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Showing 1–3 of 3 results
Advanced filters: Author: Samuel A. Maiwald Clear advanced filters

  • Using biochemistry, chemical biology, and cryo-EM, Maiwald et al. elucidate how TRIP12 forms K29 linkages and K29/K48-linked branched ubiquitin chains, revealing a mechanism for polyubiquitylation shared by some HECT E3s.

    • Samuel A. Maiwald
    • Laura A. Schneider
    • Brenda A. Schulman
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1766-1775

  • Kelch-domain KLHDCX E3 ligases bind substrate C-terminal glycines. This study reveals substrate selectivity by E3s with similar structures; C-degrons are perceived by a “C-terminus anchor motif”, whose display on different Kelch propeller blades along with distal interactions establish specificity.

    • Daniel C. Scott
    • Sagar Chittori
    • Brenda A. Schulman
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17

  • The authors define a NEDD8-activated cullin-RING E3 poly-ubiquitylation mechanism using chemistry, cryo-EM and rapid kinetics. Near-perfect catalytic efficiency is achieved by an E2 ‘synergy loop’ connecting to the E3, donor and acceptor ubiquitins.

    • Joanna Liwocha
    • Jerry Li
    • Gary Kleiger
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 378-389