Microthermal-induced subcellular-targeted protein damage in cells on plasmonic nanosilver-modified surfaces evokes a two-phase HSP-p97/VCP response
Jazyk angličtina Země Velká Británie, Anglie Médium electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
33514738
PubMed Central
PMC7846584
DOI
10.1038/s41467-021-20989-9
PII: 10.1038/s41467-021-20989-9
Knihovny.cz E-zdroje
- MeSH
- analýza jednotlivých buněk metody MeSH
- kovové nanočástice chemie MeSH
- lidé MeSH
- nádorové buněčné linie MeSH
- povrchová plasmonová rezonance MeSH
- proteasomový endopeptidasový komplex metabolismus MeSH
- protein obsahující valosin genetika metabolismus MeSH
- proteiny tepelného šoku HSP70 metabolismus MeSH
- reakce na tepelný šok * MeSH
- stříbro chemie MeSH
- ubikvitin metabolismus MeSH
- vysoká teplota škodlivé účinky MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- proteasomový endopeptidasový komplex MeSH
- protein obsahující valosin MeSH
- proteiny tepelného šoku HSP70 MeSH
- stříbro MeSH
- ubikvitin MeSH
- VCP protein, human MeSH Prohlížeč
Despite proteotoxic stress and heat shock being implicated in diverse pathologies, currently no methodology to inflict defined, subcellular thermal damage exists. Here, we present such a single-cell method compatible with laser-scanning microscopes, adopting the plasmon resonance principle. Dose-defined heat causes protein damage in subcellular compartments, rapid heat-shock chaperone recruitment, and ensuing engagement of the ubiquitin-proteasome system, providing unprecedented insights into the spatiotemporal response to thermal damage relevant for degenerative diseases, with broad applicability in biomedicine. Using this versatile method, we discover that HSP70 chaperone and its interactors are recruited to sites of thermally damaged proteins within seconds, and we report here mechanistically important determinants of such HSP70 recruitment. Finally, we demonstrate a so-far unsuspected involvement of p97(VCP) translocase in the processing of heat-damaged proteins. Overall, we report an approach to inflict targeted thermal protein damage and its application to elucidate cellular stress-response pathways that are emerging as promising therapeutic targets.
Danish Cancer Society Research Center Copenhagen Denmark
Regional Centre for Applied Molecular Oncology Masaryk Memorial Cancer Institute Brno Czech Republic
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