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Related Concept Videos

Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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...
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...
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...

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Related Experiment Video

Updated: May 12, 2026

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Recent insights into HSP70: proteostasis and beyond.

Kristina Pustovaya1, Artem Venediktov1, Vladislav Soldatov2

  • 1Human Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.

Frontiers in Molecular Biosciences
|May 11, 2026
PubMed
Summary

70 kDa heat shock proteins (HSP70s) are key regulators of cellular balance. Recent studies reveal novel roles beyond proteostasis, including anti-inflammatory and RNA-binding functions, expanding their known biological significance.

Keywords:
GRP78HSC70HSPA1Amolecular chaperonesmortalinprotein quality control

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Last Updated: May 12, 2026

Intracellular Refolding Assay
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07:57

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Published on: January 20, 2023

Area of Science:

  • Molecular Biology
  • Cellular Physiology
  • Biochemistry

Background:

  • 70 kDa heat shock proteins (HSP70s) are established regulators of proteostasis.
  • Their roles in cellular physiology and pathology are diverse and complex.

Purpose of the Study:

  • To review and integrate foundational knowledge of HSP70 biology with recent discoveries.
  • To highlight emerging functions beyond classical proteostasis roles.

Main Methods:

  • Literature review integrating foundational and recent research on HSP70s.
  • Analysis of new data on HSP70 substrate specificity and molecular dynamics.
  • Examination of evidence for noncanonical functions.

Main Results:

  • HSP70s exhibit novel substrate specificity and molecular dynamics in client interactions.
  • Noncanonical functions include anti-inflammatory properties, promotion of adipose tissue browning, and enhanced angiogenesis.
  • HSP70s bind double-stranded RNA, expanding their functional repertoire beyond mRNA degradation.

Conclusions:

  • HSP70s possess a broader functional repertoire than previously understood.
  • Emerging roles in inflammation, metabolism, and RNA binding are significant.
  • These findings necessitate a re-evaluation of HSP70 functions in health and disease.