Cofilin Suppresses Tau-Induced Defects in Dense-Core Granule Formation and Aβ-Induced Neurodegeneration
Bhavna VermaiD, Amy Cording, Lewis BlincoweiD, Shauna Rice, Harrison Vine, S. Mark Wainwright, Deborah C. I. GoberdhaniD, Clive Wilson
Abstract
Intracellular neurofibrillary tangles formed from hyperphosphorylated tau and extracellular amyloid plaques containing aggregated A{beta}-peptides, specific cleavage products of the Amyloid Precursor Protein (APP), are the primary histopathological hallmarks of Alzheimers Disease (AD), the leading cause of dementia in humans. However, the initiating steps that lead to these pathologies and early neurodegeneration, and the mechanisms by which tau- and A{beta}-induced effects might be linked remain unclear. Using the prostate-like secondary cell (SC) in Drosophila, we recently showed that A{beta} modulates normal APP- and membrane-associated protein aggregation in the dense-core granule (DCG) compartments of the regulated secretory pathway by interfering with subsequent membrane:DCG dissociation. This disrupts endolysosomal trafficking and propagates the resulting endolysosomal defects to other cells that endocytose the secreted abnormal DCG proteins. Here we show that overexpressing human tau also disrupts DCG aggregation and membrane:DCG dissociation inside SC secretory compartments, leading to increased endolysosomal targeting of these compartments. In a genetic screen, we find that knockdown of cofilin, which encodes an actin-severing protein required for dynamic remodelling of microfilaments, generates a similar phenotype. Consistent with this, overexpression of Cofilin, which is known to suppress tau-induced neurodegeneration in flies, reduces tau-induced DCG defects in SCs. Indeed, we find that Cofilin overexpression also suppresses A{beta}-induced degeneration in the fly eye. We conclude that membrane:DCG aggregate dissociation in DCG compartments is disrupted by both tau- and A{beta}-induced genetic changes that are relevant to AD, and this partially involves inhibition of actin cytoskeleton dynamics. Increasing actin remodelling activity can suppress neurodegeneration induced by both tau and A{beta}, suggesting that this process provides an important functional link between them that might be targeted therapeutically.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 0
- Organism
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Tauopathy primes co-filament assembly and dysfunction of TDP-43
Meghraj Singh Baghel, Grace D. Burns, … Philip C. Wong·bioRxiv·May 14, 2026
- How Alzheimer's Abeta propagates and triggers tau pathology in intact neurons
Tomoya Sasahara, Shoko Hongo, … Minako M. Hoshi·bioRxiv·Aug 28, 2024
- Tau-tubulin kinase 1 and amyloid-β peptide induce phosphorylation of collapsin response mediator protein-2 and enhance neurite degeneration in Alzheimer disease mouse models
Seiko Ikezu, Kaitlin L. Ingraham Dixie, … Tsuneya Ikezu·Acta Neuropathologica CommunicationsPeer-reviewed·Feb 4, 2020
- Seed structure and phosphorylation in the fuzzy coat impact tau seeding competency
Alysa Kasen, Sofia Lövestam, … Michael X. Henderson·Nature CommunicationsPeer-reviewed·Oct 17, 2025
- Intrahippocampal delivery of hyperphosphorylated human tau oligomers induces neurodegeneration in non-transgenic wildtype mice
Hong‐Ru Chen, Hsiao‐Tien Chien Hagar, … Chia-Yi Kuan·bioRxiv·Mar 10, 2025
- Amyloid beta oligomers modulate neuronal autophagy through the primary cilium
Olatz Pampliega, Federico Nicolás Soria, … Erwan Bézard·bioRxiv·Jun 2, 2021