A novel role for the late-onset Alzheimer’s disease (LOAD)-associated protein Bin1 in regulating postsynaptic trafficking and glutamatergic signaling
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Postsynaptic trafficking plays a key role in regulating synapse structure and function. While spiny excitatory synapses can be stable throughout adult life, their morphology and function is impaired in Alzheimer's disease (AD). However, little is known about how AD risk genes impact synaptic function. Here we used structured superresolution illumination microscopy (SIM) to study the late-onset Alzheimer's disease (LOAD) risk factor BIN1, and show that this protein is abundant in postsynaptic compartments, including spines. While postsynaptic Bin1 shows colocalization with clathrin, a major endocytic protein, it also colocalizes with the small GTPases Rab11 and Arf6, components of the exocytic pathway. Bin1 participates in protein complexes with Arf6 and GluA1, and manipulations of Bin1 lead to changes in spine morphology, AMPA receptor surface expression and trafficking, and AMPA receptor-mediated synaptic transmission. Our data provide new insights into the mesoscale architecture of postsynaptic trafficking compartments and their regulation by a major LOAD risk factor.
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Synaptic fragility/sensitivity was proposed as a pathological trigger depending on genetic risk factors, some of which have already been linked to synaptic mechanisms such as BIN1, FERMT2, PTK2B or CD2AP.
“we proposed synaptic fragility/sensitivity as a pathological trigger10, depending on genetic risk factors, some of which have already been linked to synaptic mechanisms, such as BIN1, FERMT2, PTK2B or CD2AP9–12.”
From PLCG2 downregulation impairs synaptic function and increases Alzheimer’s disease hallmarks in neuronal cultures (2026) · cites this paper as [9]
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- Authors
- Schürmann, B., Bermingham, D. P., Kopeikina, K. J., Myczek, K., Yoon, S., Horan, K. E., Kelly, C. J., Martin-de-Saavedra, M. D., Forrest, M. P., Fawcett-Patel, J. M., Smith, K. R., Gao, R., Bach, A., Burette, A. C., Rappoport, J. Z., Weinberg, R. J., Martina, M., & Penzes, P.
- Affiliations
- Northwestern University (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Penzes, Peter
- ORCID
- Venue
- Molecular Psychiatry
- Published
- 2019-04-09
- Volume
- 25
- Issue
- 9
- Pages
- 2000-2016
- ISSN
- 1359-4184 (ISSN-L)
- 1476-5578
- PMC
- PMC6785379
- OpenAlex
- W2940322549
- Cited by
- 72
- References
- 38
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 9 · 2023: 6 · 2022: 18 · 2021: 9 · 2020: 6 · 2019: 2
- FWCI
- 4.18
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Psychiatry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute of Mental Health (MH097216, MH107182)
- U.S. Department of Health & Human Services | NIH | National Institute on Aging (AG063433)
- U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NS039444, NS064091)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- BIN1, late-onset Alzheimer's disease, glutamatergic signaling, AMPA receptor trafficking, synaptic structure, dendritic spines, ARF6, Rab11, clathrin, GluR1, synaptic transmission, super-resolution imaging
- MeSH terms
- Adult, Alzheimer Disease, Humans, Synaptic Transmission, Nuclear Proteins, Synapses, Receptors, AMPA, Tumor Suppressor Proteins, Adaptor Proteins, Signal Transducing
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