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

Antonova, Aneliya; Hummel, Barbara; Khavaran, Ashkan; Redhaber, Desiree M.; Aprile-Garcia, Fernando; Rawat, Prashant; Gundel, Kathrin; Schneck, Megan; Hansen, Erik C.; Mitschke, Jan; Mittler, Gerhard; Miething, Cornelius; Sawarkar, Ritwick

doi:org/10.1016/j.celrep.2019.09.084

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

MPS-Authors

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;

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

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

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.

Cite as: https://hdl.handle.net/21.11116/0000-0005-98ED-5

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.