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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...
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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Updated: Jun 17, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Sigma-1 receptor chaperones and diseases.

Shang-Yi Tsai1, Teruo Hayashi, Tomohisa Mori

  • 1Cellular Pathobiology Section, Cellular Neurobiology Research Branch, IRP, NIDA, NIH, DHHS, 333 Cassell Drive, Baltimore, MD 21224, USA.

Central Nervous System Agents in Medicinal Chemistry
|December 22, 2009
PubMed
Summary

The sigma-1 receptor acts as a chaperone protein, regulating calcium signaling and protecting cells from stress. Its role in diseases like cancer and addiction requires further study.

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Last Updated: Jun 17, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
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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 Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Area of Science:

  • Cellular Biology
  • Neuroscience
  • Protein Biochemistry

Background:

  • Chaperone proteins assist in protein folding and are implicated in various diseases.
  • The sigma-1 receptor is a recently identified receptor chaperone.
  • It plays a role in cellular stress responses and signaling pathways.

Purpose of the Study:

  • To elucidate the function of the sigma-1 receptor as a chaperone.
  • To understand its role in calcium (Ca2+) signaling and cellular stress.
  • To explore its implications in various diseases.

Main Methods:

  • Investigated the sigma-1 receptor's interaction with the IP3 receptor.
  • Examined the sigma-1 receptor's translocation under cellular stress conditions.
  • Reviewed existing literature on sigma-1 receptor's involvement in diseases.

Main Results:

  • The sigma-1 receptor chaperones the IP3 receptor at the endoplasmic reticulum-mitochondrion interface, ensuring proper Ca2+ signaling.
  • Under pathological stress, it translocates to protect cells from apoptosis.
  • The sigma-1 receptor is crucial for metabotropic receptor signaling and cellular survival.

Conclusions:

  • The sigma-1 receptor is a vital receptor chaperone with essential roles in Ca2+ signaling and cellular stress response.
  • Its dysregulation is linked to diseases such as addiction, pain, depression, stroke, and cancer.
  • Further research is needed to confirm the direct contribution of its chaperone activity to these pathologies.