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Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.

FEBS letters | May 6, 2011

Misfolded, luminal endoplasmic reticulum (ER) proteins must be recognized before being degraded by a process called ERAD-L. Using site-specific photocrosslinking in Saccharomyces cerevisiae, we tested luminal interactions of a glycosylated ERAD-L substrate with potential recognition components. Major interactions were observed with Hrd3p. These are independent of the glycan and of other ERAD components, and can occur throughout the length of the unfolded substrate. The lectin Yos9p only interacts with a polypeptide segment distant from the degradation signal. Hrd3p may thus be the first substrate-recognizing component. Der1p appears to have a role in a pathway that is parallel to that involving Hrd3p.

Pubmed ID: 21486563 RIS Download

Mesh terms: Binding Sites | Carrier Proteins | Cross-Linking Reagents | Endoplasmic Reticulum | Immunoblotting | Immunoprecipitation | Membrane Glycoproteins | Membrane Proteins | Multiprotein Complexes | Protein Binding | Protein Folding | Protein Transport | Recombinant Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Substrate Specificity | Ubiquitin-Protein Ligases | Ultraviolet Rays

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Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM052586
  • Agency: NIGMS NIH HHS, Id: GM052586
  • Agency: Howard Hughes Medical Institute, Id:

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