CoChat
Sign Up
Cited by 256Cellular transport and secretionNeuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental Disorders

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 access
Butler, Margaret Husta, David, Carol, Ochoa, Gian-Carlo, Freyberg, Zachary, Daniell, Laurie, Grabs, Detlev, Cremona, Ottavio, Camilli, Pietro De·1997·The Journal of Cell Biology
DOI 10.1083/jcb.137.6.1355PMC PMC2132527
Open this paper in CoChat — free account

Abstract

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.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1083/jcb.137.6.1355

Cites

66 of 66 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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?

  • BIN1 undergoes complex alternative splicing to generate multiple isoforms with diverse functions in multiple cellular processes including endocytosis and membrane remodeling.

    “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]

    The Results (Cloning of Amphiphysin II) identify alternatively spliced BIN1 variants. The Discussion proposes that different isoforms may serve distinct functions, including roles related to endocytosis, but presents these roles as hypotheses rather than established functions of BIN1 isoforms. It does not establish membrane remodeling as one of those functions; page numbers were not provided in our copy. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • A C-terminal SH3 domain found in all BIN1 isoforms mediates interaction with proteins involved in endocytosis such as dynamin, synaptojanin, and endophilin.

    “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]

    The Results ('Amphiphysin II Is Primarily Expressed in Brain and Muscle'; page not specified) report that the amphiphysin II/BIN1 SH3 domain binds dynamin I and synaptojanin, although it binds synaptojanin less effectively than the amphiphysin I domain. The paper describes alternative splicing and a conserved SH3-containing domain, but does not establish the claim for every BIN1 isoform or report an interaction with endophilin. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Seven brain-specific and two ubiquitous BIN1 isoforms have been reported previously.

    “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]

    The Results sections on cloning and tissue expression describe alternatively spliced BIN1/amphiphysin II variants, including a splice segment preferentially found in brain. They do not report seven brain-specific and two ubiquitous isoforms; the two full-length clones described are not identified as ubiquitous. Page numbers are unavailable in our copy. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • BIN1 is broadly expressed in several tissues, with the highest expression in skeletal muscle.

    “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]

  • It is generally assumed, and in a few papers described, that BIN1 is expressed in neurons.

    “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]

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

Flagged first, then by citations

1 of the 67 references couldn’t be matched to a known paper.

Research works printed but not linked: 2

  1. Kordeli E Lambert S Bennett V AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier J Biol Chem 1995 270 2352 2359 7836469
  2. Peters, A., S. Palay, and H. Webster. 1991. The axon. In The Fine Structure of the Nervous System. A. Peters, S.L. Palay, and H. Webster, editors. Oxford University Press, New York. 101–137.

Cited by

Sorted by citations

Related

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
ORCID
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
DOI
10.1083/jcb.137.6.1355
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
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

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