The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring.

@article{Willison2018TheSA,
  title={The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring.},
  author={Keith R. Willison},
  journal={The Biochemical journal},
  year={2018},
  volume={475 19},
  pages={
          3009-3034
        }
}
  • K. Willison
  • Published 5 October 2018
  • Biology
  • The Biochemical journal
Actin is folded to its native state in eukaryotic cytosol by the sequential allosteric mechanism of the chaperonin-containing TCP-1 (CCT). The CCT machine is a double-ring ATPase built from eight related subunits, CCT1-CCT8. Non-native actin interacts with specific subunits and is annealed slowly through sequential binding and hydrolysis of ATP around and across the ring system. CCT releases a folded but soft ATP-G-actin monomer which is trapped 80 kJ/mol uphill on the folding energy surface by… 
The substrate specificity of eukaryotic cytosolic chaperonin CCT
  • K. Willison
  • Biology
    Philosophical Transactions of the Royal Society B: Biological Sciences
  • 2018
TLDR
A toy model in which cytoskeletal protein biogenesis and folding flux through CCT couples cell growth and size control to time dependent cell cycle mechanisms is presented.
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Single-molecule nanopore sensing of actin dynamics and drug binding†
TLDR
The state of actin is determined at the macromolecular level (filamentous or globular) and in its monomeric form bound to inhibitors and the promise of nanopore sensing is demonstrated for in-depth understanding of protein folding landscapes and for drug discovery.
The Challenging Riddle about the Janus-Type Role of Hsp60 and Related Extracellular Vesicles and miRNAs in Carcinogenesis and the Promises of Its Solution
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The possible applications of the Hsp60 involvement in carcinogenesis not only in diagnosis, but also in the development of specific anti-cancer therapies centered on the use of the chaperonin as therapeutic target or agent and depending on its role, pro- or anti-tumor.
The landscape of molecular chaperones across human tissues reveals a layered architecture of core and variable chaperones
The sensitivity of the protein-folding environment to chaperone disruption can be highly tissue-specific. Yet, the organization of the chaperone system across physiological human tissues has received
Muscle Histopathological Abnormalities in a Patient With a CCT5 Mutation Predicted to Affect the Apical Domain of the Chaperonin Subunit
Recognition of diseases associated with mutations of the chaperone system genes, e.g., chaperonopathies, is on the rise. Hereditary and clinical aspects are established, but the impact of the
Molecular mechanisms in chaperonopathies: clues to understanding the histopathological abnormalities and developing novel therapies
TLDR
The data provide insights into what may happen when CCT5 and HSPA9 malfunction in patients, e.g. accumulation of cytotoxic protein aggregates with tissue destruction; or for Hsp60 with aberrant PTM, degradation and/or secretion of the chaperonin with mitochondrial damage.
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TLDR
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