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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.
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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...
Types of Receptors: Cell Surface Receptors01:28

Types of Receptors: Cell Surface Receptors

Cell-surface receptors, also known as transmembrane receptors, are cell surface, membrane-anchored (integral) proteins that bind to external ligand molecules. This type of receptor spans the plasma membrane and performs signal transduction, converting an extracellular signal into an intracellular signal. Ligands that interact with cell-surface receptors do not have to enter the cell that they affect. Cell-surface receptors are also called cell-specific proteins or markers because they are...
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...
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Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
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Cell surface receptors for molecular chaperones.

Stuart K Calderwood1, Jimmy Theriault, Phillip J Gray

  • 1Molecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Room 553, 21-27 Burlington Avenue, Boston, MA 02215, USA. scalderw@bidmc.harvard.edu

Methods (San Diego, Calif.)
|October 9, 2007
PubMed
Summary

Extracellular heat shock proteins (HSPs) activate immune cells via cell surface receptors. Heat shock protein 70 enhances anti-tumor immunity by promoting antigen presentation and T cell activation.

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Published on: January 24, 2012

Area of Science:

  • Immunology
  • Molecular Biology
  • Oncology

Background:

  • Extracellular heat shock proteins (HSPs) are increasingly recognized for their potent effects on immune, inflammatory, and neuronal cells.
  • These effects are mediated through interactions with various cell surface receptors, including LRP/CD91, CD40, Toll-like receptors, Scavenger receptors, and c-type Lectins.
  • Despite originating from diverse gene superfamilies, extracellular HSPs often converge on similar receptor types to elicit responses.

Purpose of the Study:

  • To investigate heat shock protein (HSP) binding to different receptor types.
  • To elucidate the role of HSP-receptor interactions in tumor immunology.
  • To understand how HSPs, particularly HSP70, orchestrate anti-tumor immune responses.

Main Methods:

  • Assessment of heat shock protein binding to various cell surface receptor types.
  • Analysis of the immune effects induced by extracellular heat shock protein 70 (HSP70) released from tumor cells or administered via vaccine.
  • Evaluation of HSP70's role in antigen presentation and T cell activation.

Main Results:

  • Extracellular HSP70, released from dying tumor cells or used in vaccines, triggers significant immune responses.
  • HSP70 induces pro-inflammatory signaling, leading to the activation of antigen-presenting cells (APCs).
  • HSP70 facilitates cross-presentation of antigenic peptides from tumor cytoplasm into APCs for display on MHC class I molecules, activating cytotoxic T lymphocytes (CTLs) and promoting tumor cell killing.

Conclusions:

  • Heat shock protein-receptor binding is crucial for orchestrating anti-tumor immunity.
  • HSP70 plays a key role in activating APCs and enabling cross-presentation, leading to tumor-specific CTL responses.
  • Understanding these molecular chaperone-receptor interactions can guide the development of enhanced molecular chaperone-based cancer immunotherapies.