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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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Molecular Chaperones and Protein Folding03:00

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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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Regulation of the Unfolded Protein Response01:31

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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...
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Mitochondrial Precursor Proteins01:39

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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Protein Folding Quality Check in the RER01:29

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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...
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Related Experiment Video

Updated: Feb 18, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Molecular Chaperone Receptors.

Ayesha Murshid1, Jimmy Theriault1, Jianlin Gong2

  • 1Molecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA, 02215, USA.

Methods in Molecular Biology (Clifton, N.J.)
|November 28, 2017
PubMed
Summary

Extracellular heat shock proteins (HSP) bind to cell surface receptors, including c-type lectin receptors (CLR) and scavenger receptors (SR). This discovery advances understanding of HSP-mediated cell signaling and immunity.

Keywords:
ExtracellularHeatImmunityProteinReceptorScavengerShock

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Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Extracellular heat shock proteins (HSP) are crucial for cell signaling and immune responses.
  • Surface receptors on various cell types mediate many HSP effects.
  • Understanding these interactions is key to deciphering cellular communication.

Purpose of the Study:

  • To identify and characterize receptors that bind extracellular heat shock proteins (HSP).
  • To investigate the binding specificities of Hsp70 to different receptor classes.
  • To explore methods for discovering HSP receptors and studying their function.

Main Methods:

  • Utilized Chinese Hamster Ovary (CHO-K1) cells lacking endogenous HSP binding capacity.
  • Cloned candidate receptors into these null cells to assess HSP binding.
  • Employed techniques to study individual receptors and in vivo HSP receptor function.

Main Results:

  • Identified that Hsp70 binds strongly to at least two receptor classes: c-type lectin receptors (CLR) and scavenger receptors (SR).
  • Demonstrated Hsp70 binding to LOX-1 (a CLR and SR) via its c-type lectin binding domain (CTLD).
  • Showed Hsp70 binding to SR family members SREC-I and FEEL-1/CLEVER-1/STABILIN-1, which possess EGF-like repeats.

Conclusions:

  • Hsp70 interacts with multiple cell surface receptor families, including CLRs and SRs.
  • Specific domains like CTLD and extracellular repeats mediate these HSP-receptor interactions.
  • The study provides foundational methods for discovering and analyzing HSP receptors in vitro and in vivo.