A role for phosphorylation in the proteolytic processing of the human NF-KB1 precursor

Koutarou Fujimoto, Hideyo Yasuda, Yoshihisa Sato, Ken ichi Yamamoto

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

A precursor, p105, for one of the subunits (p50) of the NF-κB transcription factor, plays an important role in inducible expression of diverse cellular genes, p105 also functions as a cytoplasmic inhibitor for NF-κB, and the proteolytic processing of its inhibitory C-terminal region is required for generation of active NF-κB. Here, it is reported that the human p105 C-terminal region is phosphorylated in vivo on Ser894 and Ser908, which are potential phosphorylation sites in vitro for proline-directed serine/threonine kinases such as cyclin-dependent kinase. Furthermore, the mutation of these in vivo phosphorylation sites retards p105 processing in vivo, suggesting that p105 processing is regulated in a phosphorylation-dependent manner.

Original languageEnglish
Pages (from-to)183-189
Number of pages7
JournalGene
Volume165
Issue number2
DOIs
Publication statusPublished - 1995
Externally publishedYes

Keywords

  • Transcription factor
  • inflammation
  • p105
  • proteasome

ASJC Scopus subject areas

  • Genetics

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