Evidence map›Paper›PMID 26478182›Full record

ArticleCell2015

Molecular logic of neuronal self-recognition through protocadherin domain interactions.

Rotem Rubinstein, Chan Aye Thu, Kerry Marie Goodman, Holly Noelle Wolcott, Fabiana Bahna, Seetha Mannepalli, Goran Ahlsen, Maxime Chevee, Adnan Halim, Henrik Clausen and 3 more

Abstract read
In one paragraph

Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

116 citing papers in PubMed.

  1. Article
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  5. Article
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  7. Article
  8. Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026
    Review
  9. Article
  10. Surface delivery quantification reveals distinct trafficking efficiencies among clustered protocadherin isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Clustered protocadherinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article

56 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Rotem RubinsteinDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Department of Systems Biology, Columbia University, New York, NY 10032, USA.
Chan Aye ThuDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Kerry Marie GoodmanDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Holly Noelle WolcottDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Fabiana BahnaDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA.
Seetha MannepalliDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Goran AhlsenDepartment of Systems Biology, Columbia University, New York, NY 10032, USA; Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA.
Maxime CheveeDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Adnan HalimCopenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.
Henrik ClausenCopenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.
Tom ManiatisDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Lawrence ShapiroDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Department of Systems Biology, Columbia University, New York, NY 10032, USA. Electronic address: lss8@columbia.edu.
Barry HonigDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Department of Systems Biology, Columbia University, New York, NY 10032, USA; Department of Medicine, Columbia University, New York, NY 10032, USA; Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10032, USA; Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA. Electronic address: bh6@columbia.edu.

Funding

TRAINING PROGRAM IN MOLECULAR BIOPHYSICST32GM008281 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PALMER, ARTHUR G · 1988 to 2017
$5.4M
MOLECULAR BASIS OF CADHERIN MEDIATED CELL ADHESIONR01GM062270 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI SHAPIRO, LAWRENCE S · 2001 to 2015
$3.4M
The structural basis of cis and trans protocadherin interactionsR01GM107571 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MANIATIS, THOMAS P, SHAPIRO, LAWRENCE S · 2013 to 2016
$1.8M
NIGMS NIH HHS R01 GM062270NIGMS NIH HHS R01GM062270NIGMS NIH HHS R01 GM107571NIGMS NIH HHS R01GM107571NIGMS NIH HHS T32 GM008281NIGMS NIH HHS T32GM008281
6 · The paper itself

Abstract

Self-avoidance, a process preventing interactions of axons and dendrites from the same neuron during development, is mediated in vertebrates through the stochastic single-neuron expression of clustered protocadherin protein isoforms. Extracellular cadherin (EC) domains mediate isoform-specific homophilic binding between cells, conferring cell recognition through a poorly understood mechanism. Here, we report crystal structures for the EC1-EC3 domain regions from four protocadherin isoforms representing the α, β, and γ subfamilies. All are rod shaped and monomeric in solution. Biophysical measurements, cell aggregation assays, and computational docking reveal that trans binding between cells depends on the EC1-EC4 domains, which interact in an antiparallel orientation. We also show that the EC6 domains are required for the formation of cis-dimers. Overall, our results are consistent with a model in which protocadherin cis-dimers engage in a head-to-tail interaction between EC1-EC4 domains from apposed cell surfaces, possibly forming a zipper-like protein assembly, and thus providing a size-dependent self-recognition mechanism.

Indexed as

Amino Acid SequenceAnimalsCadherinsCrystallography, X-RayMiceModels, MolecularMolecular Sequence DataNervous System Physiological PhenomenaNeuronsProtein Structure, TertiarySequence AlignmentCadherins

Identifiers

PMID26478182
PMCPMC4624033

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.