Regulation of survivin function by Hsp90

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Regulation of survivin function by Hsp90.

Pathways controlling cell proliferation and cell survival require flexible adaptation to environmental stresses. These mechanisms are frequently exploited in cancer, allowing tumor cells to thrive in unfavorable milieus. Here, we show that Hsp90, a molecular chaperone that is central to the cellular stress response, associates with survivin, an apoptosis inhibitor and essential regulator of mit...

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Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone which is essential in eukaryotes. It is required for the activation and stabilization of a wide variety of client proteins and many of them are involved in important cellular pathways. Since Hsp90 affects numerous physiological processes such as signal transduction, intracellular transport, and protein degradation, it became ...

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Mechanisms of Hsp90 regulation

Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This implicates Hsp90 in diverse biological processes that require a variety of co-ordinated regulatory mechanisms to control its activity. Perhaps the most important regulator is heat shock factor 1 (HSF1), which is primarily responsible for upregulating Hsp90 by binding heat...

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Survivin: Transcriptional Regulation and Protein Function in Cancer

Cite this article: Neophytou CM, Constantinou AI (2017) Survivin: Transcriptional Regulation and Protein Function in Cancer. J Immunol Clin Res 4(2): 1041. *Corresponding author Andreas I. Constantinou, Laboratory of Cancer Biology and Chemoprevention, Department of Biological Sciences, Faculty of Pure and Applied Sciences, University of Cyprus, P.O. Box 20537, 1678 Nicosia, Cyprus, Tel: 357 22...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2003

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.2434345100