Cited by 90Cell Adhesion Molecules ResearchSkin and Cellular Biology ResearchCellular Mechanics and Interactions

Recruitment of Nectin-3 to Cell-Cell Junctions through trans-Heterophilic Interaction with CD155, a Vitronectin and Poliovirus Receptor That Localizes to αvβ3 Integrin-containing Membrane Microdomains

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Mueller, Steffen, Wimmer, Eckard·2003·Journal of Biological Chemistry

Abstract

Nectins present a novel class of Ig superfamily adhesion molecules that, cooperatively with cadherins, establish and maintain cell-cell adherens junctions. CD155, the cognate receptor for poliovirus, undergoes cell-matrix contacts by binding to the extracellular matrix protein vitronectin. The significant homology of nectins with CD155 prompted us to investigate the possibility of their interaction. We determined that nectin-3 binds CD155 and its putative mouse homologue Tage4 in cell-based ligand binding assays. Coculture of nectin-3- and CD155-expressing HeLa cells led to CD155-dependent recruitment of nectin-3 to cell-cell contacts. In a heterologous coculture system with CD155 expressing mouse neuroblastoma cells, HeLa cell-expressed nectin-3 was recruited to contact sites with CD155 bearing neurites. CD155 and nectin-3 colocalized to epithelial cell-cell junctions in renal proximal tubules and in the amniotic membrane. Efficient interaction depended on CD155 dimerization, which appears to be aided by cell type-specific cofactors. We furthermore found CD155 to codistribute with alpha(v) integrin microdomains on the surface of transfected mouse fibroblasts and at amniotic epithelial cell junctions. Our findings demonstrate the possible trans-interaction between the bona fide cell-cell adherens type adhesion system (cadherin/nectin) and the cell-matrix adhesion system (integrin/CD155) by virtue of their nectin-3 and CD155 components, respectively.

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Crossref · 10.1074/jbc.m304166200

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  • Substitutions in the IRES contribute most to the attenuated phenotype of the Sabin 1 and Sabin 3 strains.

    “The substitutions in the IRES, which alter stem-loop structures (63, 68, 126, 132) and reduce the efficiency of initiation of translation of the poliovirus RNA template (68, 188), contribute most to the attenuated phenotype of the Sabin 1 and Sabin 3 strains.”
  • Mutations that restore the original stem-loop structure in the IRES are frequently found in vaccine-related isolates from healthy OPV recipients, patients with VAPP, and the environment.

    “Mutations that restore the original stem-loop structure in the IRES [Sabin 1: G480A (backmutation) or U525C (suppressor); Sabin 2: A481G;Sabin3:U472C]arefrequentlyfound in vaccine-related isolates from healthy OPV recipients (127, 132) and patients with VAPP (61), as well as from the environment (228).”

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Authors
Mueller, S., & Wimmer, E.
Affiliations
Stony Brook University (US)
Corresponding author
Wimmer, Eckard
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-08
Volume
278
Issue
33
Pages
31251-31260
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1980311792
Cited by
90
References
56
Citations by year
2024: 2 · 2023: 1 · 2022: 5 · 2021: 1 · 2020: 4 · 2019: 3 · 2018: 2 · 2017: 3 · 2016: 4 · 2015: 1 · 2014: 2 · 2013: 6 · 2012: 6
FWCI
4.51
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
National Institute of Allergy and Infectious Diseases (AI-39485)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
nectin-3, CD155, integrin αvβ3, poliovirus receptor, cell-cell contact, adherens junctions, alpha v beta 3 integrin, lipid rafts, trans-interactions, epithelial cell adhesion, amniotic membrane, proximal tubule
MeSH terms
Nectins, Amnion, Animals, Antigens, Neoplasm, Cell Adhesion, Cell Communication, Epithelial Cells, Fibroblasts, HeLa Cells, Humans, Intercellular Junctions, Kidney, Ligands, Membrane Proteins, Neoplasm Proteins, Neuroblastoma, Receptors, Cell Surface, Receptors, Virus, Cell Adhesion Molecules, PC12 Cells, Protein Structure, Tertiary, Dimerization, COS Cells, Integrin alphaVbeta3, Mice, Rats

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