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Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5

  1. Author:
    Lee, S.
    Tsai, Y. C.
    Mattera, R.
    Smith, W. J.
    Kostelansky, M. S.
    Weissman, A. M.
    Bonifacino, J. S.
    Hurley, J. H.

  2. Author Address

    NIDDK, Mol Biol Lab, NIH, Bethesda, MD 20892 USA. NCI, Lab Prot Dynam & Signaling, NIH, Ft Detrick, MD 21702 USA. NICHHD, Cell Biol & Metab Branch, NIH, Bethesda, MD 20892 USA Hurley, JH, NIDDK, Mol Biol Lab, NIH, Bethesda, MD 20892 USA
    1. Year: 2006
    2. Date: MAR
  2. Journal: Nature Structural & Molecular Biology
    1. 13
    2. 3
    3. Pages: 264-271
  4. Type of Article: Article
  1. Abstract:

    Rabex-5 is an exchange factor for Rab5, a master regulator of endosomal trafficking. Rabex-5 binds monoubiquitin, undergoes covalent ubiquitination and contains an intrinsic ubiquitin ligase activity, all of which require an N-terminal A20 zinc finger followed immediately by a helix. The structure of the N-terminal portion of Rabex-5 bound to ubiquitin at 2.5-angstrom resolution shows that Rabex-5-ubiquitin interactions occur at two sites. The first site is a new type of ubiquitin-binding domain, an inverted ubiquitin-interacting motif, which binds with similar to 29-mu M affinity to the canonical IIe44 hydrophobic patch on ubiquitin. The second is a diaromatic patch on the A20 zinc finger, which binds with similar to 22-mu M affinity to a polar region centered on Asp58 of ubiquitin. The A20 zinc-finger diaromatic patch mediates ubiquitin-ligase activity by directly recruiting a ubiquitin-loaded ubiquitin-conjugating enzyme

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External Sources

  1. View record in Web of Science®
  2. WOS: 000235776900018

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