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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
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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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“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.
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“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]
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“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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“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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“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]
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“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]
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“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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Cells Control BIN1-Mediated Membrane Tubulation by Altering the Membrane Charge
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Peripheral Blood T Cell Gene Expression Responses to Exercise and HMB in Sarcopenia
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Kim, K., Kim, T.-S., Kang, K., & Choi, K. (2001) · Oncogene · doi:10.1038/sj.onc.1204839 · Cited by 15
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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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