Cotranslatioaal dimerization of the Rel homology domain of NF-κB1 generates p50-p105 heterodimers and is required for effective p50 production

Li Lin, George N. DeMartino, Warner C. Greene

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

Generation of the NF-κB p50 transcription factor is mediated by the proteasome. We found previously that p50 is generated during translation of the NFKB1 gene and that this cotranslational processing allows the production of both p50 and p105 from a single mRNA. We now demonstrate that the Rel homology domain in p50 undergoes cotranslational dimerization and that this interaction is required for efficient production of p50. We further show that this coupling of dimerization and proteasome processing during translation uniquely generates p50-p105 heterodimers. Accordingly, after the primary cotranslational event, additional posttranslational steps regulate p50 homodimer formation and the intracellular ratio of p50 and p105. This cellular strategy places p50 under the control of the p105 inhibitor early in its biogenesis, thereby regulating the pool of p50 homodimers within the cell.

Original languageEnglish (US)
Pages (from-to)4712-4722
Number of pages11
JournalEMBO Journal
Volume19
Issue number17
StatePublished - Sep 1 2000

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Dimerization
Proteasome Endopeptidase Complex
Processing
Transcription Factors
Genes
Messenger RNA

Keywords

  • Cotranslational dimerization
  • Cotranslational processing
  • NF-κB1
  • Proteasome

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Cotranslatioaal dimerization of the Rel homology domain of NF-κB1 generates p50-p105 heterodimers and is required for effective p50 production. / Lin, Li; DeMartino, George N.; Greene, Warner C.

In: EMBO Journal, Vol. 19, No. 17, 01.09.2000, p. 4712-4722.

Research output: Contribution to journalArticle

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