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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.

Cell | Jul 28, 2006

http://www.ncbi.nlm.nih.gov/pubmed/16873066

Many misfolded endoplasmic reticulum (ER) proteins are eliminated by ERAD, a process in which substrates are polyubiquitylated and moved into the cytosol for proteasomal degradation. We have identified in S. cerevisiae distinct ubiquitin-ligase complexes that define different ERAD pathways. Proteins with misfolded ER-luminal domains use the ERAD-L pathway, in which the Hrd1p/Hrd3p ligase forms a near stoichiometric membrane core complex by binding to Der1p via the linker protein Usa1p. This core complex associates through Hrd3p with Yos9p, a substrate recognition protein in the ER lumen. Substrates with misfolded intramembrane domains define a pathway (ERAD-M) that differs from ERAD-L by being independent of Usa1p and Der1p. Membrane proteins with misfolded cytosolic domains use the ERAD-C pathway and are directly targeted to the Doa10p ubiquitin ligase. All three pathways converge at the Cdc48p ATPase complex. These results lead to a unifying concept for ERAD that may also apply to mammalian cells.

Pubmed ID: 16873066 RIS Download

Mesh terms: Adenosine Triphosphatases | Carrier Proteins | Cell Cycle Proteins | Endoplasmic Reticulum | Fungal Proteins | Ligases | Membrane Glycoproteins | Membrane Proteins | Models, Biological | Protein Folding | Protein Structure, Tertiary | Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Substrate Specificity | Ubiquitin | Ubiquitin-Protein Ligases

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM052586

BioGRID (Data, Interactions)

GO (Data, Gene Annotation)

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