Structure of cell-cell adhesion mediated by the Down syndrome cell adhesion molecule.
DSCAM
IgSF
cell adhesion
cell–cell interaction
electron tomography
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
28 09 2021
28 09 2021
Historique:
accepted:
09
07
2021
entrez:
17
9
2021
pubmed:
18
9
2021
medline:
8
10
2021
Statut:
ppublish
Résumé
The Down syndrome cell adhesion molecule (DSCAM) belongs to the immunoglobulin superfamily (IgSF) and plays important roles in neural development. It has a large ectodomain, including 10 Ig-like domains and 6 fibronectin III (FnIII) domains. Previous data have shown that DSCAM can mediate cell adhesion by forming homophilic dimers between cells and contributes to self-avoidance of neurites or neuronal tiling, which is important for neural network formation. However, the organization and assembly of DSCAM at cell adhesion interfaces has not been fully understood. Here we combine electron microscopy and other biophysical methods to characterize the structure of the DSCAM-mediated cell adhesion and generate three-dimensional views of the adhesion interfaces of DSCAM by electron tomography. The results show that mouse DSCAM forms a regular pattern at the adhesion interfaces. The Ig-like domains contribute to both
Identifiants
pubmed: 34531300
pii: 2022442118
doi: 10.1073/pnas.2022442118
pmc: PMC8488690
pii:
doi:
Substances chimiques
Cell Adhesion Molecules
0
DSCAML1 protein, mouse
0
Drosophila Proteins
0
Dscam protein, mouse
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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