Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

Heat-Shock Protein 90 Controls the Expression of Cell-Cycle Genes by Stabilizing Metazoan-Specific Host-Cell Factor HCFC1

MPG-Autoren

Antonova,  Aneliya
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Hummel,  Barbara
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Khavaran,  Ashkan
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Aprile-Garcia,  Fernando
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Rawat,  Prashant
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Gundel,  Kathrin
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Schneck,  Megan
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Hansen,  Erik C.
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Mittler,  Gerhard
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

/persons/resource/persons241703

Sawarkar,  Ritwick
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Externe Ressourcen

https://www.sciencedirect.com/science/article/pii/S2211124719312884?via%3Dihub
(Verlagsversion)

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Antonova, A., Hummel, B., Khavaran, A., Redhaber, D. M., Aprile-Garcia, F., Rawat, P., et al. (2019). Heat-Shock Protein 90 Controls the Expression of Cell-Cycle Genes by Stabilizing Metazoan-Specific Host-Cell Factor HCFC1. Cell Reports, 29, 1645-1659. doi:org/10.1016/j.celrep.2019.09.084.


Zitierlink: https://hdl.handle.net/21.11116/0000-0005-98ED-5
Zusammenfassung
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.