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Molecular chaperones in protein folding and proteostasis

Author

Listed:
  • F. Ulrich Hartl

    (Max Planck Institute of Biochemistry)

  • Andreas Bracher

    (Max Planck Institute of Biochemistry)

  • Manajit Hayer-Hartl

    (Max Planck Institute of Biochemistry)

Abstract

Most proteins must fold into defined three-dimensional structures to gain functional activity. But in the cellular environment, newly synthesized proteins are at great risk of aberrant folding and aggregation, potentially forming toxic species. To avoid these dangers, cells invest in a complex network of molecular chaperones, which use ingenious mechanisms to prevent aggregation and promote efficient folding. Because protein molecules are highly dynamic, constant chaperone surveillance is required to ensure protein homeostasis (proteostasis). Recent advances suggest that an age-related decline in proteostasis capacity allows the manifestation of various protein-aggregation diseases, including Alzheimer's disease and Parkinson's disease. Interventions in these and numerous other pathological states may spring from a detailed understanding of the pathways underlying proteome maintenance.

Suggested Citation

  • F. Ulrich Hartl & Andreas Bracher & Manajit Hayer-Hartl, 2011. "Molecular chaperones in protein folding and proteostasis," Nature, Nature, vol. 475(7356), pages 324-332, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7356:d:10.1038_nature10317
    DOI: 10.1038/nature10317
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    Citations

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    Cited by:

    1. Franke, R., 2016. "CHIMERA: Top-down model for hierarchical, overlapping and directed cluster structures in directed and weighted complex networks," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 461(C), pages 384-408.
    2. Il-Soo Park & Seongchan Kim & Yeajee Yim & Ginam Park & Jinahn Choi & Cheolhee Won & Dal-Hee Min, 2022. "Multifunctional synthetic nano-chaperone for peptide folding and intracellular delivery," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Verena Kohler & Andreas Kohler & Lisa Larsson Berglund & Xinxin Hao & Sarah Gersing & Axel Imhof & Thomas Nyström & Johanna L. Höög & Martin Ott & Claes Andréasson & Sabrina Büttner, 2024. "Nuclear Hsp104 safeguards the dormant translation machinery during quiescence," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    4. Guosheng Chen & Linjing Tong & Siming Huang & Shuyao Huang & Fang Zhu & Gangfeng Ouyang, 2022. "Hydrogen-bonded organic framework biomimetic entrapment allowing non-native biocatalytic activity in enzyme," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    5. Maru Jaime-Garza & Carlos A. Nowotny & Daniel Coutandin & Feng Wang & Mariano Tabios & David A. Agard, 2023. "Hsp90 provides a platform for kinase dephosphorylation by PP5," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    6. Erik B Nordquist & Charles A English & Eugenia M Clerico & Woody Sherman & Lila M Gierasch & Jianhan Chen, 2021. "Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones," PLOS Computational Biology, Public Library of Science, vol. 17(11), pages 1-24, November.
    7. Krishna B. S. Swamy & Hsin-Yi Lee & Carmina Ladra & Chien-Fu Jeff Liu & Jung-Chi Chao & Yi-Yun Chen & Jun-Yi Leu, 2022. "Proteotoxicity caused by perturbed protein complexes underlies hybrid incompatibility in yeast," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    8. 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.
    9. Jaime Carrasco & Rosa Antón & Alejandro Valbuena & David Pantoja-Uceda & Mayur Mukhi & Rubén Hervás & Douglas V. Laurents & María Gasset & Javier Oroz, 2023. "Metamorphism in TDP-43 prion-like domain determines chaperone recognition," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    10. Ke Shui & Chenwei Wang & Xuedi Zhang & Shanshan Ma & Qinyu Li & Wanshan Ning & Weizhi Zhang & Miaomiao Chen & Di Peng & Hui Hu & Zheng Fang & Anyuan Guo & Guanjun Gao & Mingliang Ye & Luoying Zhang & , 2023. "Small-sample learning reveals propionylation in determining global protein homeostasis," Nature Communications, Nature, vol. 14(1), pages 1-23, December.
    11. Hyunju Cho & Yumeng Liu & SangYoon Chung & Sowmya Chandrasekar & Shimon Weiss & Shu-ou Shan, 2024. "Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    12. Dahai Yu & Lin Lv & Li Fang & Bo Zhang & Junnan Wang & Ge Zhan & Lei Zhao & Xin Zhao & Baoxin Li, 2017. "Inhibitory effects and mechanism of dihydroberberine on hERG channels expressed in HEK293 cells," PLOS ONE, Public Library of Science, vol. 12(8), pages 1-19, August.

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