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NRBF2 plays an important role in regulating degradation of APP-C-terminal fragments through modulating autophagy.
Here we show that a putative fifth subunit, nuclear receptor binding factor 2 (NRBF2), is a tightly bound component of the class III phosphatidylinositol 3-kinase complex I that profoundly affects its activity and architecture. NRBF2 is a homodimer and drives the dimerization of the larger PI3KC3-C1 complex, with implications for the higher-order organization of the preautophagosomal structure.
This study reveals NRBF2 as a critical molecular switch of PtdIns3K and autophagy activation, and its on/off state is precisely controlled by MTORC1 through phosphorylation.
Atg38 and its human ortholog NRBF2, accessory components of complex I consisting of Vps15-Vps34-Vps30/Atg6-Atg14 (yeast) and PIK3R4/VPS15-PIK3C3/VPS34-BECN1/Beclin 1-ATG14 (human), were characterized.
Polymorphisms in a putative enhancer at the 10q21.2 Breast Cancer Risk Locus regulate NRBF2 expression, implicating this gene in the etiology of breast cancer.
Nrbf2 may interact with the Atg14L-containing Beclin 1-Vps34 protein complex to modulate protein-protein interactions within the complex.
NRBF2 regulates macroautophagy as a component of Vps34 Complex I.
The activation domain, their small size (COPR1, 26.9 kDa; COPR2, 32.4 kDa), and strict dependence on AF-2 for interaction distinguish COPR1 and COPR2 from the SMRT/NCoR type of corepressor and may dampen rather than repress NR-mediated gene expression.
These data reveal a key role for NRBF2 in the assembly of the specific Atg14L-Beclin 1-Vps34-Vps15 complex for autophagy induction.
May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro).
comodulator of PPAR and RXR 1
, comodulator of PPAR and RXR 2
, nuclear receptor binding factor-2
, nuclear receptor-binding factor 2