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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Bacterial Protein Maturation01:26

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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The Spindle Assembly Checkpoint02:19

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The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
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Related Experiment Video

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Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
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The HSP90 chaperone machinery.

Florian H Schopf1, Maximilian M Biebl1, Johannes Buchner1

  • 1Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, Garching, Germany.

Nature Reviews. Molecular Cell Biology
|April 22, 2017
PubMed
Summary

Heat shock protein 90 (HSP90) is crucial for cellular proteostasis and protein folding. Understanding HSP90 client interactions offers new therapeutic targets for cancer and neurodegenerative diseases.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Heat shock protein 90 (HSP90) is a vital chaperone machinery regulating proteostasis in eukaryotic cells.
  • HSP90 influences diverse cellular processes, including DNA repair, immune response, and neurodegenerative disease, due to its numerous protein substrates.
  • Co-chaperones modulate HSP90's ATPase activity, impacting client protein processing.

Purpose of the Study:

  • To elucidate the interactions between HSP90, its co-chaperones, and client proteins.
  • To highlight the therapeutic potential of targeting HSP90 for various diseases.

Main Methods:

  • Investigating the molecular mechanisms of HSP90-client interactions.
  • Analyzing the role of co-chaperones in HSP90 conformational changes.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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  • Defining the network of HSP90 and its associated proteins.

    • Main Results:

    • Detailed mapping of client protein interactions with the HSP90 machinery.
    • Identification of key co-chaperones regulating HSP90 function.
    • Established the link between HSP90 regulation and cellular processes.

    Conclusions:

    • HSP90's extensive role in cellular regulation makes it a significant drug target.
    • Targeting HSP90 offers therapeutic strategies for cancer and protein misfolding diseases.