Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Research Highlight
  • Published:

Metastasis

Contract and move

Nature Reviews Molecular Cell Biology volume 7, pages 878–879 (2006)Cite this article

Using human cancer cell lines the authors compared the small interfering RNA (siRNA)-mediated depletion of the promigratory transmembrane receptor ENDO180 (also known as CD280) and two other endocytic receptors. ENDO180 is constitutively recruited into clathrin-coated pits on the cell surface, which are then internalized into intracellular endosomes. Only the depletion of ENDO180 induced tail-retraction defects, indicative of reduced Rho–ROCK–MLC2-mediated contractile forces. This phenotype was comparable to that observed when cells were treated with Rho or ROCK inhibitors, establishing ENDO180–Rho–ROCK–MLC2 as a functional pathway. Moreover, ENDO180 siRNA or a ROCK inhibitor reduced the phosphorylation of three other ROCK substrates, LIM kinase-1 and -2, and myosin phosphatase-1.

Isacke and colleagues also show that ENDO180 is required for the spatial activation of Rho–ROCK–MLC2. Using cell lines that stably express an ENDO180 mutant that cannot be internalized, the authors demonstrate that ROCK cannot be recruited to focal adhesions. This shows that intracellular ENDO180-containing endosomes are required to activate Rho–ROCK.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

References

ORIGINAL RESEARCH PAPER

  1. Sturge, J. et al. Endosomes generate localized Rho-ROCK-MLC2-based contractile signals via Endo180 to promote adhesion disassembly. J. Cell Biol. 175, 337–347 (2006)

    Article  CAS  Google Scholar 

FURTHER READING

  1. Curino, A. C. et al. Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy. J. Cell Biol. 169, 977–985 (2005)

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Associate Editor, Nature Reviews Cancer,

    Gemma Alderton

Authors
  1. Gemma Alderton
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Alderton, G. Contract and move. Nat Rev Mol Cell Biol 7, 878–879 (2006). https://doi.org/10.1038/nrm2077

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/nrm2077

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing