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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
Published on: October 17, 2014
An adhesion-independent, aPKC-dependent function for cadherins in morphogenetic movements
Karla Seifert1, Hady Ibrahim, Torben Stodtmeister
1Center for Molecular Medicine Cologne, University of Cologne, 50923 Cologne, Germany.
Journal of Cell Science
|June 25, 2009
Summary
Cadherins have a dual role in cell movement: adhesion and a novel signaling pathway involving atypical PKC (aPKC) and Rac. This discovery connects cadherins to cell polarity and impacts understanding of development and cancer progression.
Area of Science:
- Cell Biology
- Developmental Biology
- Cancer Research
Background:
- Cadherin shedding is implicated in cell migration during development and cancer progression.
- The precise in vivo functions of cadherin extracellular domains beyond adhesion are not fully understood.
Purpose of the Study:
- To investigate the biological function of the extracellular cadherin domain (CEC1-5) independently of shedding.
- To elucidate the novel roles of cadherins in convergent extension (CE) movements and cell polarity.
Main Methods:
- Utilized Xenopus model system to study in vivo biological functions.
- Examined the effects of CEC1-5 on gastrulation and CE movements.
- Investigated rescue mechanisms involving membrane-anchored domains, atypical PKC (aPKC), and Rac.
Main Results:
- The extracellular cadherin domain (CEC1-5) interfered with CE movements during Xenopus gastrulation.
- Gastrulation defects were rescued by a cadherin cytoplasmic domain, aPKC, or active Rac, indicating modulation of a signaling pathway.
- Cadherins interact with aPKC, and the extracellular domain alters this interaction and aPKC phosphorylation, linking cadherins to polarity.
Conclusions:
- Cadherins possess a dual role in CE movements: adhesion and an adhesion-independent function involving aPKC and Rac, directly connecting them to cell polarity.
- Cadherin shedding may regulate cancer cell migration and invasion by modulating polarity protein activity.
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