The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Armadillo is required for adherens junction assembly, cell polarity, and morphogenesis during Drosophila embryogenesis.
Open accessAbstract
Morphological and biochemical analyses have identified a set of proteins which together form a structure known as the adherens junction. Elegant experiments in tissue culture support the idea that adherens junctions play a key role in cell-cell adhesion and in organizing cells into epithelia. During normal embryonic development, cells quickly organize epithelia; these epithelial cells participate in many of the key morphogenetic movements of gastrulation. This prompted the hypothesis that adherens junctions ought to be critical for normal embryonic development. Drosophila Armadillo, the homologue of vertebrate beta-catenin, is a core component of the adherens junction protein complex and has been hypothesized to be essential for adherens junction function in vivo. We have used an intermediate mutant allele of armadillo, armadilloXP33, to test these hypotheses in Drosophila embryos. Adherens junctions cannot assemble in the absence of Armadillo, leading to dramatic defects in cell-cell adhesion. The epithelial cells of the embryo lose adhesion to each other, round up, and apparently become mesenchymal. Mutant cells also lose their normal cell polarity. These disruptions in the integrity of epithelia block the appropriate morphogenetic movements of gastrulation. These results provide the first demonstration of the effect of loss of adherens junctions on Drosophila embryonic development.
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“Indeed, experiments in Drosophila have shown that mutations in junctional proteins not only affect junction formation but also disturb epithelial polarity, whereas polarity mutants have a profound effect on junction formation as well (Cox et al, 1996;Muller and Wieschaus, 1996;Tanentzapf et al, 2000).”
From E‐cadherin is essential for in vivo epidermal barrier function by regulating tight junctions (2005) · cites this paper as Cox et al, 1996
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Müller, H. A., & Wieschaus, E. (1996) · The Journal of cell biology · doi:10.1083/jcb.134.1.149 · Cited by 384
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“Genetic and biochemical*Department of Immunology University Hospital studies have revealed the regions essential for interaction with Armadillo’s adherens junction partners (Orsulic3508 GA, Utrecht The Netherlands and Peifer, 1996a; Cox et al., 1996; Pai et al., 1996).”
BackgroundSelf-citationAdherens junctions: from molecules to morphogenesis
Harris, T., & Tepass, U. (2010) · Nature reviews. Molecular cell biology · doi:10.1038/nrm2927 · Cited by 983
“These responses require the cells to be connected by AJ”
BackgroundMOLECULAR AND FUNCTIONAL ANALYSIS OF CADHERIN-BASED ADHERENS JUNCTIONS
Yap, A. S., Brieher, W. M., & Gumbiner, B. M. (1997) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.13.1.119 · Cited by 818
Phosphorylation of β-Catenin by AKT Promotes β-Catenin Transcriptional Activity
Fang, D., Hawke, D. H., Zheng, Y., Xia, Y., Meisenhelder, J., Nika, H., Mills, G. B., Kobayashi, R., Hunter, T. R., & Lu, Z. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611871200 · Cited by 888
Metadata
- Authors
- Cox, R. T., Kirkpatrick, C., & Peifer, M.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1996-07-01
- Volume
- 134
- Issue
- 1
- Pages
- 133-148
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2120919
- OpenAlex
- W2030945799
- Cited by
- 300
- References
- 58
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 4 · 2023: 2 · 2022: 7 · 2021: 6 · 2020: 8 · 2019: 9 · 2018: 6 · 2017: 7 · 2016: 4 · 2015: 3 · 2014: 3 · 2013: 10 · 2012: 7
- FWCI
- 7.46
- 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)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM007092, 5T32 GM-07092)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- armadillos, β-catenin, cell-cell adhesion, epithelial morphogenesis, cell polarity, gastrulation, Drosophila embryogenesis, mesenchymal transition, epithelial barrier integrity
- MeSH terms
- Actins, Animals, Cell Adhesion, Cytoskeletal Proteins, DNA Mutational Analysis, Drosophila melanogaster, Epithelial Cells, Gastrula, Intercellular Junctions, Membrane Proteins, Actin Cytoskeleton, Microscopy, Electron, Scanning, Morphogenesis, Oogenesis, Proteins, Transcription Factors, Trans-Activators, Cell Adhesion Molecules, Cadherins, Cell Polarity, Drosophila Proteins, alpha Catenin, Armadillo Domain Proteins
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