NRBP1-Containing CRL2/CRL4A Regulates Amyloid β Production by Targeting BRI2 and BRI3 for Degradation

Takashi Yasukawa, Aya Tsutsui, Chieri Tomomori-Sato, Shigeo Sato, Anita Saraf, Michael P. Washburn, Laurence Florens, Tohru Terada, Kentaro Shimizu, Ronald C. Conaway, Joan W. Conaway, Teijiro Aso

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Yasukawa et al. demonstrate that BRI2 and BRI3, physiological inhibitors of Aβ production and aggregation, are substrates of NRBP1-ubiquitin ligase. In the presence of TSC22D3 and TSC22D4, a dimer of the substrate receptor NRBP1 assembles into a functional Cul2- and Cul4A-containing heterodimeric CRL through overlapping BC-box and cryptic H-box motifs on NRBP1.

Original languageEnglish (US)
Pages (from-to)3478-3491.e6
JournalCell Reports
Volume30
Issue number10
DOIs
StatePublished - Mar 10 2020
Externally publishedYes

Keywords

  • Alzheimer's disease
  • amyloid β
  • amyloid-β precursor protein/APP
  • BRI2/ITM2B
  • BRI3/ITM2C
  • CRL
  • Cullin
  • E3 ubiquitin ligase
  • NRBP1
  • ubiquitination

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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