Cited by 67Cellular Mechanics and InteractionsCell Adhesion Molecules ResearchDevelopmental Biology and Gene Regulation

The Drosophila CD2AP/CIN85 orthologue Cindr regulates junctions and cytoskeleton dynamics during tissue patterning

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Johnson, Ruth I., Seppa, Midori J., Cagan, Ross L.·2008·The Journal of Cell Biology

Abstract

Developing tissues require cells to undergo intricate processes to shift into appropriate niches. This requires a functional connection between adhesion-mediating events at the cell surface and a cytoskeletal reorganization to permit directed movement. A small number of proteins are proposed to link these processes. Here, we identify one candidate, Cindr, the sole Drosophila melanogaster member of the CD2AP/CIN85 family (this family has been previously implicated in a variety of processes). Using D. melanogaster retina, we demonstrate that Cindr links cell surface junctions (E-cadherin) and adhesion (Roughest) with multiple components of the actin cytoskeleton. Reducing cindr activity leads to defects in local cell movement and, consequently, tissue patterning and cell death. Cindr activity is required for normal localization of Drosophila E-cadherin and Roughest, and we show additional physical and functional links to multiple components of the actin cytoskeleton, including the actin-capping proteins capping protein alpha and capping protein beta. Together, these data demonstrate that Cindr is involved in dynamic cell rearrangement in an emerging epithelium.

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  • CD2AP is involved in cell-cell adhesion, regulates the actin cytoskeleton, and physically interacts with p130CAS (CASS1).

    “CD2AP is involved in cell–cell adhesion, regulates the actin cytoskeleton and physically interacts with p130CAS (CASS1) [61, 74].”

    From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [61]

    The Introduction links CD2AP to adhesion molecules and actin dynamics, supporting the cell–cell adhesion and cytoskeleton portions of the claim. Our copy does not report a physical interaction with p130Cas; p130Cas appears only in a reference title about the two proteins localizing to different F-actin structures. (LLM, conf=0.88)

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Cited by

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Authors
Johnson, R. I., Seppa, M. J., & Cagan, R. L.
Affiliations
  • Icahn School of Medicine at Mount Sinai (US)
  • Washington University in St. Louis (US)
Venue
The Journal of Cell Biology
Published
2008-03-24
Volume
180
Issue
6
Pages
1191-1204
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2046239158
Cited by
67
References
1
Citations by year
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FWCI
2.58
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)
  • Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
  • Wesleyan University Digital Collections (Wesleyan University) (submittedVersion, public-domain)
Funders
  • National Institutes of Health
  • National Eye Institute (R01-EY1149, R01EY011495)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords
Drosophila melanogaster, E-cadherin, cell adhesion, cell junctions, actin cytoskeleton, capping protein, cell motility, tissue patterning, retinal development, epithelial morphogenesis, cell death
MeSH terms
Actins, Animals, Cell Adhesion, Cytoskeletal Proteins, Cytoskeleton, Drosophila melanogaster, Embryo, Nonmammalian, Epithelium, Eye, Eye Proteins, Intercellular Junctions, Microfilament Proteins, Cell Adhesion Molecules, Neuronal, Cadherins, Gene Expression Regulation, Developmental, Body Patterning, Drosophila Proteins, Animals, Genetically Modified, Adaptor Proteins, Signal Transducing, Actin Capping Proteins

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