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 language | English (US) |
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Pages (from-to) | 3478-3491.e6 |
Journal | Cell Reports |
Volume | 30 |
Issue number | 10 |
DOIs | |
State | Published - Mar 10 2020 |
Externally published | Yes |
Keywords
- Alzheimer's disease
- BRI2/ITM2B
- BRI3/ITM2C
- CRL
- Cullin
- E3 ubiquitin ligase
- NRBP1
- amyloid β
- amyloid-β precursor protein/APP
- ubiquitination
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology