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Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase

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  • Min Deng

    (Yale University)

  • Mark Hochstrasser

    (Yale University)

Abstract

The ubiquitin system targets many cellular proteins. Doa10 (also known as Ssm4), a yeast transmembrane ubiquitin ligase (E3), resides in the endoplasmic reticulum (ER), but it attaches ubiquitin to soluble proteins that concentrate in the nucleus. A central question is how nuclear substrates gain access to an enzyme in the ER. Here we show that Doa10 reaches the inner nuclear membrane. A subcomplex of nuclear pore subunits is important for this transport. Notably, another ER transmembrane E3, Hrd1 (also known as Der3), cannot localize efficiently to the inner nuclear membrane. Tethering Doa10 at the cell periphery inhibits degradation of soluble nuclear substrates but not cytoplasmic ones. If Doa10 is released from these peripheral sites, localization of Doa10 to the nuclear envelope and degradation of its nuclear substrates are restored in parallel. Thus, localization of Doa10 to the inner nuclear membrane is necessary for nuclear substrate degradation. These data indicate that different membrane ubiquitin ligases are spatially sorted within the ER–nuclear envelope membrane system and that this differential localization contributes to their specificity.

Suggested Citation

  • Min Deng & Mark Hochstrasser, 2006. "Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase," Nature, Nature, vol. 443(7113), pages 827-831, October.
    • Handle: RePEc:nat:nature:v:443:y:2006:i:7113:d:10.1038_nature05170
    DOI: 10.1038/nature05170
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    Cited by:

    1. Kevin Wu & Samuel Itskanov & Diane L. Lynch & Yuanyuan Chen & Aasha Turner & James C. Gumbart & Eunyong Park, 2024. "Substrate recognition mechanism of the endoplasmic reticulum-associated ubiquitin ligase Doa10," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Bayan Mashahreh & Shir Armony & Kristoffer Enøe Johansson & Alon Chappleboim & Nir Friedman & Richard G. Gardner & Rasmus Hartmann-Petersen & Kresten Lindorff-Larsen & Tommer Ravid, 2022. "Conserved degronome features governing quality control associated proteolysis," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. J. Josephine Botsch & Roswitha Junker & Michèle Sorgenfrei & Patricia P. Ogger & Luca Stier & Susanne Gronau & Peter J. Murray & Markus A. Seeger & Brenda A. Schulman & Bastian Bräuning, 2024. "Doa10/MARCH6 architecture interconnects E3 ligase activity with lipid-binding transmembrane channel to regulate SQLE," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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