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Showing 1–8 of 8 results
Advanced filters: Author: Gary Kleiger Clear advanced filters

  • Conjugation of ubiquitin chains onto proteins is an important post-translational modification that regulates the stability, localization and activity of substrate proteins. A series of enzymes known as E1, E2 and E3 mediate assembly of ubiquitin chains but the pathway remains unclear. Theoretical and experimental methodologies are now introduced to study the formation of ubiquitin chains at millisecond time resolution, demonstrating that substrate polyubiquitylation proceeds sequentially.

    • Nathan W. Pierce
    • Gary Kleiger
    • Raymond J. Deshaies
    Research
    Nature
    Volume: 462, P: 615-619

  • 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

  • Using synthetic ubiquitins with non-natural acceptor site, the authors revealed that the length of lysine side chain in acceptor ubiquitins affects ubiquitin chain linkage specificity with native lysine as the preferred geometry.

    • Joanna Liwocha
    • David T. Krist
    • Brenda A. Schulman
    Research
    Nature Chemical Biology
    Volume: 17, P: 272-279

  • 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

  • Cryo-electron microscopy of neddylated SCF-family ligases interacting with the RBR-type E3 ligase ARIH1 reveals the steps through which E3–E3 super-assemblies ubiquitylate a diverse set of substrates presented on F-box proteins.

    • Daniel Horn-Ghetko
    • David T. Krist
    • Brenda A. Schulman
    ResearchOpen Access
    Nature
    Volume: 590, P: 671-676

  • The AAA+ protein p97 and its UBA-UBX cofactors are thought to promote degradation by separating ubiquitinated proteins from membranes or protein complexes. UBA-UBX proteins can interact with cullin-RING ubiquitin ligases, and UBXD7 is now seen to specifically bind NEDD8 on active, neddylated cullins, promoting degradation of a Cul3 substrate.

    • Willem den Besten
    • Rati Verma
    • Raymond J Deshaies
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 511-516

  • In the ubiquitin-proteasome system, E2 enzymes such as Cdc34A mediate the transfer of ubiquitin to protein substrates, which are thus marked for proteasomal degradation or other fates. New structural data reveal that the small-molecule inhibitor CC0651 impairs Cdc34A activity by stabilizing the normally transient Cdc34A–ubiquitin complex.

    • Hao Huang
    • Derek F Ceccarelli
    • Frank Sicheri
    Research
    Nature Chemical Biology
    Volume: 10, P: 156-163