ArticleCellular and molecular life sciences : CMLS2014
OCIAD2 activates γ-secretase to enhance amyloid β production by interacting with nicastrin.
Article in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- OCIAD2 Stabilizes Integrin β1 Signaling Through SNX17-Mediated Endosomal Recycling to Lipid Rafts and Modulates Cisplatin Response in HNSCC.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Cerulenin partially corrects the disrupted developmental transcriptomic signature in Huntington's disease striatal medium spiny neurons.Stem cells (Dayton, Ohio) · 2025Article
- Ovarian carcinoma immunoreactive antigen-like protein 2 (OCIAD2) is a novel complex III-specific assembly factor in mitochondria.Molecular biology of the cell · 2022Article
- Ovarian carcinoma immunoreactive antigen domain 2 controls mitochondrial apoptosis in lung adenocarcinoma.Cancer science · 2021Article
- High temperature promotes amyloid β-protein production and γ-secretase complex formation via Hsp90.The Journal of biological chemistry · 2020Article
- Article
- OCIAD1 contributes to neurodegeneration in Alzheimer's disease by inducing mitochondria dysfunction, neuronal vulnerability and synaptic damages.EBioMedicine · 2020Article
- A double helical motif in OCIAD2 is essential for its localization, interactions and STAT3 activation.Scientific reports · 2018Article
- OCIAD2 suppressed tumor growth and invasion via AKT pathway in Hepatocelluar carcinoma.Carcinogenesis · 2017Article
- iRhom1 regulates proteasome activity via PAC1/2 under ER stress.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gamma (γ)-secretase holoenzyme is composed of four core proteins and cleaves APP to generate amyloid beta (Aβ), a key molecule that causes major neurotoxicity during the early stage of Alzheimer's disease (AD). However, despite its important role in Aβ production, little is known about the regulation of γ-secretase. OCIAD2, a novel modulator of γ-secretase that stimulates Aβ production, and which was isolated from a genome-wide functional screen using cell-based assays and a cDNA library comprising 6,178 genes. Ectopic expression of OCIAD2 enhanced Aβ production, while reduction of OCIAD2 expression suppressed it. OCIAD2 expression facilitated the formation of an active γ-secretase complex and enhanced subcellular localization of the enzyme components to lipid rafts. OCIAD2 interacted with nicastrin to stimulate γ-secretase activity. OCIAD2 also increased the interaction of nicastrin with C99 and stimulated APP processing via γ-secretase activation, but did not affect Notch processing. In addition, a cell-permeable Tat-OCIAD2 peptide that interfered with the interaction of OCIAD2 with nicastrin interrupted the γ-secretase-mediated AICD production. Finally, OCIAD2 expression was significantly elevated in the brain of AD patients and PDAPP mice. This study identifies OCIAD2 as a selective activator of γ-secretase to increase Aβ generation.
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Registered trials
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