Chaperones

Chaperones are proteins that assist in protein folding and multi-protein complex assembly co-translationally or post-translationally. Generally, a single chaperone has multiple client proteins. An example of chaperones are heat shock proteins, which are upregulated in response to heat – a risk factor for protein misfolding and aggregation.

Latest Research and Reviews

  • Research | | open

    SecB homologs can be associated with stress-responsive type II toxin–antitoxin (TA) systems and form tripartite toxin-antitoxin-chaperone systems (TAC). Here the authors provide structural insights into TACs by presenting the crystal structure of the M. tuberculosis TA-associated SecB chaperone in complex with the C-terminal ChAD (chaperone addiction) extension of the antitoxin HigA1.

    • Valérie Guillet
    • , Patricia Bordes
    • , Cécile Bon
    • , Julien Marcoux
    • , Virginie Gervais
    • , Ambre Julie Sala
    • , Suzana Dos Reis
    • , Nawel Slama
    • , Israel Mares-Mejía
    • , Anne-Marie Cirinesi
    • , Laurent Maveyraud
    • , Pierre Genevaux
    •  & Lionel Mourey
  • Research |

    A computationally designed molecular chaperone inhibits the interaction of normal prions with abnormal isoforms associated with transmissible spongiform encephalopathy, prolongs survival in infected mice and limits symptoms in infected macaques.

    • Keiichi Yamaguchi
    • , Yuji O. Kamatari
    • , Fumiko Ono
    • , Hiroaki Shibata
    • , Takayuki Fuse
    • , Abdelazim Elsayed Elhelaly
    • , Mayuko Fukuoka
    • , Tsutomu Kimura
    • , Junji Hosokawa-Muto
    • , Takeshi Ishikawa
    • , Minoru Tobiume
    • , Yoshinori Takeuchi
    • , Yutaka Matsuyama
    • , Daisuke Ishibashi
    • , Noriyuki Nishida
    •  & Kazuo Kuwata
  • Reviews |

    Misfolded proteins have a high propensity to form potentially toxic aggregates. Cells employ a complex network of processes, involving chaperones and proteolytic machineries that ensure proper protein folding and remodel or degrade misfolded species and aggregates. This proteostasis network declines with age, which can be linked to human degenerative diseases.

    • Mark S. Hipp
    • , Prasad Kasturi
    •  & F. Ulrich Hartl
  • Research | | open

    The role of mesencephalic astrocyte-derived neurotrophic factor (MANF) in maintenance of protein folding homeostasis inside the ER has remained unclear. Here the authors determine the structure of the complex between MANF and the ER-localized chaperone BiP and provide evidence that MANF serves as an anti-nucleotide exchange factor for BiP.

    • Yahui Yan
    • , Claudia Rato
    • , Lukas Rohland
    • , Steffen Preissler
    •  & David Ron
  • Research | | open

    BAG3 is a Hsp70 co-chaperone that is highly expressed in muscles. Here the authors show that several myofibrillar myopathy causing BAG3 mutations are not impaired in Hsp70 binding, but rather impair the ADP-ATP exchange step of the Hsp70 cycle, causing the aggregation of BAG3, Hsp70 and Hsp70 clients and leading to a collapse of protein homeostasis.

    • Melanie Meister-Broekema
    • , Rebecca Freilich
    • , Chandhuru Jagadeesan
    • , Jennifer N. Rauch
    • , Rocio Bengoechea
    • , William W. Motley
    • , E. F. Elsiena Kuiper
    • , Melania Minoia
    • , Gabriel V. Furtado
    • , Maria A. W. H. van Waarde
    • , Shawn J. Bird
    • , Adriana Rebelo
    • , Stephan Zuchner
    • , Peter Pytel
    • , Steven S. Scherer
    • , Federica F. Morelli
    • , Serena Carra
    • , Conrad C. Weihl
    • , Steven Bergink
    • , Jason E. Gestwicki
    •  & Harm H. Kampinga
  • Research |

    A combination of proteomics and structural analyses reveals the assembly mechanism of transcription factor TFIID in human cells and identifies the chaperonin CCT as a checkpoint in the process.

    • Simona V. Antonova
    • , Matthias Haffke
    • , Eleonora Corradini
    • , Mykolas Mikuciunas
    • , Teck Y. Low
    • , Luca Signor
    • , Robert M. van Es
    • , Kapil Gupta
    • , Elisabeth Scheer
    • , Harmjan R. Vos
    • , László Tora
    • , Albert J. R. Heck
    • , H. T. Marc Timmers
    •  & Imre Berger

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