Biological relevance of Hsp90-binding immunophilins in cancer development and treatment

International Journal of Cancer. Journal International Du Cancer
Gisela I MazairaM D Galigniana

Abstract

Immunophilins are a family of intracellular receptors for immunosuppressive drugs. Those immunophilins that are related to immunosuppression are the smallest proteins of the family, i.e., FKBP12 and CyPA, whereas the other members of the family have higher molecular weight because the show additional domains to the drug-binding site. Among these extra domains, the TPR-domain is perhaps the most relevant because it permits the interaction of high molecular weight immunophilins with the 90-kDa heat-shock protein, Hsp90. This essential molecular chaperone regulates the biological function of several protein-kinases, oncogenes, protein phosphatases, transcription factors and cofactors . Hsp90-binding immunophilins where first characterized due to their association with steroid receptors. They regulate the cytoplasmic transport and the subcellular localization of these and other Hsp90 client proteins, as well as transcriptional activity, cell proliferation, cell differentiation and apoptosis. Hsp90-binding immunophilins are frequently overexpressed in several types of cancers and play a key role in cell survival. In this article we analyze the most important biological actions of the best characterized Hsp90-binding immunophilins in...Continue Reading

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Citations

Jul 5, 2016·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Theo Rein
Dec 6, 2017·International Journal of Molecular Sciences·Gabriel R FriesTheo Rein
Nov 23, 2019·Biochemical Society Transactions·Cristina Daneri-BecerraMario D Galigniana
Aug 28, 2018·Nuclear Receptor Research·Gisela I MazairaMario D Galigniana
May 29, 2016·Molecular Oncology·Mariana LagadariMario D Galigniana

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