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@ARTICLE{Isermann:300301,
author = {T. Isermann$^*$ and K. L. Schneider and F. Wegwitz and T.
De Oliveira and L.-C. Conradi and V. Volk and F. Feuerhake
and B. Papke$^*$ and S. Stintzing$^*$ and B. Mundt and F.
Kühnel and U. M. Moll and R. Schulz-Heddergott},
title = {{E}nhancement of colorectal cancer therapy through
interruption of the {HSF}1-{HSP}90 axis by p53 activation or
cell cycle inhibition.},
journal = {Cell death and differentiation},
volume = {nn},
issn = {1350-9047},
address = {[London]},
publisher = {Springer Nature},
reportid = {DKFZ-2025-00751},
pages = {nn},
year = {2025},
note = {epub},
abstract = {The stress-associated chaperone system is an actionable
target in cancer therapies. It is ubiquitously upregulated
in cancer tissues and enables tumorigenicity by stabilizing
oncoproteins. Most inhibitors target the key component,
heat-shock protein 90 (HSP90). Although HSP90 inhibitors are
highly tumor-selective, they fail in clinical trials. These
failures are partly due to interference with a negative
regulatory feedback loop in the heat-shock response (HSR):
in response to HSP90 inhibition, there is compensatory
synthesis of stress-inducible chaperones, mediated by the
transcription factor heat-shock-factor 1 (HSF1). We recently
identified that wild-type p53 reduces the HSR by repressing
HSF1 via a p21-CDK4/6-MAPK-HSF1 axis. Here, we test whether
in HSP90-based therapies, simultaneous p53 activation or
direct cell cycle inhibition interrupts the deleterious
HSF1-HSR axis and improves the efficiency of HSP90
inhibitors. We found that the clinically relevant p53
activator Idasanutlin suppresses the HSF1-HSR activity in
HSP90 inhibitor-based therapies. This combination
synergistically reduces cell viability and accelerates cell
death in p53-proficient colorectal cancer (CRC) cells,
murine tumor-derived organoids, and patient-derived
organoids (PDOs). Mechanistically, upon combination therapy,
CRC cells upregulate p53-associated pathways, apoptosis, and
inflammatory pathways. Likewise, in a CRC mouse model, dual
HSF1-HSP90 inhibition represses tumor growth and remodels
immune cell composition. Importantly, inhibition of the
cyclin-dependent kinases 4/6 (CDK4/6) under HSP90 inhibition
phenocopies synergistic repression of the HSR in
p53-proficient CRC cells. Moreover, in p53-deficient CRC
cells, HSP90 inhibition in combination with CDK4/6
inhibitors similarly suppresses the HSF1-HSR and reduces
cancer growth. Likewise, p53-mutated PDOs respond to dual
HSF1-HSP90 inhibition, providing a strategy to target CRC
independent of the p53 status. In sum, we provide new
options to improve HSP90-based therapies to enhance CRC
therapies.},
cin = {BE01},
ddc = {610},
cid = {I:(DE-He78)BE01-20160331},
pnm = {899 - ohne Topic (POF4-899)},
pid = {G:(DE-HGF)POF4-899},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:40204953},
doi = {10.1038/s41418-025-01502-x},
url = {https://inrepo02.dkfz.de/record/300301},
}