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Protein degradation

Chain gang

Nature Reviews Molecular Cell Biology volume 10, page 370 (2009)Cite this article

“...all non-Lys63-linked polyubiquitin chains mediate proteasomal degradation…”

Using mass spectrometry (MS) in yeast, the authors found high levels of unconventional polyubiquitin chains (especially those linked to Lys11) on a broad range of substrates. The levels of these chains, as well as of Lys48-linked chains, increased when the 26S proteasome was chemically or genetically inhibited, whereas the level of Lys63-linked chains was not affected (which was to be expected, given the well-known non-proteolytic functions of Lys63-linked chains). These results suggest that all non-Lys63-linked polyubiquitin chains mediate proteasomal degradation.

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References

ORIGINAL RESEARCH PAPER

  1. Xu, P. et al. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137, 133–145 (2009)

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FURTHER READING

  1. Ravid, T. & Hochstrasser, M. Diversity of degradation signals in the ubiquitin-proteasome system. Nature Rev. Mol. Cell Biol. 9, 679–689 (2008)

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  2. Vembar, S. S. & Brodsky, J. L. One step at a time: endoplasmic reticulum-associated degradation. Nature Rev. Mol. Cell Biol. 9, 944–957 (2008)

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Authors
  1. Francesca Cesari
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Cesari, F. Chain gang. Nat Rev Mol Cell Biol 10, 370 (2009). https://doi.org/10.1038/nrm2691

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