Regulation of the interaction between the neuronal BIN 1 isoform 1 and Tau proteins – role of the SH 3 domain
Open accessAbstract
Bridging integrator 1 (bin1) gene is a genetic determinant of Alzheimer's disease (AD) and has been reported to modulate Alzheimer's pathogenesis through pathway(s) involving Tau. The functional impact of Tau/BIN 1 interaction as well as the molecular details of this interaction are still not fully resolved. As a consequence, how BIN 1 through its interaction with Tau affects AD risk is also still not determined. To progress in this understanding, interaction of Tau with two BIN 1 isoforms was investigated using Nuclear Magnetic Resonance spectroscopy. 1 H, 15 N spectra showed that the C‐terminal SH 3 domain of BIN 1 isoform 1 (BIN 1Iso1) is not mobile in solution but locked with the core of the protein. In contrast, the SH 3 domain of BIN 1 isoform 9 (BIN 1Iso9) behaves as an independent mobile domain. This reveals an equilibrium between close and open conformations for the SH 3 domain. Interestingly, a 334–376 peptide from the clathrin and AP‐2‐binding domain (CLAP) domain of BIN 1Iso1, which contains a SH 3‐binding site, is able to compete with BIN 1‐SH 3 intramolecular interaction. For both BIN 1 isoforms, the SH 3 domain can interact with Tau(210–240) sequence. Tau(210–240) peptide can indeed displace the intramolecular interaction of the BIN 1‐SH 3 of BIN 1Iso1 and form a complex with the released domain. The measured Kd were in agreement with a stronger affinity of Tau peptide. Both CLAP and Tau peptides occupied the same surface on the BIN 1‐SH 3 domain, showing that their interaction is mutually exclusive. These results emphasize an additional level of complexity in the regulation of the interaction between BIN 1 and Tau dependent of the BIN 1 isoforms.
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Human BIN1 directly binds Tau, and this interaction in neurons depends on the level of BIN1 expression and the phosphorylation statuses of both BIN1 and Tau.
“human BIN1 directly binds Tau and this interaction in neurons depends on the level of BIN1 expression, as well as the phosphorylation statuses of both BIN1 and Tau [85, 89, 110, 124].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [89]
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Self-citationBIN1 regulates BACE1 intracellular trafficking and amyloid-β production
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Van Acker, Z. P., Bretou, M., & Annaert, W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0323-7 · Cited by 222 · see citing works
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
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Self-citationThe BIN1 rs744373 SNP is associated with increased tau-PET levels and impaired memory
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Self-citationStructural Basis of Tau Interaction With BIN1 and Regulation by Tau Phosphorylation
Lasorsa, A., Malki, I., Cantrelle, F.-X., Merzougui, H., Boll, E., Lambert, J.-C., & Landrieu, I. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00421 · Cited by 58 · see citing works
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- Authors
- Malki, I., Cantrelle, F., Sottejeau, Y., Lippens, G., Lambert, J., & Landrieu, I.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Inserm (FR)
- Corresponding author
- Landrieu, Isabelle
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2017-08-30
- Volume
- 284
- Issue
- 19
- Pages
- 3218-3229
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2740332229
- Cited by
- 54
- References
- 5
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 9 · 2023: 6 · 2022: 11 · 2021: 3 · 2020: 5 · 2019: 9 · 2018: 1
- FWCI
- 2.92
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- FEBS Journal (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- LillOA (Université de Lille (University Of Lille)) (submittedVersion, other-oa)
- Funders
- Centre National de la Recherche Scientifique (FR‐3050, FR‐3688)
- Labex
- Agence Nationale de la Recherche (ANR‐15‐CE16‐0002)
- Alzheimer's Association (BFG‐14‐318355)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- BIN1, tau protein, SH3 domain, Alzheimer's disease, protein-protein interaction, intramolecular interactions, conformational equilibrium, peptide binding affinity, neurofibrillary tangles
- MeSH terms
- Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Binding Sites, Cloning, Molecular, Escherichia coli, Humans, Kinetics, Models, Molecular, Neurons, Nuclear Proteins, Peptides, Protein Binding, Recombinant Proteins, Gene Expression, Sequence Alignment, tau Proteins, Sequence Homology, Amino Acid, Nuclear Magnetic Resonance, Biomolecular, Protein Isoforms, Amino Acid Motifs, Tumor Suppressor Proteins, Adaptor Proteins, Signal Transducing, Protein Interaction Domains and Motifs
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