulates NFκB activity

Alan Saltzman, George Searfoss, Christophe Marcireau, Maureen Stone, Rose Ressner, Robin Munro, Carol Franks, Jill D'Alonzo, Bruno Tocque, Michael Jaye, Yuri Ivashchenko*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

hUBC9, an E2 ubiquitin conjugating enzyme, was identified by yeast two-hybrid screening and coprecipitation studies to interact with MEKK1 and the type I TNF-α receptor, respectively. Because both of these proteins regulate NFκB activity, the role of hUBC9 in modulating NFκB activity was investigated. Overexpression of hUBC9 in HeLa cells stimulated the activity of NFκB as detetermined by NFκB reporter and IL-6 secretion assays. hUBC9 also synergized with MEKK1 to activate NFκB reporter activity. Thus, hUBC9 modulates NFκB activity which, at least in part, can be attributed to its interaction with MEKK1 and the type I TNF-α receptor.

Original languageEnglish
Pages (from-to)431-435
Number of pages5
JournalFEBS Letters
Volume425
Issue number3
DOIs
StatePublished - 3 Apr 1998
Externally publishedYes

Keywords

  • MEKK1
  • Nuclear factor κB
  • Tumor necrosis factor-α
  • Ubiquitin conjugating enzyme
  • Yeast two-hybrid

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