Cadherins and their partners in the nematode worm Caenorhabditis elegans

Jeff Hardin, Allison Lynch, Timothy Loveless, Jonathan Pettitt

Research output: Chapter in Book/Report/Conference proceedingChapter

10 Citations (Scopus)

Abstract

The extreme simplicity of Caenorhabditis elegans makes it an ideal system to study the basic principles of cadherin function at the level of single cells within the physiologically relevant context of a developing animal. The genetic tractability of C. elegans also means that components of cadherin complexes can be identified through genetic modifier screens, allowing a comprehensive in vivo characterization of the macromolecular assemblies involved in cadherin function during tissue formation and maintenance in C. elegans. This work shows that a single cadherin system, the classical cadherin–catenin complex, is essential for diverse morphogenetic events during embryogenesis through its interactions with a range of mostly conserved proteins that act to modulate its function. The role of other members of the cadherin family in C. elegans, including members of the Fat-like, Flamingo/CELSR and calsyntenin families is less well characterized, but they have clear roles in neuronal development and function.
Original languageEnglish
Title of host publicationThe Molecular biology of Cadherins
EditorsFrans van Roy
PublisherElsevier Science
Pages239-262
Number of pages24
ISBN (Print)978-0-12-394311-8
DOIs
Publication statusPublished - 2013

Publication series

Name Progress in Molecular Biology and Translational Science
PublisherElsevier
Volume116

Keywords

  • C. elegans
  • morphogenesis
  • α-Catenin
  • β-Catenin
  • cadherin
  • neuronal migration
  • epidermal adhesion
  • gastrulation
  • ingression

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  • Cite this

    Hardin, J., Lynch, A., Loveless, T., & Pettitt, J. (2013). Cadherins and their partners in the nematode worm Caenorhabditis elegans. In F. van Roy (Ed.), The Molecular biology of Cadherins (pp. 239-262). ( Progress in Molecular Biology and Translational Science; Vol. 116). Elsevier Science . https://doi.org/10.1016/B978-0-12-394311-8.00011-X