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Working on a chain: E3s ganging up for ubiquitylation

  1. Author:
    Metzger, M. B.
    Weissman, A. M.

  2. Author Address

    [Metzger, Meredith B.; Weissman, Allan M.] NCI, Lab Prot Dynam & Signaling, Ctr Canc Res, NIH, Frederick, MD 21702 USA.;Metzger, MB, NCI, Lab Prot Dynam & Signaling, Ctr Canc Res, NIH, Frederick, MD 21702 USA.;amw@nih.gov
    1. Year: 2010
    2. Date: Dec
  2. Journal: Nature Cell Biology
    1. 12
    2. 12
    3. Pages: 1124-1126
  4. Type of Article: Editorial Material
  5. ISSN: 1465-7392
  1. Abstract:

    Substrate specificity in ubiquitylation is conferred by ubiquitin ligases (E3s). Now, several ways that E3s can interact to mediate ubiquitylation are illustrated for Ubr1 (a RING finger E3) and Ufd4 (a HECT domain E3), in Saccharomyces cerevisiae. These interactions and the related concept of E4 activity are discussed.

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External Sources

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  2. DOI: 10.1038/ncb1210-1124
  3. View record in Web of Science®
  4. WOS: 000284831200002

Library Notes

  1. Fiscal Year: FY2010-2011
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