Aberrant Activation of Focal Adhesion Proteins Mediates Fibrillar Amyloid β-Induced Neuronal Dystrophy
Open accessAbstract
Neuronal dystrophy is a pathological hallmark of Alzheimer's disease (AD) that is not observed in other neurodegenerative disorders that lack amyloid deposition. Treatment of cortical neurons with fibrillar amyloid beta (Abeta) peptides induces progressive neuritic dystrophy accompanied by a marked loss of synaptophysin immunoreactivity (Grace et al., 2002). Here, we report that fibrillar Abeta-induced neuronal dystrophy is mediated by the activation of focal adhesion (FA) proteins and the formation of aberrant FA structures adjacent to Abeta deposits. In the AD brain, activated FA proteins are observed associated with the majority of senile plaques. Clustered integrin receptors and activated paxillin (phosphorylated at Tyr-31) and focal adhesion kinase (phosphorylated at Tyr-297) are mainly detected in dystrophic neurites surrounding Abeta plaque cores, where they colocalize with hyperphosphorylated tau. Deletion experiments demonstrated that the presence of the LIM domains in the paxillin C terminus and the recruitment of the protein-Tyr phosphatase (PTP)-PEST to the FA complex are required for Abeta-induced neuronal dystrophy. Therefore, both paxillin and PTP-PEST appear to be critical elements in the generation of the dystrophic response. Paxillin is a scaffolding protein to which other FA proteins bind, leading to the formation of the FA contact and initiation of signaling cascades. PTP-PEST plays a key role in the dynamic regulation of focal adhesion contacts in response to extracellular cues. Thus, in the AD brain, fibrillar Abeta may induce neuronal dystrophy by triggering a maladaptive plastic response mediated by FA protein activation and tau hyperphosphorylation.
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The integrin-cofilin pathway is critical in synaptic dysfunction in AD.
“Together, these results implicate the integrin–cofilin pathway to be critical in synaptic dysfunction in AD [36, 147].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [36]
The Discussion (page not provided) links integrin-based focal adhesion signaling to amyloid-β-induced neuronal dystrophy and notes that dystrophy is associated with synaptic loss in AD. It does not identify cofilin as part of the pathway or establish that an integrin–cofilin pathway is critical to synaptic dysfunction. (LLM, conf=0.87)
Experimental — accuracy not yet measuredDynamic FAK signaling is commonly seen surrounding Aβ plaques in human AD patients.
“For instance, dynamic FAK signaling is commonly seen sur rounding Aβ plaques in human AD patients (Grace and Busciglio, 2003; Saleh et al., 2022)”
From Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis (2026) · cites this paper as Grace and Busciglio, 2003
Multiple canonical focal adhesion signaling molecules are actively engaged in the AD brain.
“Interestingly, previous work has uncovered that multiple canonical focal ad hesion signaling molecules are actively engaged in the AD brain.”
From Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis (2026) · cites this paper as Grace and Busciglio, 2003
Focal adhesion signaling has recently been linked to AD through both genetic risk factors and Aβ-associated signaling events.
“Interestingly, focal adhesion signaling has re cently been linked to AD through both genetic risk factors and Aβ-associated signaling events (Grace and Busciglio, 2003; Lambert et al., 2013; Lin et al., 2017; Manocha et al., 2015; Ramos de Matos et al., 2018; Saleh et al., 2022; Schwartzentruber et al., 2021; Wang et al., 2015b)”
From Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis (2026) · cites this paper as Grace and Busciglio, 2003
Aberrant activation of the FA pathway may mediate Aβ fibril-induced neuronal dystrophy.
“In addition, aberrant activation of the FA pathway may mediate Aβ fibril-induced neuronal dystrophy [36].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [36]
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- Authors
- Grace, E. A., & Busciglio, J.
- Affiliations
- UConn Health (US)
- ORCID
- Busciglio, Jorge
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2003-01-15
- Volume
- 23
- Issue
- 2
- Pages
- 493-502
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6741895
- OpenAlex
- W1562586507
- Cited by
- 113
- References
- 81
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 4 · 2019: 2 · 2018: 2 · 2017: 5 · 2016: 5 · 2015: 4 · 2014: 3 · 2013: 7 · 2012: 4
- FWCI
- 6.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- University of Connecticut
- National Institutes of Health
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD-38466, R01HD038466)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, fibrillar amyloid-beta, neuronal dystrophy, focal adhesion proteins, paxillin, PTP-PEST, focal adhesion kinase, integrins, tau hyperphosphorylation, synaptophysin, LIM domain, amyloid plaques, synaptic dysfunction, maladaptive plasticity
- MeSH terms
- Alzheimer Disease, Animals, Cells, Cultured, Cytoskeletal Proteins, Cytoskeleton, Luminescent Proteins, Neurons, Phosphoproteins, Phosphorylation, Recombinant Fusion Proteins, Transfection, Signal Transduction, Cell Adhesion Molecules, Integrins, Amyloid beta-Peptides, Neurites, tau Proteins, Cell Death, Protein Tyrosine Phosphatases, Protein Structure, Tertiary, Protein Transport, Focal Adhesions, Macromolecular Substances, Green Fluorescent Proteins, Rats, Paxillin, Protein Tyrosine Phosphatase, Non-Receptor Type 12
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