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Cited by 181Alzheimer's disease research and treatmentsCellular Mechanics and InteractionsNeuroinflammation and Neurodegeneration Mechanisms

Actin dynamics and cofilin‐actin rods in alzheimer disease

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Bamburg, James R., Bernstein, Barbara W.·2016·Cytoskeleton
DOI 10.1002/cm.21282PMC PMC5345344
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Abstract

Cytoskeletal abnormalities and synaptic loss, typical of both familial and sporadic Alzheimer disease (AD), are induced by diverse stresses such as neuroinflammation, oxidative stress, and energetic stress, each of which may be initiated or enhanced by proinflammatory cytokines or amyloid‐β (Aβ) peptides. Extracellular Aβ‐containing plaques and intracellular phospho‐tau‐containing neurofibrillary tangles are postmortem pathologies required to confirm AD and have been the focus of most studies. However, AD brain, but not normal brain, also have increased levels of cytoplasmic rod‐shaped bundles of filaments composed of ADF/cofilin‐actin in a 1:1 complex (rods). Cofilin, the major ADF/cofilin isoform in mammalian neurons, severs actin filaments at low cofilin/actin ratios and stabilizes filaments at high cofilin/actin ratios. It binds cooperatively to ADP‐actin subunits in F‐actin. Cofilin is activated by dephosphorylation and may be oxidized in stressed neurons to form disulfide‐linked dimers, required for bundling cofilin‐actin filaments into stable rods. Rods form within neurites causing synaptic dysfunction by sequestering cofilin, disrupting normal actin dynamics, blocking transport, and exacerbating mitochondrial membrane potential loss. Aβ and proinflammatory cytokines induce rods through a cellular prion protein‐dependent activation of NADPH oxidase and production of reactive oxygen species. Here we review recent advances in our understanding of cofilin biochemistry, rod formation, and the development of cognitive deficits. We will then discuss rod formation as a molecular pathway for synapse loss that may be common between all three prominent current AD hypotheses, thus making rods an attractive therapeutic target. © 2016 Wiley Periodicals, Inc.

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  • Formation of cofilin-actin rods in distal dendrites is detrimental for synapses.

    “Formation of cofilin–actin rods in distal dendrites is detrimental for synapses [7, 19] and cofilin–actin rod pathology has been observed in the brains of post-mortem AD patients [101] and in animal models of AD [7].”

    From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [7]

    The Signaling Pathways Mediating Neuronal Rod Formation section reports fewer spines and synaptic events in neurites containing rods, supporting a localized detrimental effect on synapses. The passages identify the affected structures as neurites, not specifically distal dendrites; the Conclusions and Perspectives section also notes that rods may transiently protect stressed neurons. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • Cofilin-actin rod pathology has been observed in the brains of post-mortem AD patients and in animal models of AD.

    “Formation of cofilin–actin rods in distal dendrites is detrimental for synapses [7, 19] and cofilin–actin rod pathology has been observed in the brains of post-mortem AD patients [101] and in animal models of AD [7].”

    From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [7]

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Authors
Bamburg, J. R., & Bernstein, B. W.
Affiliations
Colorado State University (US)
Corresponding author
Bamburg, James R.
ORCID
Bamburg, James R.
Venue
Cytoskeleton
Publisher
Wiley
Published
2016-03
Volume
73
Issue
9
Pages
477-497
ISSN
  • 1949-3584 (ISSN-L)
  • 1949-3592
DOI
10.1002/cm.21282
PMC
PMC5345344
OpenAlex
W2272690659
Cited by
181
References
19
Citations by year
2026: 25 · 2025: 18 · 2024: 15 · 2023: 14 · 2022: 11 · 2021: 25 · 2020: 20 · 2019: 17 · 2018: 16 · 2017: 13 · 2016: 6
FWCI
1.96
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations
  • Cytoskeleton (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institutes of Health (AG044812, AG049668)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
Alzheimer's disease, cofilin, actin dynamics, actin filament severing, amyloid-beta, inflammatory cytokines, NADPH oxidase, reactive oxygen species, cellular prion protein, mitochondrial membrane potential, synaptic loss, neuroinflammation, oxidative stress, cognitive impairment, therapeutic target
MeSH terms
Actins, Adenosine Diphosphate, Alzheimer Disease, Animals, Biological Transport, Active, Humans, Actin Cytoskeleton, Amyloid beta-Peptides, Actin Depolymerizing Factors, Protein Multimerization

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