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CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70

Author

Listed:
  • Shu-Bing Qian

    (Carolina Cardiovascular Biology Center)

  • Holly McDonough

    (Carolina Cardiovascular Biology Center)

  • Frank Boellmann

    (Carolina Cardiovascular Biology Center)

  • Douglas M. Cyr

    (University of North Carolina)

  • Cam Patterson

    (Carolina Cardiovascular Biology Center)

Abstract

CHIP — a co-chaperone/ubiquitin ligase — not only targets chaperone substrates for degradation, but mediates Hsp70 turnover after misfolded substrates have been depleted. The sequential catalysis of the CHIP-associated chaperone adaptor and its bound substrate provides a mechanism for maintaining homeostasis by tuning chaperone levels appropriately to reflect the status of protein folding within the cytoplasm.

Suggested Citation

  • Shu-Bing Qian & Holly McDonough & Frank Boellmann & Douglas M. Cyr & Cam Patterson, 2006. "CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70," Nature, Nature, vol. 440(7083), pages 551-555, March.
    • Handle: RePEc:nat:nature:v:440:y:2006:i:7083:d:10.1038_nature04600
    DOI: 10.1038/nature04600
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    Cited by:

    1. Alex J. Callahan & Satish Gandhesiri & Tara L. Travaline & Rahi M. Reja & Lia Lozano Salazar & Stephanie Hanna & Yen-Chun Lee & Kunhua Li & Olena S. Tokareva & Jean-Marie Swiecicki & Andrei Loas & Gre, 2024. "Mirror-image ligand discovery enabled by single-shot fast-flow synthesis of D-proteins," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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