Structural Basis of Tau Interaction With BIN1 and Regulation by Tau Phosphorylation
Open accessAbstract
Bridging integrator-1 (BIN1) gene is associated with an increased risk to develop Alzheimer’s disease, a tauopathy characterized by intra-neuronal accumulation of phosphorylated Tau protein as paired helical filaments. Direct interaction of BIN1 and Tau proteins was demonstrated to be mediated through BIN1 SH3 C-terminal domain and Tau(210-240) peptide within Tau proline-rich domain. We previously showed that BIN1 SH3 interaction with Tau is decreased by phosphorylation within Tau proline-rich domain, of at least T231. In addition, the BIN1/Tau interaction is characterized by a dynamic equilibrium between a closed and open conformations of BIN1 isoform 1, involving an intramolecular interaction with its C-terminal BIN1 SH3 domain. However, the role of the BIN1/Tau interaction, and its potential dysregulation in Alzheimer’s disease, is not yet fully understood. Here we showed that within Tau(210-240) peptide, among the two proline-rich motifs potentially recognized by SH3 domains, only motif P216TPPTR221 is bound by BIN1 SH3. A structural model of the complex between BIN1 SH3 and Tau peptide(213-229), based on nuclear magnetic resonance spectroscopy data, revealed the molecular detail of the interaction. P216 and P219 within the proline-rich motif were in direct contact with the aromatic F588 and W562 of the BIN1 SH3 domain. The contact surface is extended through electrostatic interactions between the positively charged R221 and K224 residues of Tau peptide and those negatively charged of BIN1 SH3, corresponding to E556 and E557. We next investigated the impact of multiple Tau phosphorylations within Tau(210-240) on its interaction with BIN1 isoform 1. Tau(210-240) phosphorylated at four different sites (T212, T217, T231 and S235), contrary to unphosphorylated Tau, was unable to compete with the intramolecular interaction of BIN1 SH3 domain with its CLAP domain. In accordance, the affinity of BIN1 SH3 for phosphorylated Tau(210-240) peptide was reduced, with a 5-fold increase in the dissociation constant, from a Kd of 44µM to 256µM. This study highlights the complexity of the regulation of BIN1 isoform 1 with Tau. As abnormal phosphorylation of Tau is linked to the pathology development, this regulation by phosphorylation might have important functional consequences.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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 [85]
The Introduction reports direct BIN1–Tau interaction and a BIN1/Tau complex in primary neurons. The Results section on BIN1 isoform 1 shows that phosphorylation of Tau weakens binding. Our copy does not show that neuronal binding depends on BIN1 expression level or BIN1 phosphorylation status; its expression discussion concerns Tau pathology or propagation, not binding. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
<i>Coot</i> : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works
Meta-Analysis of 74,046 Individuals Identifies 11 New Susceptibility Loci for Alzheimer’s Disease
(EADI), E. A. D. I., Lambert, J.-C., (GERAD), G. A. E. R. I. A. D., Alzheimer's Disease Genetic Consortium (ADGC), (CHARGE), C. F. H. A. A. R. I. G. E., Ibrahim-Verbaas, C. A., Harold, D., Naj, A. C., Sims, R., Bellenguez, C., et al. (2013) · Nature Genetics · doi:10.1038/ng.2802 · Cited by 4,336 · see citing works
Self-citationGradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
Piotto, M., Saudek, V., & Sklenář, V. (1992) · Journal of Biomolecular NMR · doi:10.1007/bf02192855 · Cited by 3,720 · see citing works
Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326 · see citing works
The CCPN data model for NMR spectroscopy: Development of a software pipeline
Vranken, W., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinás, M., Ulrich, E. L., Markley, J. L., Ionides, J., & Laue, E. D. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20449 · Cited by 3,222 · see citing works
HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information
Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187 · see citing works
Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172 · see citing works
The HADDOCK2.2 Web Server: User-Friendly Integrative Modeling of Biomolecular Complexes
van Zundert, G. C. P., Rodrigues, J. P. G. L. M., Trellet, M., Schmitz, C., Kastritis, P. L., Karaca, E., Melquiond, A. S. J., van Dijk, M., de Vries, S. J., & Bonvin, A. M. J. J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.09.014 · Cited by 2,785 · see citing works
Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease
the European Alzheimer's Disease Initiative Investigators, Lambert, J.-C., Heath, S., Even, G., Campion, D., Sleegers, K., Hiltunen, M., Combarros, O., Zelenika, D., Bullido, M. J., et al. (2009) · Nature Genetics · doi:10.1038/ng.439 · Cited by 2,234 · see citing works
Self-citationGenome-wide Analysis of Genetic Loci Associated With Alzheimer Disease
Seshadri, S. (2010) · JAMA · doi:10.1001/jama.2010.574 · Cited by 1,219 · see citing works
Feng, S., Chen, J., Yu, H., Simon, J. A., & Schreiber, S. L. (1994) · Science · doi:10.1126/science.7526465 · Cited by 799 · see citing works
APOE and Alzheimer disease: a major gene with semi-dominant inheritance
Genin, E., Hannequin, D., Wallon, D., Sleegers, K., Hiltunen, M., Combarros, O., Bullido, M. J., Engelborghs, S., De Deyn, P., Berr, C., et al. (2011) · Molecular Psychiatry · doi:10.1038/mp.2011.52 · Cited by 714 · see citing works
Self-citationFunctional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
Takei, K., Slepnev, V. I., Haucke, V., & Camilli, P. V. D. (1999) · Nature Cell Biology · doi:10.1038/9004 · Cited by 657 · see citing works
The BAR Domain Superfamily: Membrane-Molding Macromolecules
Frost, A. S., Unger, V. M., & Camilli, P. V. D. (2009) · Cell · doi:10.1016/j.cell.2009.04.010 · Cited by 571 · see citing works
Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.
Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565 · see citing works
Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
Lim, W. A., Richards, F. M., & Fox, R. O. (1994) · Nature · doi:10.1038/372375a0 · Cited by 517 · see citing works
Abnormal Alzheimer‐like phosphorylation of tau‐protein by cyclin‐dependent kinases cdk2 and cdk5
Baumann, K., Mandelkow, E., Biernat, J., Piwnica-Worms, H. M., & Mandelkow, E. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80849-p · Cited by 479 · see citing works
David, C., McPherson, P. S., Mundigl, O., & Camilli, P. V. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.331 · Cited by 409 · see citing works
Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology
GERAD consortium, Chapuis, J., Hansmannel, F., Gistelinck, M., Mounier, A., Van Cauwenberghe, C., Kolen, K. V., Geller, F., Sottejeau, Y., Harold, D., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.1 · Cited by 407 · see citing works
Self-citationIshiguro, K., Shiratsuchi, A., Sato, S., Omori, A., Arioka, M., Kobayashi, S., Uchida, T., & Imahori, K. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81066-9 · Cited by 402 · see citing works
Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375 · see citing works
Zheng‐Fischhöfer, Q., Biernat, J., Mandelkow, E., Illenberger, S., Godemann, R., & Mandelkow�, E. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2520542.x · Cited by 322 · see citing works
Physiological and pathological phosphorylation of tau by Cdk5
Kimura, T., Ishiguro, K., & Hisanaga, S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00065 · Cited by 297 · see citing works
Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites
Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266 · see citing works
Loss of Bin1 Promotes the Propagation of Tau Pathology
Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works
Amphiphysin 2 (BIN1) in physiology and diseases
Prokic, I., Cowling, B. S., & Laporte, J. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1138-1 · Cited by 188 · see citing works
Bin1 and CD2AP polarise the endocytic generation of beta‐amyloid
Ubelmann, F., Burrinha, T., Salavessa, L., Gomes, R., Ferreira, C., Moreno, N., & Guimas Almeida, C. (2017) · The EMBO Reports · doi:10.15252/embr.201642738 · Cited by 165 · see citing works
Garrett, D. S., Seok, Y., Liao, D., Peterkofsky, A., Gronenborn, A. M., & Clore, G. M. (1997) · Biochemistry · doi:10.1021/bi962924y · Cited by 153 · see citing works
Holler, C. J., Davis, P. R., Beckett, T. L., Platt, T. L., Webb, R. L., Head, E., & Murphy, M. P. (2014) · Journal of Alzheimer’s Disease · doi:10.3233/jad-132450 · Cited by 145 · see citing works
Structural Impact of Tau Phosphorylation at Threonine 231
Schwalbe, M., Kadavath, H., Biernat, J., Ozenne, V., Blackledge, M. J., Mandelkow�, E., & Zweckstetter, M. (2015) · Structure · doi:10.1016/j.str.2015.06.002 · Cited by 130 · see citing works
Pineda‐Lucena, A., Ho, C. S. W., Mao, D. Y. L., Sheng, Y., Laister, R. C., Muhandiram, R., Lü, Y., Seet, B. T., Katz, S., Szyperski, T., et al. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.046 · Cited by 124 · see citing works
Dourlen, P., Fernandez-Gomez, F. J., Dupont, C., Grenier-Boley, B., Bellenguez, C., Obriot, H., Caillierez, R., Sottejeau, Y., Chapuis, J., Bretteville, A., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.59 · Cited by 118 · see citing works
Self-citationLuna‐Vargas, M. P. A., Christodoulou, E., Alfieri, A., van Dijk, W. J., Stadnik, M., Hibbert, R. G., Sahtoe, D. D., Clerici, M., Marco, V. D., Littler, D. R., et al. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.03.017 · Cited by 110 · see citing works
Luna‐Muñoz, J., García‐Sierra, F., Falcón, V., Menéndez, I., Chávez-Macías, L., & Mena, R. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-8104 · Cited by 109 · see citing works
Sottejeau, Y., Bretteville, A., Cantrelle, F.-X., Malmanche, N., Demiaute, F., Mendes, T., Delay, C., Alves Dos Alves, H., Flaig, A., Davies, P., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0237-8 · Cited by 98 · cited 9× · see citing works
“We have previously reported that the BIN1 SH3 binds directly to Tau PRD (Sottejeau et al., 2015).”
BackgroundResultInfluentialSelf-citationSibille, N., Huvent, I., Fauquant, C., Verdegem, D., Amniai, L., Leroy, A., Wieruszeski, J., Lippens, G. M., & Landrieu, I. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23210 · Cited by 92 · see citing works
Self-citationWang, A., Grzesiek, S., Tschudin, R. G., Lodi, P. J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00182281 · Cited by 89 · see citing works
Leroy, A., Landrieu, I., Huvent, I., Legrand, D., Codeville, B., Wieruszeski, J.-M., & Lippens, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149419 · Cited by 86 · see citing works
Self-citationThe Peptidyl Prolyl cis/trans-Isomerase Pin1 Recognizes the Phospho-Thr212-Pro213 Site on Tau
Smet‐Nocca, C., Sambo, A., Wieruszeski, J., Leroy, A., Landrieu, I., Buée, L., & Lippens, G. M. (2004) · Biochemistry · doi:10.1021/bi035479x · Cited by 84 · see citing works
Self-citationKanelis, V., Donaldson, L. W., Muhandiram, D. R., Rotin, D., Forman-Kay, J. D., & Kay, L. E. (2000) · Journal of Biomolecular NMR · doi:10.1023/a:1008355012528 · Cited by 79 · see citing works
Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase
Qi, H., Prabakaran, S., Cantrelle, F., Chambraud, B., Gunawardena, J., Lippens, G. M., & Landrieu, I. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700914 · Cited by 67 · see citing works
Self-citationSmet‐Nocca, C., Wieruszeski, J., Buée, L., Landrieu, I., & Lippens, G. M. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.06.048 · Cited by 61 · see citing works
Self-citationMalki, I., Cantrelle, F., Sottejeau, Y., Lippens, G., Lambert, J., & Landrieu, I. (2017) · The FEBS Journal · doi:10.1111/febs.14185 · Cited by 54 · see citing works
Self-citationBin1 directly remodels actin dynamics through its BAR domain
Dräger, N. M., Nachman, E., Winterhoff, M., Brühmann, S., Shah, P., Katsinelos, T., Boulant, S., Teleman, A. A., Faix, J., & Jahn, T. R. (2017) · The EMBO Reports · doi:10.15252/embr.201744137 · Cited by 51 · see citing works
Proline Conformation in a Functional Tau Fragment
Ahuja, P., Cantrelle, F., Huvent, I., Hanoulle, X., Lopez, J. M., Smet‐Nocca, C., Wieruszeski, J., Landrieu, I., & Lippens, G. M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.11.023 · Cited by 41 · see citing works
Self-citationTossavainen, H., Aitio, O., Hellman, M., Saksela, K., & Permi, P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.732412 · Cited by 41 · see citing works
NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease
Landrieu, I., Leroy, A., Smet‐Nocca, C., Huvent, I., Amniai, L., Hamdane, M., Sibille, N., Buée, L., Wieruszeski, J., & Lippens, G. M. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381006 · Cited by 32 · see citing works
Self-citationTowards understanding the phosphorylation code of tau
Lippens, G. M., Amniai, L., Wieruszeski, J., Sillen, A., Leroy, A., & Landrieu, I. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120050 · Cited by 21 · see citing works
Self-citationWelburn, J. P. I., & Endicott, J. (2004) · Humana Press eBooks · doi:10.1385/1-59259-857-9:219 · Cited by 14 · see citing works
Flagged first, then by citations
2 of the 51 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Amyloid-β-independent regulators of tau pathology in Alzheimer disease
van der Kant, R., Goldstein, L. S. B., & Ossenkoppele, R. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-019-0240-3 · Cited by 580 · see citing works
Barthélemy, N. R., Bateman, R. J., Hirtz, C., Marin, P., Becher, F., Sato, C., Gabelle, A., & Lehmann, S. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00596-4 · Cited by 229 · see citing works
Dourlen, P., Kilinc, D., Malmanche, N., Chapuis, J., & Lambert, J.-C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02004-0 · Cited by 168 · see citing works
Self-citationImmunotherapies for Neurodegenerative Diseases
Mortada, I., Farah, R., Nabha, S. M., Ojcius, D. M., Fares, Y., Almawi, W. Y., & Sadier, N. S. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.654739 · Cited by 112 · see citing works
3‐O‐Sulfation of Heparan Sulfate Enhances Tau Interaction and Cellular Uptake
Zhao, J., Zhu, Y., Song, X., Xiao, Y., Su, G., Liu, X., Wang, Z., Xu, Y., Liu, J., Eliezer, D., et al. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201913029 · Cited by 111 · see citing works
The BIN1 rs744373 SNP is associated with increased tau-PET levels and impaired memory
Franzmeier, N., Rubinski, A., Neitzel, J., Ewers, M., (ADNI), T. A. D. N. I., Weiner, M. W., Aisen, P., Petersen, R., Jack, C. R., Jagust, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09564-5 · Cited by 109 · see citing works
Cardiac microtubules in health and heart disease
Caporizzo, M. A., Chen, C. Y., & Prosser, B. L. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219868960 · Cited by 109 · see citing works
Gomes, L. A., Uytterhoeven, V., Lopez-Sanmartin, D., Tomé, S. O., Tousseyn, T., Vandenberghe, R. R., Vandenbulcke, M., Arnim, C. A. F. V., Verstreken, P., & Thal, D. R. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02251-6 · Cited by 74 · see citing works
Sartori, M., Mendes, T., Desai, S., Lasorsa, A., Herledan, A., Malmanche, N., Mäkinen, P., Marttinen, M., Malki, I., Chapuis, J., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02017-9 · Cited by 72 · see citing works
Self-citationAlzheimer’s disease risk gene BIN1 induces Tau-dependent network hyperexcitability
Voskobiynyk, Y., Roth, J. R., Cochran, J. N., Rush, T., Carullo, N. V. N., Mesina, J. S., Waqas, M., Vollmer, R. M., Day, J. J., McMahon, L. L., et al. (2020) · eLife · doi:10.7554/elife.57354 · Cited by 66 · see citing works
A Systematic Compilation of Human SH3 Domains: A Versatile Superfamily in Cellular Signaling
Mehrabipour, M., Jasemi, N. S. K., Dvorský, R., & Ahmadian, M. R. (2023) · Cells · doi:10.3390/cells12162054 · Cited by 39 · see citing works
Carroll, T., Guha, S. K., Nehrke, K. W., & Johnson, G. V. W. (2021) · Biology · doi:10.3390/biology10101047 · Cited by 35 · see citing works
Glennon, E. B. C., Lau, D. H. W., Gabriele, R. M. C., Taylor, M. F., Troakes, C., Opie-Martin, S., Elliott, C., Killick, R., Hanger, D. P., Perez‐Nievas, B. G., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa011 · Cited by 33 · see citing works
The ArfGAP ASAP1 Controls Actin Stress Fiber Organization via Its N-BAR Domain
Gasilina, A., Vitali, T., Luo, R., Jian, X., & Randazzo, P. A. (2019) · iScience · doi:10.1016/j.isci.2019.11.015 · Cited by 32 · see citing works
Synaptic sabotage: How Tau and α-Synuclein undermine synaptic health
Uytterhoeven, V., Verstreken, P., & Nachman, E. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202409104 · Cited by 28 · see citing works
Hu, H., Tan, L., Bi, Y., Xu, W., Tan, L., Shen, X., Hou, X., Ma, Y., Dong, Q., & Yu, J. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01218-9 · Cited by 25 · see citing works
BIN1 and Alzheimer’s disease: the tau connection
Dourlen, P., Kilinc, D., Landrieu, I., Chapuis, J., & Lambert, J. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.03.004 · Cited by 23 · see citing works
Self-citationCell type-specific functions of Alzheimer's disease endocytic risk genes
Maninger, J., Nowak, K., Goberdhan, S., O’Donoghue, R., & Connor‐Robson, N. (2024) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2022.0378 · Cited by 21 · see citing works
Dai, D., Tropea, T. F., Robinson, J. L., Suh, E. R., Hurtig, H. I., Weintraub, D. A., Deerlin, V. M. V., Lee, E. B., Trojanowski, J. Q., & Chen‐Plotkin, A. S. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02199-7 · Cited by 14 · see citing works
A Connected Network of Interacting Proteins Is Involved in Human-Tau Toxicity in Drosophila
Feuillette, S., Charbonnier, C., Frébourg, T., Campion, D., & Lecourtois, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00068 · Cited by 14 · see citing works
Roth, J. R., Rush, T., Thompson, S. J., Aldaher, A. R., Dunn, T. B., Mesina, J. S., Cochran, J. N., Boyle, N. R., Dean, H. B., Yang, Z. W., et al. (2023) · Neurotherapeutics · doi:10.1016/j.neurot.2023.10.001 · Cited by 12 · see citing works
Association of the top 20 Alzheimer's disease risk genes with [18F]flortaucipir PET
Stage, E., Risacher, S. L., Lane, K. A., Gao, S., Nho, K. T., Saykin, A. J., Apostolova, L. G., & Initiative, A. D. N. (2022) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.12308 · Cited by 11 · see citing works
Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy
Zámbó, B., Edelweiss, E. F., Morlet, B., Négroni, L., Pajkos, M., Dosztányi, Z., Østergaard, S., Travé, G., Laporte, J., & Gógl, G. (2024) · eLife · doi:10.7554/elife.95397 · Cited by 9 · see citing works
Effect of BIN1 on cardiac dysfunction and malignant arrhythmias
Jiang, X., Zhu, Y., Liu, H., Chen, S., & Zhang, D. (2019) · Acta Physiologica · doi:10.1111/apha.13429 · Cited by 8 · see citing works
Wang, X., Chang, C., Wang, D., & Hong, S. (2019) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2019.05.004 · Cited by 8 · see citing works
Lasorsa, A., Bera, K., Malki, I., Dupré, E., Cantrelle, F., Merzougui, H., Sinnaeve, D., Hanoulle, X., Hritz, J., & Landrieu, I. (2023) · Biochemistry · doi:10.1021/acs.biochem.2c00717 · Cited by 7 · see citing works
Self-citationCehlár, O., Bagarova, O., Hornakova, L., & Škrabana, R. (2021) · General Physiology and Biophysics · doi:10.4149/gpb_2021031 · Cited by 7 · see citing works
Hajjar, L. E., Bridot, C., Nguyen, M., Cantrelle, F., Landrieu, I., & Smet‐Nocca, C. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_15 · Cited by 6 · see citing works
Self-citationLatina, V., Atlante, A., Malerba, F., Regina, F. L., Balzamino, B. O., Micera, A., Pignataro, A., Stigliano, E., Cavallaro, S., Calissano, P., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119683 · Cited by 5 · see citing works
Tira, R., Leo, G., Prandini, L., Barracchia, C. G., D’Onofrio, M., Mollica, L., Capaldi, S., Assfalg, M., & Munari, F. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202504292 · Cited by 4 · see citing works
Proteomic Characterization of the Alzheimer’s Disease Risk Factor BIN1 Interactome
McMillan, J. D., Wang, S., Wohlfahrt, J., Guergues, J., Stevens, S. M., & Thinakaran, G. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101055 · Cited by 4 · see citing works
Coordination of autophagosome closure and release by the Alzheimer’s disease-associated protein BIN1
Palmer, J. E., Puri, C., O’Rourke, R., Son, S. M., Sang, C., Huang, Y. A., & Rubinsztein, D. C. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116266 · Cited by 4 · see citing works
A comprehensive review on novel opportunities for Alzheimer therapy by targeting BIN1
Saha, T., & Karati, D. (2025) · Egyptian Journal of Medical Human Genetics · doi:10.1186/s43042-025-00759-8 · Cited by 3 · see citing works
Conformational dependence of chemical shifts in the proline rich region of TAU protein
Stöckelmaier, J., & Oostenbrink, C. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp02484b · Cited by 3 · see citing works
3‐O‐Sulfation of Heparan Sulfate Enhances Tau Interaction and Cellular Uptake
Zhao, J., Zhu, Y., Song, X., Xiao, Y., Su, G., Liu, X., Wang, Z., Xu, Y., Liu, J., Eliezer, D., et al. (2019) · Angewandte Chemie · doi:10.1002/ange.201913029 · Cited by 3 · see citing works
Wei, Y., Ye, X., Li, H., Zhang, X., Wang, Y., Li, Y., Fang, R., Xiang, J., & Wu, S. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01435-y · Cited by 2 · see citing works
Duckhorn, J. C., Kim, D. K., & Huang, Y. A. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00243 · Cited by 2 · see citing works
Alternative splicing in Alzheimer’s disease: Driver, modifier, or consequence of neurodegeneration
Aranda-Abreu, G. E., Rojas-Durán, F., Hernández‐Aguilar, M. E., Herrera‐Covarrubias, D., Tlapa-Monge, L. R., & Mestizo-Gutiérrez, S. L. (2026) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2026.112211 · Cited by 1 · see citing works
Tira, R., Leo, G., Prandini, L., Barracchia, C. G., D’Onofrio, M., Mollica, L., Capaldi, S., Assfalg, M., & Munari, F. (2025) · Angewandte Chemie · doi:10.1002/ange.202504292 · Cited by 1 · see citing works
Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathyPreprint
Zámbó, B., Edelweiss, E. F., Morlet, B., Négroni, L., Pajkos, M., Dosztányi, Z., Østergaard, S., Travé, G., Laporte, J., & Gógl, G. (2024) · eLife · doi:10.7554/elife.95397.1 · Cited by 1 · see citing works
Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathyPreprint
Zámbó, B., Edelweiss, E. F., Morlet, B., Négroni, L., Pajkos, M., Dosztányi, Z., Østergaard, S., Travé, G., Laporte, J., & Gógl, G. (2024) · eLife · doi:10.7554/elife.95397.2 · Cited by 1 · see citing works
Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathyPreprint
Zámbó, B., Edelweiss, E. F., Morlet, B., Négroni, L., Pajkos, M., Dosztányi, Z., Østergaard, S., Travé, G., Laporte, J., & Gógl, G. (2024) · eLife · doi:10.7554/elife.95397.3 · Cited by 1 · see citing works
実験核物理領域,理論核物理領域「LHCとRHICの競演が拓く新世代のクォーク・グルーオン・プラズマ物性」(2012年秋季大会シンポジウムの報告,学会報告)
佐藤, 進. (2013) · 日本物理學會誌
eLife Assessment: Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy
Andreotti, A. H. (2024) · eLife · doi:10.7554/elife.95397.1.sa2
Author response: Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy
Zámbó, B., Edelweiss, E. F., Morlet, B., Négroni, L., Pajkos, M., Dosztányi, Z., Østergaard, S., Travé, G., Laporte, J., & Gógl, G. (2024) · eLife · doi:10.7554/elife.95397.2.sa3
Author response: Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy
Zámbó, B., Edelweiss, E. F., Morlet, B., Négroni, L., Pajkos, M., Dosztányi, Z., Østergaard, S., Travé, G., Laporte, J., & Gógl, G. (2024) · eLife · doi:10.7554/elife.95397.3.sa3
Chan, D., Spires‐Jones, T. L., Provenzano, F. A., Glennon, E. B. C., & Duff, K. (2025) · Oxford University Press eBooks · doi:10.1093/med/9780190065324.003.0020
Mitochondrial Dysfunction in Alzheimer’s Disease: A Comprehensive Review of Synaptopathy Mechanisms
Yoon, S. (2025) · IntechOpen eBooks · doi:10.5772/intechopen.1009341
Blazier, D. M., Lewandowski, E. M., Ram, N., Zhang, X., Wang, S., Patel, O., Collier, L. A., Defilippi, P., Chen, Y., & Thinakaran, G. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110665
Gaffour, A., Bakker, M. J., Bera, K., & Přecechtělová, J. P. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.09.037
Barthélemy, N. R., Bateman, R. J., Hirtz, C., Marin, P., Bécher, F., Sato, C., Gabelle, A., & Lehmann, S. (2020) · Figshare · doi:10.6084/m9.figshare.11998815
Barthélemy, N. R., Bateman, R. J., Hirtz, C., Marin, P., Bécher, F., Sato, C., Gabelle, A., & Lehmann, S. (2020) · Figshare · doi:10.6084/m9.figshare.11998812
Evaluating the Impact of Phosphorylation on the Dynamics of the Tau Protein Proline-Rich Region
Stöckelmaier, J., Polato, G., Hritz, J., & Oostenbrink, C. (2026) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c02011
Wei, X., Munechika, K., Sun, Y., Wan, Y., Xia, T., Hou, Y., Song, W., Yugandhar, K., Wang, Y., Lee, S.-I., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.14.711835
BIN1 (amphiphysin 2) in the pathogenesis of cognitive impairment
Shamakina, I. Y., Kokhan, V. S., Venkova, V. A., Баронец, В. Ю., Popov, S. S., & Anokhin, P. K. (2026) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro202612603145
BIN1 (Amphiphysin 2) in the Pathogenesis of Cognitive Impairment
Shamakina, I. Y., Kokhan, V. S., Venkova, V. A., Баронец, В. Ю., Popov, S. S., & Anokhin, P. K. (2026) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-026-02059-z
Valentim, C., Denecke, J., Frerich, S., Betthauser, T. J., Li, Y., Ahmadi, R., Franzmeier, N., (ADNI), A. D. N. I., Malik, R., & Ewers, M. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71939
- Authors
- Lasorsa, A., Malki, I., Cantrelle, F.-X., Merzougui, H., Boll, E., Lambert, J.-C., & Landrieu, I.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Inserm (FR)
- Corresponding author
- Landrieu, Isabelle
- ORCID
- Venue
- Frontiers in Molecular Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2018-11-14
- Volume
- 11
- Pages
- 421-421
- ISSN
- 1662-5099 (ISSN-L)
- PMC
- PMC6246682
- OpenAlex
- W2900451439
- Cited by
- 58
- References
- 51
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 12 · 2023: 4 · 2022: 1 · 2021: 5 · 2020: 7 · 2019: 10 · 2013: 1
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Frontiers in Molecular Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
- Funders
- Agence Nationale de la Recherche (ANR-15-CE16-0002, 11-LABX-0009)
- 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
- tau protein, SH3 domain, proline-rich region, protein-protein interaction, tau phosphorylation, Alzheimer's disease, intramolecular interactions, binding affinity, structural model, tauopathy, paired helical filaments
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
