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Ubiquitylation

Choosing to be single

Nature Reviews Molecular Cell Biology volume 3, page 314 (2002)Cite this article

How does the cellular machinery decide whether proteins should be monoubiquitylated rather than polyubiquitylated? This decision is crucial because being tagged with a single copy of ubiquitin determines whether proteins become involved in controlling endocytosis rather than being targeted for destruction by the proteasome.

Now, three reports shed light on this process by showing that ubiquitin recognition and monoubiquitylation depend on the ubiquitin-interacting motif (UIM), which is found in many groups of proteins, including endocytic proteins and ubiquitin ligases.

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References

ORIGINAL RESEARCH PAPERS

  1. Polo, S. et al. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451–455 (2002)

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  2. Shih, S. C. et al. Epsins and Vps27/Hrs contain ubiquitin-binding domains that function in receptor endocytosis and downregulation. Nature Cell Biol. 4, 389–393 (2002)

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  3. Raiborg, C. et al. Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nature Cell Biol. 4, 394–398 (2002)

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FURTHER READING

  1. Riezman, H. The ubiquitin connection Nature 416, 381–383 (2002)

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Authors
  1. Simon Frantz
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Frantz, S. Choosing to be single. Nat Rev Mol Cell Biol 3, 314 (2002). https://doi.org/10.1038/nrm823

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  • DOI: https://doi.org/10.1038/nrm823

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