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Updated: Feb 18, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
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.
Abstract:
Extracellular heat shock proteins (HSP) play important roles in cell signaling and immunity. Many of these effects are mediated by surface receptors expressed on a wide range of cell types. We have investigated the nature of such proteins by cloning candidate receptors into cells (CHO-K1) with the rare property of being null for HSP binding. Using this approach we have discovered that Hsp70 binds avidly to at least two classes of receptors including: (1) c-type lectin receptors (CLR) and (2) scavenger receptors (SR). However, the structural nature of the receptor-ligand interactions is not clear at this time. Hsp70 can bind to LOX-1 (a member of both the CLR and SR), with the c-type lectin binding domain (CTLD) as well as the SR family members SREC-I and FEEL-1/CLEVER-1/STABILIN-1, which by contrast have arrays of EGF-like repeats in their extracellular domains. In this chapter we will discuss: (1) methods for discovery of HSP receptors, (2) approaches to the study of individual receptors in cells that contain multiple such receptors, and (3) methods for investigating HSP receptor function in vivo.
Insights
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.
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.
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