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April 1, 1993Genes & DevelopmentOpen Access

p105 and p98 precursor proteins play an active role in NF-kappa B-mediated signal transduction.

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Authors

FMFrank MercurioTherapeutics Clinical ResearchJDJoseph A. DiDonatoCleveland ClinicCRCaridad RosetteLawrence Livermore National Laboratory

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Implication

Molecular study demonstrates cytoplasmic retention and processing of NF-kappa B by precursor proteins, indicating an alternative activation pathway.

Key Points

  • To determine whether the precursor proteins p105 and p98 actively participate in NF-kappa B-mediated signal transduction through interactions with other Rel family transcription factors.
  • Assayed complex formation between precursor proteins (p105 and p98) and Rel/NF-kappa B members, including p65 and c-Rel.
  • Assessed the subcellular localization of the associated subunits and monitored stimulus-dependent proteolytic processing of the complexes.
  • Both p105 and p98 formed stable complexes with p65 and c-Rel, which was sufficient to maintain cytoplasmic retention of these normally nuclear proteins.
  • Precursor complexes underwent stimulus-responsive proteolytic processing to generate active p50/c-Rel and p55/c-Rel complexes, revealing an alternative induction pathway distinct from classic I kappa B phosphorylation.

Cite This Study

Mercurio et al. (1993) studied this question.

synapsesocial.com/papers/6a1a7ad07ff99bba0645bd4ehttps://doi.org/10.1101/gad.7.4.705
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1I kappa B interacts with the nuclear localization sequences of the subunits of NF-kappa B: a mechanism for cytoplasmic retention.1992 · 719 citations
  2. 2Molecular Cloning and Characterization of a Novel Rel/NF-χB Family Member Displaying Structural and Functional Homology to NF-χB p50/p1051992 · 100 citations
  3. 3The v-rel oncogene product is complexed to a 40-kDa phosphoprotein in transformed lymphoid cells.1988 · 27 citations
  4. 4The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding.1992 · 233 citations