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Structural basis for dimerization quality control

Author

Listed:
  • Elijah L. Mena

    (University of California at Berkeley
    Harvard Medical School)

  • Predrag Jevtić

    (University of California at Berkeley
    University of California at Berkeley)

  • Basil J. Greber

    (University of California at Berkeley
    Lawrence Berkeley National Laboratory)

  • Christine L. Gee

    (University of California at Berkeley
    University of California at Berkeley)

  • Brandon G. Lew

    (University of California at Berkeley
    University of California at Berkeley)

  • David Akopian

    (University of California at Berkeley)

  • Eva Nogales

    (University of California at Berkeley
    University of California at Berkeley
    University of California at Berkeley
    Lawrence Berkeley National Laboratory)

  • John Kuriyan

    (University of California at Berkeley
    University of California at Berkeley
    University of California at Berkeley
    Lawrence Berkeley National Laboratory)

  • Michael Rape

    (University of California at Berkeley
    University of California at Berkeley
    University of California at Berkeley)

Abstract

Most quality control pathways target misfolded proteins to prevent toxic aggregation and neurodegeneration1. Dimerization quality control further improves proteostasis by eliminating complexes of aberrant composition2, but how it detects incorrect subunits remains unknown. Here we provide structural insight into target selection by SCF–FBXL17, a dimerization-quality-control E3 ligase that ubiquitylates and helps to degrade inactive heterodimers of BTB proteins while sparing functional homodimers. We find that SCF–FBXL17 disrupts aberrant BTB dimers that fail to stabilize an intermolecular β-sheet around a highly divergent β-strand of the BTB domain. Complex dissociation allows SCF–FBXL17 to wrap around a single BTB domain, resulting in robust ubiquitylation. SCF–FBXL17 therefore probes both shape and complementarity of BTB domains, a mechanism that is well suited to establish quality control of complex composition for recurrent interaction modules.

Suggested Citation

  • Elijah L. Mena & Predrag Jevtić & Basil J. Greber & Christine L. Gee & Brandon G. Lew & David Akopian & Eva Nogales & John Kuriyan & Michael Rape, 2020. "Structural basis for dimerization quality control," Nature, Nature, vol. 586(7829), pages 452-456, October.
    • Handle: RePEc:nat:nature:v:586:y:2020:i:7829:d:10.1038_s41586-020-2636-7
    DOI: 10.1038/s41586-020-2636-7
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    Cited by:

    1. Maximilian Seidel & Anja Becker & Filipa Pereira & Jonathan J. M. Landry & Nayara Trevisan Doimo Azevedo & Claudia M. Fusco & Eva Kaindl & Natalie Romanov & Janina Baumbach & Julian D. Langer & Erin M, 2022. "Co-translational assembly orchestrates competing biogenesis pathways," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Weize Wang & Ling Liang & Zonglin Dai & Peng Zuo & Shang Yu & Yishuo Lu & Dian Ding & Hongyi Chen & Hui Shan & Yan Jin & Youdong Mao & Yuxin Yin, 2024. "A conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3KLHL22," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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