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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

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.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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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Assays for the Degradation of Misfolded Proteins in Cells
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Published on: August 28, 2016

Presenilin mutants subvert chaperone function.

M J Gething

    Nature Cell Biology
    |February 3, 2000
    PubMed
    Summary
    This summary is machine-generated.

    Mutant presenilin proteins worsen Alzheimer's disease by increasing toxic Abeta42 peptides. They also impair the endoplasmic reticulum's stress response pathway, affecting molecular chaperone levels.

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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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    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Cellular Stress Response

    Background:

    • Mutant presenilin proteins are implicated in Alzheimer's disease pathogenesis.
    • These mutations elevate the production of amyloid-beta 42 (Abeta42) peptides.
    • The endoplasmic reticulum (ER) responds to cellular stress by adjusting molecular chaperone levels.

    Discussion:

    • Mutant presenilins exacerbate Alzheimer's disease by increasing Abeta42.
    • These proteins also downregulate a critical signaling pathway.
    • This pathway regulates molecular chaperones in the ER during stress.

    Key Insights:

    • Mutant presenilins have a dual detrimental effect in Alzheimer's disease.
    • Downregulation of the ER stress response pathway is a novel mechanism.
    • This impacts the cell's ability to cope with proteotoxic stress.

    Outlook:

    • Understanding this pathway offers new therapeutic targets for Alzheimer's.
    • Modulating ER stress response could mitigate neurodegeneration.
    • Further research into chaperone regulation in neurodegenerative diseases is warranted.