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Targeting of gp78 for ubiquitin-mediated proteasomal degradation by Hrd1: Cross-talk between E3s in the endoplasmic reticulum

  1. Author:
    Shmueli, A.
    Tsai, Y. C.
    Yang, M.
    Braun, M. A.
    Weissman, A. M.

  2. Author Address

    Shmueli, Ayelet, Tsai, Yien Che, Yang, Mei, Braun, Mary A.; Weissman, Allan M.] NCI, Lab Prot Dynam & Signaling, Ctr Canc Res, Frederick, MD 21702 USA.
    1. Year: 2009
  2. Journal: Biochemical and Biophysical Research Communications
    1. 390
    2. 3
    3. Pages: 758-762
  4. Type of Article: Article
  5. ISSN: 0006-291X
  1. Abstract:

    There are an increasing number of ubiquitin ligases (E3s) implicated in endoplasmic Feticulum (ER)-associated degradation (ERAD) in mammals. The two for which the greatest amount of information exists are the RING finger proteins gp78 and Hrd1, which are the structural orthologs of the yeast ERAD E3 Hrd1p. We now report that Hrd1, also known as synoviolin, targets gp78 for proteasomal degradation independent of the ubiquitin ligase activity of gp78, without evidence of a reciprocal effect. This degradation is observed in mouse embryonic fibroblasts lacking Hrd1, as well as with acute manipulation of Hrd1. The significance of this is underscored by the diminished level of a gp78-specific substrate, Insig-1, when Hrd1 expression is decreased and gp78 levels are consequently increased. These finding demonstrate a previously unappreciated level of complexity of the ubiquitin system in

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  2. DOI: 10.1016/j.bbrc.2009.10.045
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