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Related Experiment Video

Updated: Jun 14, 2025

CD Spectroscopy to Study DNA-Protein Interactions

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

HSP110 Regulates the Assembly of the SWI/SNF Complex.

Océane Pointeau¹, Manon Paccagnini¹, Natalia Borges-Bonan¹

¹Institut National de la Santé et de la Recherche Médicale (Inserm), Inserm CTM UMR1231, Université Bourgogne-Europe, 21000 Dijon, France.

|June 11, 2025

Summary

This summary is machine-generated.

Heat shock protein 110 (HSP110) aids DNA repair and chromatin remodeling. This chaperone protein interacts with SWI/SNF complexes, enhancing cellular adaptive stress responses.

Keywords:

HSP110 SWI/SNF chromatin remodeling complex

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Area of Science:

Molecular Biology
Cellular Stress Response
Cancer Biology

Background:

Heat shock protein 110 (HSP110) is a chaperone involved in proteostasis and regulating oncogenic signaling pathways.
Nuclear HSP110 expression correlates with chemoresistance in gastric and colorectal cancers and is induced by DNA-damaging agents.
Previous studies showed nuclear HSP110's role in Non-Homologous End Joining (NHEJ) DNA repair.

Purpose of the Study:

To investigate the nuclear interactome of HSP110 in response to DNA damage.
To elucidate the role of HSP110 in chromatin remodeling and adaptive stress responses.

Main Methods:

Nuclear proteome analysis to identify HSP110 interacting partners.
Chromatin association assays in cells treated with DNA-damaging agents (temozolomide, oxaliplatin).
Co-immunoprecipitation to confirm direct interaction between HSP110 and SWI/SNF components.

Main Results:

HSP110's nuclear interactome is enriched with components of SWI/SNF chromatin remodeling complexes.
HSP110 associates with chromatin upon exposure to temozolomide and oxaliplatin.
HSP110 directly interacts with SMARCC2, a core subunit of SWI/SNF, facilitating complex assembly.

Conclusions:

HSP110 plays a novel role in facilitating the assembly of SWI/SNF chromatin remodeling complexes.
This function expands the known roles of HSP110 beyond proteostasis to include the regulation of critical nuclear macromolecular complexes.
HSP110 is integral to the adaptive stress response by modulating chromatin structure and DNA repair pathways.