Heat-shock protein 90 controls the expression of cell-cycle genes by stabilizing metazoan-specific host-cell factor HCFC1

Abstract: Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de novo folding in the cytosol, and this raises an important question about chaperone function in the nucleus. We performed a systematic analysis of the nuclear pool of heat-shock protein 90. Three orthogonal and independent analyses led us to the core functional interactome of HSP90. Computational and biochemical analyses identify host cell factor C1 (HCFC1) as a transcriptional regulator that depends on HSP90 for its stability. HSP90 was required to maintain the expression of HCFC1-targeted cell-cycle genes. The regulatory nexus between HSP90 and the HCFC1 module identified in this study sheds light on the relevance of chaperones in the transcription of cell-cycle genes. Our study also suggests a therapeutic avenue of combining chaperone and transcription inhibitors for cancer treatment

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch
Anmerkungen
Cell reports. - 29, 6 (2019) , 1645-1659.e9, ISSN: 2211-1247

Klassifikation
Biowissenschaften, Biologie
Schlagwort
Krebs
Chromatin
Hitzeschock-Proteine

Ereignis
Veröffentlichung
(wo)
Freiburg
(wer)
Universität
(wann)
2019
Urheber
Antonova, Aneliya
Hummel, Barbara
Khavaran, Ashkan
Redhaber, Desiree Melanie
Aprile-Garcia, Fernando
Rawat, Prashant
Gundel, Kathrin
Schneck, Megan
Hansen, Erik C.
Mitschke, Jan
Mittler, Gerhard
Miething, Cornelius
Sawarkar, Ritwick

DOI
10.1016/j.celrep.2019.09.084
URN
urn:nbn:de:bsz:25-freidok-1513121
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Letzte Aktualisierung
14.08.2025, 08:46 UTC

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Entstanden

  • 2019

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