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Amphiphysin II (SH3P9; BIN1), a Member of the Amphiphysin/Rvs Family, Is Concentrated in the Cortical Cytomatrix of Axon Initial Segments and Nodes of Ranvier in Brain and around T Tubules in Skeletal Muscle
Open accessAbstract
Amphiphysin (amphiphysin I), a dominant autoantigen in paraneoplastic Stiff-man syndrome, is a neuronal protein highly concentrated in nerve terminals, where it has a putative role in endocytosis. The yeast homologue of amphiphysin, Rvs167, has pleiotropic functions, including a role in endocytosis and in actin dynamics, suggesting that amphiphysin may also be implicated in the function of the presynaptic actin cytoskeleton. We report here the characterization of a second mammalian amphiphysin gene, amphiphysin II (SH3P9; BIN1), which encodes products primarily expressed in skeletal muscle and brain, as differentially spliced isoforms. In skeletal muscle, amphiphysin II is concentrated around T tubules, while in brain it is concentrated in the cytomatrix beneath the plasmamembrane of axon initial segments and nodes of Ranvier. In both these locations, amphiphysin II is colocalized with splice variants of ankyrin3 (ankyrinG), a component of the actin cytomatrix. In the same regions, the presence of clathrin has been reported. These findings support the hypothesis that, even in mammalian cells, amphiphysin/Rvs family members have a role both in endocytosis and in actin function and suggest that distinct amphiphysin isoforms contribute to define distinct domains of the cortical cytoplasm. Since amphiphysin II (BIN1) was reported to interact with Myc, it may also be implicated in a signaling pathway linking the cortical cytoplasm to nuclear function.
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In the citing paper
“BIN1 undergoes complex alternative splicing to generate multiple isoforms with diverse functions in multiple cellular processes including endocytosis and membrane remodeling.”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [4]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“A C-terminal SH3 domain, also found in all isoforms, mediates BIN1 interaction with proteins involved in endocytosis, such as dynamin, synaptojanin, and endophilin [1, 4–6, 14].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [4]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Expression of seven brain-specific and two ubiquitous BIN1 isoforms have been reported previously [4, 6, 7].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [4]
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In the citing paper
“BIN1 has 10 isoforms that are expressed in the Central Nervous System (CNS).”
From BIN1 protein isoforms are differentially expressed in astrocytes, neurons, and microglia: neuronal and astrocyte BIN1 are implicated in tau pathology (2020) · cites this paper as [10]
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In the citing paper
“Unlike its close paralog Amphiphysin 1, BIN1 is broadly expressed in several tissues, with the highest expression in skeletal muscle [2, 4, 6, 11].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [4]
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“The findings detailed above were surprising because it is generally assumed, and in a few papers described, that BIN1 is expressed in neurons [4, 26, 30].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [4]
In the citing paper
“Isoform 8 is specifically expressed in muscle [10].”
From BIN1 protein isoforms are differentially expressed in astrocytes, neurons, and microglia: neuronal and astrocyte BIN1 are implicated in tau pathology (2020) · cites this paper as [10]
In the citing paper
“Isoforms 1 through 7 are brain specific with isoform 1 being exclusively expressed in neurons [10].”
From BIN1 protein isoforms are differentially expressed in astrocytes, neurons, and microglia: neuronal and astrocyte BIN1 are implicated in tau pathology (2020) · cites this paper as [10]
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4350 · Cited by 53,218
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
The structure of the nervous system of the nematode Caenorhabditis elegans
White, J. G., Southgate, E., Thomson, J. N., & Brenner, S. (1986) · Philosophical Transactions of the Royal Society of London. B, Biological Sciences · doi:10.1098/rstb.1986.0056 · Cited by 5,589
High-Efficiency Transformation of Mammalian Cells by Plasmid DNA
Chen, C., & Okayama, H. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.8.2745 · Cited by 5,327
Handbook of Chemical Neuroanatomy
Stern, C. D. (1986) · Neurochemistry International · doi:10.1016/0197-0186(86)90021-5 · Cited by 4,160
Association of the APC Gene Product with β-Catenin
Rubinfeld, B., Souza, B., Albert, I., Müller, O., Chamberlain, S. H., Masiarz, F. R., Munemitsu, S. M., & Polakis, P. G. (1993) · Science · doi:10.1126/science.8259518 · Cited by 1,223
Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
Takei, K., McPherson, P. S., Schmid, S. L., & Camilli, P. V. D. (1995) · Nature · doi:10.1038/374186a0 · Cited by 768
Self-citationA presynaptic inositol-5-phosphatase
McPherson, P. S., Garcia, E. P., Slepnev, V. I., David, C., Zhang, X., Grabs, D., Sossini, W. S., Bauerfeind, R., Nemoto, Y., & Camilli, P. V. D. (1996) · Nature · doi:10.1038/379353a0 · Cited by 585
Self-citation[30] Prediction and analysis of coiled-coil structures
Lupas, A. N. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)66032-7 · Cited by 575
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Morris, C. E. (2018) · Current topics in membranes · doi:10.1016/bs.ctm.2018.06.001 · Cited by 7
Amphiphysin1 inhibits vitronectin-mediated cell adhesion, spreading, and migration in vitro
Otsuka, A., Hirose, K., Kilimann, M. W., & Kamata, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00040-8 · Cited by 7
BIN1 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
Thirkill, C. E. (2006) · British Journal of Biomedical Science · doi:10.1080/09674845.2006.11732741 · Cited by 6
Transcriptomic characterization of postnatal muscle maturation
Simon, A., Djeddi, S., Bournon, P., Reiss, D. J., Thompson, J., & Laporte, J. (2025) · Disease Models & Mechanisms · doi:10.1242/dmm.052098 · Cited by 5
BIN1 reduction ameliorates DNM2 -related Charcot–Marie–Tooth neuropathy
Goret, M., Thomas, M., Edelweiss, E. F., Messaddeq, N., & Laporte, J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419244122 · Cited by 5
DuHadaway, J. B., Rowe, F., Elliott, K., Mao, N.-C., & Prendergast, G. C. (1999) · Cell Communication & Adhesion · doi:10.3109/15419069909034394 · Cited by 5
Sawada, T., Morinobu, S., Tsuji, S., Kawano, K.-I., Watanabe, T., Suenaga, T., Takahashi, T., Yamawaki, S., & Nishida, A. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.03.001 · Cited by 5
Pineda‐Lucena, A., & Arrowsmith, C. H. (2001) · Journal of Biomolecular NMR · doi:10.1023/a:1008387817677 · Cited by 5
Böhm, J., Vasli, N., Maurer, M., Cowling, B. S., Shelton, G. D., Kreß, W., Toussaint, A., Prokic, I., Schara, U., Anderson, T. J., et al. (2013) · PLoS Genetics · doi:10.1371/annotation/22ca13f1-1ce9-4bb5-9c9e-98670f7c4240 · Cited by 8
Zhu, X., Yu, Y., Jiang, Z., Otani, Y., & Fujitani, M. (2025) · Biomolecules · doi:10.3390/biom15060901 · Cited by 5
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
Proteomic insight into human directed selection of the domesticated chicken Gallus gallus.
Schmidt, C. J., Kim, D. K., Pendarvis, G. K., Abasht, B., & McCarthy, F. (2023) · PLoS ONE · doi:10.1371/journal.pone.0289648 · Cited by 5
Pannese, E. (2014) · Springer eBooks · doi:10.1007/978-3-319-06856-5_5 · Cited by 4
Fagg, W. S., Liu, N., Braunschweig, U., de Castro, K. L. P., Chen, X., Ditmars, F. S., Widen, S. G., Donohue, J. P., Módis, K., Russell, W. K., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.22.423880 · Cited by 4
Lipid-Dependent Interaction of Human N-BAR Domain Proteins with Sarcolemma Mono- and Bilayers
Auerswald, A., Gruber, T., Balbach, J., & Meister, A. (2020) · Langmuir · doi:10.1021/acs.langmuir.0c00649 · Cited by 3
The Molecular Machinery for Synaptic Vesicle Endocytosis
McPherson, P. S., Ritter, B., & Augustine, G. J. (2008) · Springer eBooks · doi:10.1007/978-0-387-77232-5_5 · Cited by 3
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Spooner, H. C., & Dixon, R. E. (2025) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00198.2025 · Cited by 3
SPECIAL FEATURES OF VESICLE TRAFFICKING IN SKELETAL MUSCLE CELLS
Kaisto, T. (2003) · Cited by 2
Organization of Ca2+ Signaling Microdomains in Cardiac Myocytes
Li, J., Richmond, B., & Hong, T. (2022) · Springer eBooks · doi:10.1007/978-3-031-08309-9_2 · Cited by 3
Grabs, D., & Bergmann, M. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-0005-3 · Cited by 2
Self-citationProteomic insight into human directed evolution of the domesticated chicken Gallus gallusPreprint
Schmidt, C. J., Kim, D. K., Pendarvis, G. K., Abasht, B., & McCarthy, F. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.07.525900 · Cited by 2
Duckhorn, J. C., Kim, D. K., & Huang, Y. A. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00243 · Cited by 2
Association of type 1 stiff-person syndrome and insulinoma: a case report and narrative review
Sibilla, M., Beccuti, G., Belcastro, S., Mortara, U., Parisi, S., Campra, D., Piovesan, A., Ferrero, B., Maccario, M., Papotti, M., et al. (2025) · HORMONES · doi:10.1007/s42000-025-00666-y · Cited by 1
Sharp, J. A., Lefèvre, C. M., & Nicholas, K. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815251-5.00003-7 · Cited by 1
Estudo clínico, histológico e molecular da miopatia centronuclear
Neto, O. L. A. (2014) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2014.tde-13012015-113703 · Cited by 1
Genetic mapping of eight SH3 domain genes on seven mouse chromosomes
Lee, C. G., Morse, H. C., Kay, B. K., & Kozak, C. A. (1999) · Mammalian Genome · doi:10.1007/s003359901011 · Cited by 1
Functional Characterization of Amphiphysin in Drosophila melanogaster
Chow, B. (2012) · TSpace (University of Toronto) · Cited by 1
Dysferlin and its role in the pathogenesis of muscular dystrophy
Hofhuis, J. (2013) · doi:10.53846/goediss-4183 · Cited by 1
Sharp, J. A., Watt, A. P., Bisana, S., Modepalli, V., Wanyonyi, S. S., Kumar, A., Kwek, J. H. L., COLLINS, R. A., Lefèvre, C. M., & Nicholas, K. R. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405171-3.00003-9
15 Role of immunohistochemical loss of bin1/amphiphysin2 in prostatic carcinoma
DuHadaway, J. B., & Prendergast, G. C. (2002) · Handbook of immunohistochemistry and in situ hybridization of human carcinomas · doi:10.1016/s1874-5784(02)80047-2
Chapter 3 The Caveolae Internalization Machinery
Orlichenko, L. S., & McNiven, M. A. (2005) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(05)36003-6
Turton, J. C., & Morgan, K. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7309-1_6
Lombardi, R. (2001) · edoc (University of Basel) · doi:10.5451/unibas-002540561
Indoleamine 2,3-Dioxygenase in Immune Escape: Regulation and Therapeutic Inhibition
Muller, A. J., & Prendergast, G. C. (2007) · Elsevier eBooks · doi:10.1016/b978-012372551-6/50083-3
Okamoto, Y. (2001) · Okayama Igakkai Zasshi (Journal of Okayama Medical Association) · doi:10.4044/joma1947.113.3_247
Cardiac T-Tubule Membranes - Nanostructure and Remodeling Mechanisms in Disease
Wagner, E. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4002
Zheng, H. (2020) · International Conference on Biomedical and Bioinformatics Engineering (ICBBE) · doi:10.1145/3444884.3444898
Atlas of Genetics and Cytogenetics in Oncology and Haematology
Thomas, S., Chang, M. Y., & Prendergast, G. C. (2015)
Towards improving the diagnosis and management of chronic cough in China.
Zeng, G., Sun, B., & Zhong, N. (2011) · PubMed
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
BIN1 expression in the presynaptic compartment leads to isoform-specific synaptotoxicityPreprint
Lambert, E., Gelle, C., Leclerc, V., Freire‐Regatillo, A., Barois, N., Malfoi, T., Hermant, X., Demiautte, F., Lafont, F., Amouyel, P., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.11.669624
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
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
Paracrine control of milk protein gene expression in tammar wallaby
Wanyonyi, S. S. (2013)
Berbey, C. (2009) · theses.fr (ABES) · doi:10.70675/02cc281ezae30z4efez838azab652b9c988c
Margaritakis, A., Qian, M., Johnson, D. H., Zeno, W. F., Ulmer, T. S., & Chung, P. J. (2026) · Communications Chemistry · doi:10.1038/s42004-026-01994-9
Nattarayan, V. (2019) · theses.fr (ABES) · doi:10.70675/ae3ccc54z0dc2z41eaz9235z249d0e67d964
Rôle des cavéoles dans la formation des tubules-T et dans la physiopathologie des cavéolinopathies
Lemerle, E. (2021) · theses.fr (ABES) · doi:10.70675/58c77c5fz53b2z4b69zbd20z59c3f768f824
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
RNA Splicing Dysregulation in Parkinson’s Disease
Bruno, M. G., Menichetti, G., Valentino, A., Javaid, A., Belpinati, F., Ruggiero, A., Valenti, M. T., Paolone, G., Cavaliere, F., Trabetti, E., et al. (2026) · Genes · doi:10.3390/genes17080911
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
Metadata
- Authors
- Butler, M. H., David, C., Ochoa, G.-C., Freyberg, Z., Daniell, L., Grabs, D., Cremona, O., & Camilli, P. D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1997-06-16
- Volume
- 137
- Issue
- 6
- Pages
- 1355-1367
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2132527
- OpenAlex
- W2031188680
- Cited by
- 256
- References
- 67
- Citations by year
- 2026: 5 · 2025: 13 · 2024: 2 · 2023: 7 · 2022: 6 · 2021: 13 · 2020: 11 · 2019: 7 · 2018: 6 · 2017: 3 · 2016: 11 · 2015: 6 · 2014: 12 · 2013: 11 · 2012: 3
- FWCI
- 5.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (P01CA046128, CA46128)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- BIN1, ankyrin-G, axon initial segment, nodes of Ranvier, T-tubules, actin cytoskeleton, endocytosis, clathrin, differential splicing, skeletal muscle, brain, stiff person syndrome
- MeSH terms
- Amino Acid Sequence, Animals, Axons, Base Sequence, Brain Chemistry, Carrier Proteins, Cerebral Cortex, Cloning, Molecular, Cytoplasm, Humans, Molecular Sequence Data, Muscle Proteins, Nerve Tissue Proteins, Nuclear Proteins, Rabbits, Ranvier's Nodes, Tumor Cells, Cultured, Gene Expression, DNA, Complementary, Muscle, Skeletal, src Homology Domains, COS Cells, Tumor Suppressor Proteins, Adaptor Proteins, Signal Transducing, Mice, Rats
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