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Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex

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  • David Reverter

    (Sloan-Kettering Institute)

  • Christopher D. Lima

    (Sloan-Kettering Institute)

Abstract

SUMO-1 (for small ubiquitin-related modifier) belongs to the ubiquitin (Ub) and ubiquitin-like (Ubl) protein family. SUMO conjugation occurs on specific lysine residues within protein targets, regulating pathways involved in differentiation, apoptosis, the cell cycle and responses to stress by altering protein function through changes in activity or cellular localization or by protecting substrates from ubiquitination1,2. Ub/Ubl conjugation occurs in sequential steps and requires the concerted action of E2 conjugating proteins and E3 ligases1,2. In addition to being a SUMO E3, the nucleoporin Nup358/RanBP2 localizes SUMO-conjugated RanGAP1 to the cytoplasmic face of the nuclear pore complex by means of interactions in a complex that also includes Ubc9, the SUMO E2 conjugating protein3,4,5,6. Here we describe the 3.0-Å crystal structure of a four-protein complex of Ubc9, a Nup358/RanBP2 E3 ligase domain (IR1-M) and SUMO-1 conjugated to the carboxy-terminal domain of RanGAP1. Structural insights, combined with biochemical and kinetic data obtained with additional substrates, support a model in which Nup358/RanBP2 acts as an E3 by binding both SUMO and Ubc9 to position the SUMO–E2-thioester in an optimal orientation to enhance conjugation.

Suggested Citation

  • David Reverter & Christopher D. Lima, 2005. "Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex," Nature, Nature, vol. 435(7042), pages 687-692, June.
    • Handle: RePEc:nat:nature:v:435:y:2005:i:7042:d:10.1038_nature03588
    DOI: 10.1038/nature03588
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    Cited by:

    1. Melda Tozluoğlu & Ezgi Karaca & Ruth Nussinov & Türkan Haliloğlu, 2010. "A Mechanistic View of the Role of E3 in Sumoylation," PLOS Computational Biology, Public Library of Science, vol. 6(8), pages 1-10, August.
    2. Nathalia Varejão & Jara Lascorz & Joan Codina-Fabra & Gemma Bellí & Helena Borràs-Gas & Jordi Torres-Rosell & David Reverter, 2021. "Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs," Nature Communications, Nature, vol. 12(1), pages 1-14, December.

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