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Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation

Author

Listed:
  • Nadinath B. Nillegoda

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance)

  • Janine Kirstein

    (Leibniz-Institute for Molecular Pharmacology (FMP))

  • Anna Szlachcic

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance)

  • Mykhaylo Berynskyy

    (Heidelberg Institute for Theoretical Studies (HITS))

  • Antonia Stank

    (Heidelberg Institute for Theoretical Studies (HITS)
    Heidelberg Graduate School of Mathematical and Computational Methods for the Sciences, Heidelberg University)

  • Florian Stengel

    (Institute of Molecular Systems Biology, ETH Zurich)

  • Kristin Arnsburg

    (Leibniz-Institute for Molecular Pharmacology (FMP))

  • Xuechao Gao

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance)

  • Annika Scior

    (Leibniz-Institute for Molecular Pharmacology (FMP))

  • Ruedi Aebersold

    (Institute of Molecular Systems Biology, ETH Zurich
    Faculty of Science, University of Zurich)

  • D. Lys Guilbride

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance)

  • Rebecca C. Wade

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance
    Heidelberg Institute for Theoretical Studies (HITS)
    Interdisciplinary Center for Scientific Computing (IWR), Heidelberg University)

  • Richard I. Morimoto

    (Rice Institute for Biomedical Research, Northwestern University)

  • Matthias P. Mayer

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance)

  • Bernd Bukau

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance)

Abstract

An efficient protein disaggregation system uncovered in metazoan cells requires transient interactions between J-protein co-chaperones of classes A and B, which synergistically boost HSP70-dependent disaggregation activity, providing a flexible further level of regulation for metazoan protein quality control, with direct relevance to human diseases such as age-related neurodegeneration.

Suggested Citation

  • Nadinath B. Nillegoda & Janine Kirstein & Anna Szlachcic & Mykhaylo Berynskyy & Antonia Stank & Florian Stengel & Kristin Arnsburg & Xuechao Gao & Annika Scior & Ruedi Aebersold & D. Lys Guilbride & R, 2015. "Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation," Nature, Nature, vol. 524(7564), pages 247-251, August.
    • Handle: RePEc:nat:nature:v:524:y:2015:i:7564:d:10.1038_nature14884
    DOI: 10.1038/nature14884
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    Citations

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    Cited by:

    1. Eduardo Pinho Melo & Tasuku Konno & Ilaria Farace & Mosab Ali Awadelkareem & Lise R. Skov & Fernando Teodoro & Teresa P. Sancho & Adrienne W. Paton & James C. Paton & Matthew Fares & Pedro M. R. Paulo, 2022. "Stress-induced protein disaggregation in the endoplasmic reticulum catalysed by BiP," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Lorea Velasco-Carneros & Jorge Cuéllar & Leire Dublang & César Santiago & Jean-Didier Maréchal & Jaime Martín-Benito & Moisés Maestro & José Ángel Fernández-Higuero & Natalia Orozco & Fernando Moro & , 2023. "The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    3. Matthias M. Schneider & Saurabh Gautam & Therese W. Herling & Ewa Andrzejewska & Georg Krainer & Alyssa M. Miller & Victoria A. Trinkaus & Quentin A. E. Peter & Francesco Simone Ruggeri & Michele Vend, 2021. "The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    4. Sheng Chen & Anuradhika Puri & Braxton Bell & Joseph Fritsche & Hector H. Palacios & Maurie Balch & Macy L. Sprunger & Matthew K. Howard & Jeremy J. Ryan & Jessica N. Haines & Gary J. Patti & Albert A, 2024. "HTRA1 disaggregates α-synuclein amyloid fibrils and converts them into non-toxic and seeding incompetent species," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    5. Kristine F. R. Pobre-Piza & Melissa J. Mann & Ashley R. Flory & Linda M. Hendershot, 2022. "Mapping SP-C co-chaperone binding sites reveals molecular consequences of disease-causing mutations on protein maturation," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    6. Dezerae Cox & Ching-Seng Ang & Nadinath B. Nillegoda & Gavin E. Reid & Danny M. Hatters, 2022. "Hidden information on protein function in censuses of proteome foldedness," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    7. S. M. Ayala Mariscal & M. L. Pigazzini & Y. Richter & M. Özel & I. L. Grothaus & J. Protze & K. Ziege & M. Kulke & M. ElBediwi & J. V. Vermaas & L. Colombi Ciacchi & S. Köppen & F. Liu & J. Kirstein, 2022. "Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT," Nature Communications, Nature, vol. 13(1), pages 1-25, December.

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