Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain
Open accessAbstract
INTRODUCTION: The application of high-throughput genomic approaches has revealed 24 novel risk loci for Alzheimer's disease (AD). We recently reported that the bridging integrator 1 (BIN1) risk gene is linked to Tau pathology. RESULTS: We used glutathione S-transferase pull-down assays and nuclear magnetic resonance (NMR) experiments to demonstrate that BIN1 and Tau proteins interact directly and then map the interaction between BIN1's SH3 domain and Tau's proline-rich domain (PRD) . Our NMR data showed that Tau phosphorylation at Thr231 weakens the SH3-PRD interaction. Using primary neurons, we found that BIN1-Tau complexes partly co-localize with the actin cytoskeleton; however, these complexes were not observed with Thr231-phosphorylated Tau species. CONCLUSION: Our results show that (i) BIN1 and Tau bind through an SH3-PRD interaction and (ii) the interaction is downregulated by phosphorylation of Tau Thr231 (and potentially other residues). Our study sheds new light on regulation of the BIN1/Tau interaction and opens up new avenues for exploring its complex's role in the pathogenesis of AD.
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The BIN1 SH3 domain can interact with proteins including c-Abl, N-WASP, actin, myosin, and Tau, suggesting involvement of the cytoskeleton in BIN1 function.
“In addition to proteins involved in endocytosis, the BIN1 SH3 domain can interact with a number of other proteins including the tyrosine kinase c-Abl, the actin nucleation-promoting factor N-WASP, actin, myosin, and Tau, suggesting the involvement of the cytoskeleton in BIN1 function [18–21].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [21]
The Results and Discussion show that BIN1’s SH3 domain interacts with Tau and that BIN1–Tau complexes partly co-localize with the actin cytoskeleton. Our copy does not establish SH3-domain interactions with c-Abl, N-WASP, actin, or myosin; its discussion of BIN1 and actin concerns BIN1 more broadly. (LLM, conf=0.87)
Experimental — accuracy not yet measuredHuman 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 [124]
The Discussion reports direct binding between BIN1’s SH3 domain and Tau and says Tau phosphorylation weakens their interaction both in vitro and in primary neurons. The Introduction and Discussion mention elevated BIN1 expression in AD brains, but do not establish that BIN1 expression level regulates the interaction in neurons. The cited passages also do not show that BIN1’s own phosphorylation status regulates it. Page numbers were not available in our copy. (LLM, conf=0.88)
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“We have previously reported that the BIN1 SH3 binds directly to Tau PRD (Sottejeau et al., 2015).”
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“…A b [26,27]. hBin1 can directly bind tau via its SH3 domain and the Bin1-tau complexes colocalize with the actin cytoskeleton in primary neurons [21,59]. dBin1 modulates tau-induced neurotoxicity in Drosophila [21,28], while in human cell culture studies, downregulation of hBin1 promotes tau…”
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“Additionally, we compared our anti-BIN1 2F11 clone to the anti-BIN1 99D clone recently used by others (11, 34, 41, 42).”
BackgroundMethodTau in Oligodendrocytes Takes Neurons in Sickness and in Health
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“In contrast, the loss of BIN1 significantly correlates with the extent of demyelination in MS lesions [105,106].”
BackgroundInfluentialNuclear Transport Deficits in Tau-Related Neurodegenerative Diseases
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“Monomeric tau is a highly soluble, intrinsically disordered protein that comprises four different major domains: the acidic N-terminal half (projection domain) projects from the MT surface and the proline-rich domain, which harbors a SH3-protein binding site (21, 22); the function(s) of these parts of the tau protein…”
BackgroundAnnadurai, N., Sanctis, J. B. D., Hajdúch, M., & Das, V. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113756 · Cited by 41 · see citing works
Loss of forebrain BIN1 attenuates hippocampal pathology and neuroinflammation in a tauopathy model
Ponnusamy, M., Wang, S., Yuksel, M., Hansen, M. T., Blazier, D. M., McMillan, J. D., Zhang, X., Dammer, E. B., Collier, L. A., & Thinakaran, G. (2022) · Brain · doi:10.1093/brain/awac318 · Cited by 42 · see citing works
NMR Meets Tau: Insights into Its Function and Pathology
Lippens, G. M., Landrieu, I., Smet‐Nocca, C., Huvent, I., Gandhi, N. S., Gigant, B., Despres, C., Qi, H., & Lopez, J. M. (2016) · Biomolecules · doi:10.3390/biom6020028 · Cited by 34 · see citing works
“Bin1, one of the first genetic factors linked to Tau pathology [152] that came out of a genome-wide association study of AD patients [153], was shown to interact physically with Tau after phosphorylation of the latter in its PRR region [154].”
BackgroundSelf-citationGlennon, 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
Carroll, T., Guha, S. K., Nehrke, K. W., & Johnson, G. V. W. (2021) · Biology · doi:10.3390/biology10101047 · Cited by 35 · see citing works
“Phosphorylation within the PRD, and specifically of T231, decreases BIN1′s affinity for tau by interrupting the interaction between the tau PRD and BIN1′s SH3 domain [106].”
BackgroundA peptide inhibitor of Tau-SH3 interactions ameliorates amyloid-β toxicity
Rush, T., Roth, J. R., Thompson, S. J., Aldaher, A. R., Cochran, J. N., & Roberson, E. D. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104668 · Cited by 30 · see citing works
“Tau’s proline-rich domain binds directly to BIN1’s SH3 domain and phosphorylation of Tau regulates this binding (Sottejeau et al., 2015), highlighting a potential role for the Tau-BIN1 interaction in Tau-mediated AD deficits.”
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
The Mechanistic Role of Bridging Integrator 1 (BIN1) in Alzheimer’s Disease
Gao, P.-R., Ye, L., Cheng, H.-R., & Li, H. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00926-y · Cited by 28 · see citing works
Danis, C., Despres, C., Bessa, L. M., Malki, I., Merzougui, H., Huvent, I., Qi, H., Lippens, G. M., Cantrelle, F., Schneider, R. C., et al. (2016) · Journal of Visualized Experiments · doi:10.3791/55001 · Cited by 26 · see citing works
Self-citationCell-autonomous and non-cell autonomous effects of neuronal BIN1 loss in vivo
McAvoy, K. M., Sait, H. R., Marsh, G., Peterson, M. A., Reynolds, T. L., Gagnon, J., Geisler, S. B., Leach, P. T., Roberts, C., Cahir-McFarland, E. D., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0220125 · Cited by 26 · see citing works
Morris, S. L., Tsai, M.-Y., Aloe, S., Bechberger, K., König, S., Morfini, G. A., & Brady, S. T. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.610037 · Cited by 25 · see citing works
“Consistent with this idea, tau is known to interact with several SH3 domain proteins in a phosphorylation-dependent manner (Reynolds et al., 2008; Usardi et al., 2011; Sottejeau et al., 2015).”
BackgroundTau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease
Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23 · see citing works
BIN1 localization is distinct from Tau tangles in Alzheimer’s disease
Rossi, P. D., Buggia-Prévot, V., Andrew, R. J., Krause, S. V., Woo, E., Nelson, P. T., Pytel, P., & Thinakaran, G. (2017) · Matters · doi:10.19185/matters.201611000018 · Cited by 25 · see citing works
“BIN1 can directly bind to Tau, and the altered expression of Drosophila Amph (the fly BIN1 homolog) significantly modifies the human Tau-induced rough eye phenotype, leading to the suggestion that BIN1 mediates LOAD risk by modulating Tau pathology [6] [7] [8].”
Tangavelou, K., & Bhaskar, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212335 · Cited by 24 · see citing works
“Tau has been shown to interact with BIN1, whereas AD-associated phosphorylated tau T231 decreases interaction with BIN1 [120].”
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
“NMR measurements revealed a molecular interaction between the SH3 domain of BIN1 and the proline-rich domain (PRD) of tau, which is regulated by tau phosphorylation at T212, T217, T231, and S235 [69 – 71] (Figure 3).”
Self-citationAkram, Z., Ahmed, I., Mack, H., Kaur, R., Silva, R. C., Castilho, B. A., Friant, S., Sattlegger, E., & Munn, A. (2020) · Cells · doi:10.3390/cells9030672 · Cited by 20 · see citing works
Endosomal trafficking and related genetic underpinnings as a hub in Alzheimer's disease
Limone, A., Veneruso, I., D’Argenio, V., & Sarnataro, D. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30864 · Cited by 16 · see citing works
“Beside this, BIN1 expression correlates also with tau pathology (Calafate et al., 2016), indeed it directly interacts with tau and such interaction is downregulated by tau phosphorylation on Thr231 (Sottejeau et al., 2015).”
BackgroundBin1 antibody lowers the expression of phosphorylated Tau in Alzheimer's disease
Thomas, S., Hoxha, K., Tran, A., & Prendergast, G. C. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29142 · Cited by 15 · see citing works
Alipour, M., Motavaf, M., Abdolmaleki, P., Zali, A., Ashrafi, F., Safari, S., & Verdom, B. H. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.884705 · Cited by 14 · see citing works
“The projection domain is made of acidic residues followed by a proline-rich region, and the MBD consists of several repeats of microtubule-binding sequences that consist of 31 or 32 residues (Sottejeau et al., 2015; Barbier et al., 2019).”
BackgroundJin, Y., Zhao, L., Zhang, Y., Chen, T., Shi, H., Sun, H., Ding, S., Chen, S., Cao, H., Zhang, G., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2393932 · Cited by 14 · see citing works
“BIN1 directly interacts with MAPT/Tau via its C-terminal SH3 domain [9,10]; in various cellular and mouse models, BIN1 regulates MAPT/ Tau pathology, the transcellular spreading of MAPT/Tau [9,11,12], and MAPT/Tau-dependent neuronal network excitability [13].”
Danis, C., Dupré, E., Hanoulle, X., Landrieu, I., Lasorsa, A., Neves, J. F., Schneider, R., & Smet‐Nocca, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_3 · Cited by 11 · see citing works
Self-citationBIN1K358R suppresses glial response to plaques in mouse model of Alzheimer's disease
Garcia‐Agudo, L. F., Shi, Z., Smith, I. F., Kramár, E. A., Tran, K., Kawauchi, S., Wang, S., Collins, S., Walker, A., Shi, K., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13767 · Cited by 10 · see citing works
Oh, Y. R., & Shin, M. (2025) · BMB Reports · doi:10.5483/bmbrep.2025-0077 · 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-citationThe Role of Tau in the Post-synapse
Regan, P. L., & Cho, K. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_10 · Cited by 7 · see citing works
Oatman, S. R., Reddy, J. S., Atashgaran, A., Wang, X., Min, Y., Quicksall, Z., Vanelderen, F., Carrasquillo, M. M., Liu, C.-C., Yamazaki, Y., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68864-9 · Cited by 6 · see citing works
“Many of these genes also have previous connections with tau, such as BIN1 which is known to interact with tau proteins in extracellular vesicles 88,89 including tau Thr231 90 which is the pTau species measured in our study, ANXA2 55,56 , as well as CDK18 57,58 needtoverifythecasualdirectionofeffectbetweentheserCpGmsan…”
InfluentialRational Modulation of Liquid–Liquid Phase Separation Offers Novel Ways to Combat Tauopathies
Zhang, X., Wang, L., Lin, N., Gao, M. Y., & Huang, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146709 · Cited by 5 · see citing works
“The PRD of tau contains seven proline-rich motifs, of which some can be recognized by the SH3 domains of the tyrosine kinase Fyn and membrane remodeling protein BIN1 [54–56].”
Thomas, S., & Prendergast, G. C. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1183932 · Cited by 7 · see citing works
“Notably, tau phosphorylation at Thr231 and other nearby residues negates Bin1 SH3 binding, precluding normal binding and enabling accumulation and aggregation of hyperphosphorylated tau that causes AD pathophysiology (Sottejeau et al., 2015).”
BackgroundBIN1 in the Pursuit of Ousting the Alzheimer’s Reign: Impact on Amyloid and Tau Neuropathology
Kaur, I., Behl, T., Sundararajan, G., Panneerselvam, P., Vijayakumar, A. R., Senthilkumar, G. P., Venkatachalam, T., Jaglan, D., Yadav, S., Anwer, K., et al. (2023) · Neurotoxicity Research · doi:10.1007/s12640-023-00670-3 · Cited by 6 · see citing works
“…account the presence of the N-terminal BAR domain in all BIN1 isoforms, which facilitates membrane binding as well as curvature, along with a C-terminal SH3 domain, mediating binding in between two proteins, including with tau (Voskobiynyk et al. 2020; Chapuis et al. 2013c; Sottejeau et al. 2015).”
BackgroundCehlár, O., Bagarova, O., Hornakova, L., & Škrabana, R. (2021) · General Physiology and Biophysics · doi:10.4149/gpb_2021031 · Cited by 7 · 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
“Of particular interest to the AD field, BIN1’s SH3 domain has also been shown to interact with tau in vitro (36–38).”
BIN1 gene replacement reverses BIN1-related centronuclear myopathy
Ji, J., Giraud, Q., Diedhiou, N., Lipkow, E., Spiegelhalter, C., & Laporte, J. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.04.036 · Cited by 5 · see citing works
Self-citationBretteville, A., Demiautte, F., & Chapuis, J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_18 · Cited by 4 · see citing works
“We recently successfully used this methodology to study the interaction of Tau with Bin1 as well as its subsequent regulation by phosphorylation (see Note 2) [9].”
BackgroundMethodInfluentialSelf-citationMendes, T., Herlédan, A., Leroux, F., Deprez, B. P., Lambert, J., & Kilinc, D. (2019) · Current Protocols in Cell Biology · doi:10.1002/cpcb.100 · Cited by 4 · see citing works
“BIN1 modulates tau pathology (Chapuis et al., 2013) and physically interacts with tau in primary neurons (Sottejeau et al., 2015).”
BackgroundSelf-citationTheron, D., Hopkins, L. N., Sutherland, H. G. E., Griffiths, L. R., & Fernandez, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713480 · 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
“In contrast, its SH3 domain interacts with Tau’s proline-rich regions [30, 38–41].”
Endocytic scaffolds at the crossroads of Alzheimer’s disease and neuronal aging
Shergill, J. K., & Tehran, D. A. (2026) · Biological Chemistry · doi:10.1515/hsz-2025-0250 · Cited by 2 · see citing works
“…role as a membrane-remodeling protein in AD, a direct interaction was reported between the SH3 domains of BINiso1 and BINIso9 and tau (Malki et al. 2017) (Figure 3), and this interaction is modulated by the phosphorylation status of both tau (Sottejeau et al. 2015) and BIN1 (Sartori et al. 2019).”
Lambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Davoine, L., Dupont, C., Amouyel, P., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.02.438184 · Cited by 2 · see citing works
Self-citationDuckhorn, 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
“Direct interactions between BIN1 and tau have been reported in multiple models (Chapuis et al., 2013; Sottejeau et al., 2015; Malki et al., 2017; Lasorsa et al., 2018; Sartori et al., 2019; Glennon et al., 2020), potentially influencing tau aggregation, propagation, and neurotoxicity.”
Maaser‐Hecker, A., Zellmer, J. C., Kim, M. M., Bakiasi, G., Maiti, A. K., Curtat, M. P. C., Choi, S. H., Prokopenko, D., Tanzi, R. E., & Bhattacharyya, R. (2026) · Science Advances · doi:10.1126/sciadv.adx2127 · Cited by 2 · see citing works
Cerebrospinal Fluid Tau and Phosphotau As Biomarkers in Alzheimer's Disease Diagnosis
Ahmadian, N., Talebi, M., Mahmoudi, J., Etegad, S. S., & Aghili, A. (2019) · Basic and Clinical Neuroscience Journal · doi:10.32598/bcn.9.10.445 · Cited by 1 · see citing works
Schneeweis, A. K., & Pak, D. T. S. (2023) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2023.106475 · Cited by 1 · see citing works
Genetic Risk Factors for Complex Forms of Alzheimer’s Disease
Bellenguez, C., & Lambert, J. (2018) · Springer eBooks · doi:10.1007/978-3-319-72938-1_4
Self-citationAutophagic Dysfunction in Neurodegeneration
Kaira, M., Ahlawat, A., Walia, V., & Garg, M. (2020) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-7998-1317-0.ch002
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
Molecular insights into the Tau-actin interaction
Fontela, Y. C. (2018) · doi:10.53846/goediss-6842
Hu, M., Esmaeeli, S., Stolzenburg, L. R., Milkovich, B., Jouni, M., Nyamugenda, E., Hammond, R. K., Reinhardt, P., Bahnassawy, L., Gasparini, L., et al. (2026) · Frontiers in Aging Neuroscience · doi:10.1101/2025.03.31.646439 · Cited by 2 · see citing works
BIN1 deficiency leads to DNA damage and neuronal insulin resistance through ATM dysregulationPreprint
Jin, Y., Shi, H., Zhao, L., Zhang, G., Ding, S., Wu, Y., Fan, W., Liu, Z., Ruan, H., Li, Y., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.20.671271
“6-8 BIN1 directly interacts with TAU, 9-11 and regulates intercellular propagation of TAU pathology; 12 overexpression of BIN1 induces neuronal network hyperexcitability in a TAU-dependent manner.”
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
“…a peptide from the C-terminal proline-rich domain of p140Cap that binds to BIN1’s SH3 domain with an affinity (K D = 7.7 μ M) comparable to those of well-characterized and functionally relevant interactors, including dynamin and tau (K D = 8–20 μ M and 12–44 μ M, respectively) (32, 34–37).”
InfluentialGaffour, A., Bakker, M. J., Bera, K., & Přecechtělová, J. P. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.09.037
Nuclear BIN1 isoforms regulate c-Myc-mediated cell cycle control in oligodendrocytesPreprint
Ma, I. W.-T., Cheng, G. W., Yeung, S. H., Yeung, M. H. Y., Kofler, J., Herrup, K., & Tse, K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.30.676706
Lambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093090
Self-citationLambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093108
Self-citationLambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093111
Self-citationLambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093117
Self-citationLambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093105
Self-citationLambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093096
Self-citationLambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093093
Self-citationAdditional file 1 of Synaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Figshare · doi:10.6084/m9.figshare.16599510
Lambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093099
Self-citationLambert, E., Saha, O., Landeira, B. S., de Farias, A. R. M., Hermant, X., Carrier, A., Pelletier, A., Gadaut, J., Davoine, L., Dupont, C., et al. (2022) · Figshare · doi:10.6084/m9.figshare.18093102
Self-citationEvaluating 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
Study of the Neuron-Astrocyte Relationship in a Rodent Model of Tauopathy
de Gérando, A. M. (2019) · theses.fr (ABES) · doi:10.70675/04658671zaca3z4fefza24dz2f5a011bebfe
Denéchaud, M. (2022) · theses.fr (ABES) · doi:10.70675/623e7224z0cb0z47b1z8a22z549acf553ac0
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
“A structural model of the Bin1-SH3/tau(213–229) complex was constructed on the basis of nuclear magnetic resonance spectroscopy data and this revealed the effect of tau(210–240) phosphorylation on its interaction with Bin1 isoform 1 [57].”
- Authors
- Sottejeau, Y., Bretteville, A., Cantrelle, F.-X., Malmanche, N., Demiaute, F., Mendes, T., Delay, C., Alves Dos Alves, H., Flaig, A., Davies, P., Dourlen, P., Dermaut, B., Laporte, J., Amouyel, P., Lippens, G., Chapuis, J., Landrieu, I., & Lambert, J.-C.
- Affiliations
- Inserm (FR)
- Centre National de la Recherche Scientifique (FR)
- Albert Einstein College of Medicine (US)
- Corresponding author
- Landrieu, Isabelle
- Lambert, Jean-Charles
- ORCID
- Venue
- Acta Neuropathologica Communications
- Published
- 2015-09-23
- Volume
- 3
- Issue
- 1
- Pages
- 58-58
- ISSN
- 2051-5960 (ISSN-L)
- PMC
- PMC4580349
- OpenAlex
- W1941934587
- Semantic Scholar
- 2535be70d4491da846131120ab4bfb7ce8b0a0a6
- Cited by
- 98
- References
- 34
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 5 · 2023: 7 · 2022: 14 · 2021: 9 · 2020: 8 · 2019: 16 · 2018: 5 · 2017: 6 · 2016: 8 · 2013: 1
- FWCI
- 4.67
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Acta Neuropathologica Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (publishedVersion)
- HAL (submittedVersion, other-oa)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, cc-by)
- LillOA (Université de Lille (University Of Lille)) (submittedVersion)
- LillOA (Université de Lille (University Of Lille)) (submittedVersion, cc-by)
- univOAK (4 institutions : Université de Strasbourg, Université de Haute Alsace, INSA Strasbourg, Bibliothèque Nationale et Universitaire de Strasbourg) (submittedVersion, cc-by)
- Funders
- Alzheimer's Association (US) (IIRG-06-25487)
- 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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- BIN1, tau protein, tau phosphorylation, SH3 domain, proline-rich region, protein-protein interaction, Alzheimer's disease, actin cytoskeleton
- MeSH terms
- Animals, Animals, Newborn, Brain, Cells, Cultured, Humans, Neurons, Magnetic Resonance Spectroscopy, Nuclear Proteins, Phosphorylation, Proline, Protein Conformation, Transfection, tau Proteins, src Homology Domains, Tumor Suppressor Proteins, Adaptor Proteins, Signal Transducing, Rats, HEK293 Cells
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