WWOX dysfunction induces sequential aggregation of TRAPPC6AΔ, TIAF1, tau and amyloid β, and causes apoptosis
Open accessAbstract
Aggregated vesicle-trafficking protein isoform TRAPPC6AΔ (TPC6AΔ) has a critical role in causing caspase activation, tau aggregation and A β generation in the brains of nondemented middle-aged humans, patients with Alzheimer’s disease (AD) and 3-week-old Wwox gene knockout mice. WWOX blocks neurodegeneration via interactions with tau and tau-phosphorylating enzymes. WWOX deficiency leads to epilepsy, mental retardation and early death. Here, we demonstrated that TGF-β 1 induces shuttling of endogenous wild-type TPC6A and TPC6AΔ in between nucleoli and mitochondria (~40–60 min per round trip), and WWOX reduces the shuttling time by 50%. TGF-β 1 initially maximizes the binding of TPC6AΔ to the C-terminal tail of WWOX, followed by dissociation. TPC6AΔ then undergoes aggregation, together with TIAF1 (TGF-β 1-induced antiapoptotic factor), in the mitochondria to induce apoptosis. An additional rescue scenario is that TGF-β 1 induces Tyr33 phosphorylation and unfolding of WWOX and its the N-terminal WW domain slowly binds TPC6AΔ to block aggregation and apoptosis. Similarly, loss of WWOX induces TPC6AΔ polymerization first, then aggregation of TIAF1, amyloid β and tau, and subsequent cell death, suggesting that a cascade of protein aggregation leads to neurodegeneration.
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WWOX may play a role in Alzheimer's disease through its interaction with tau.
“WWOX may play a role in Alzheimer’s disease through its interaction with tau28,29”
From Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing (2019) · cites this paper as [28]
WWOX has been implicated in several neurological phenotypes; it binds tau and may play a critical role in regulating tau hyper-phosphorylation, neurofibrillary formation and Aβ aggregation.
“WWOX has been implicated in several neurological phenotypes96; in addition, it binds tau and may play a critical role in regulating tau hyper-phosphorylation, neurofibrillary formation and Aβ aggregation28,29.”
From Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing (2019) · cites this paper as [28]
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Self-citation
- Authors
- Chang, J.-Y., & Chang, N.-S.
- Affiliations
- National Cheng Kung University (TW)
- Corresponding author
- Chang, N-S
- Venue
- Cell Death Discovery
- Published
- 2015-08-03
- Volume
- 1
- Issue
- 1
- Pages
- 15003-15003
- ISSN
- 2058-7716 (ISSN-L)
- PMC
- PMC4981022
- OpenAlex
- W2522568537
- Cited by
- 32
- References
- 47
- Citations by year
- 2026: 2 · 2024: 5 · 2023: 1 · 2022: 4 · 2021: 6 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 2 · 2016: 3 · 2015: 1
- FWCI
- 2.21
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Cell Death Discovery (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Defense (W81XWH-08–1-0682, W81XWH)
- American Society for Biochemistry and Molecular Biology
- National Science Council
- Ministry of Science and Technology, Taiwan (W81XWH-08-1-0682, 2320-B-006)
- National Health Research Institutes (NHRI-EX102)
- National Cheng Kung University
- National Institute of Biomedical Imaging and Bioengineering (R01EB002009)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- WWOX, tau aggregation, amyloid-beta, TGF-β1, protein aggregation, apoptosis, neurodegeneration, Alzheimer's disease, protein shuttling, WW domain, protein unfolding, caspase activation
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