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The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest [PDF]
FEBS Letters, 2000 The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast.
Didier Picard, Olivier Donze
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Cdc37 as a Co-chaperone to Hsp90
2022The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. Analysis of the structure of Hsp90-Cdc37-kinase complexes demonstrates the way in which Cdc37 interacts with and controls the folding of a large proportion of intracellular protein ...
Thomas L, Prince +4 more
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Bioorganic and Medicinal Chemistry, 2017
Targeting Hsp90-Cdc37 protein-protein interaction (PPI) is becoming an alternative approach for future anti-cancer drug development. We previously reported the discovery of an eleven-residue peptide (Pep-1) with micromolar activity for the disruption of Hsp90-Cdc37 PPI.
Xiaoli Xu, Zhengyu Jiang, Lei Wang
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Targeting Hsp90-Cdc37 protein-protein interaction (PPI) is becoming an alternative approach for future anti-cancer drug development. We previously reported the discovery of an eleven-residue peptide (Pep-1) with micromolar activity for the disruption of Hsp90-Cdc37 PPI.
Xiaoli Xu, Zhengyu Jiang, Lei Wang
exaly +3 more sources
Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes [PDF]
EMBO Journal, 2002 Cdc37 has been shown to be required for the activity and stability of protein kinases that regulate different stages of cell cycle progression. However, little is known so far regarding interactions of Cdc37 with kinases that play a role in cell division. Here we show that the loss of function of Cdc37 in Drosophila leads to defects in mitosis and male
Elena Rebollo, Cayetano Gonzalez
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Protein Expression and Purification, 2013
Hsp90 has emerged as a promising target for cancer treatment. Hsp90 interacts with co-chaperone Cdc37 to mediate the conformational maturation of its kinase client proteins. Screening small molecule inhibitors targeting Hsp90/Cdc37 might be a promising strategy for further cancer therapeutic.
Jing, He +7 more
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Hsp90 has emerged as a promising target for cancer treatment. Hsp90 interacts with co-chaperone Cdc37 to mediate the conformational maturation of its kinase client proteins. Screening small molecule inhibitors targeting Hsp90/Cdc37 might be a promising strategy for further cancer therapeutic.
Jing, He +7 more
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Physical interaction of Cdc28 with Cdc37 in Saccharomyces cerevisiae
Molecular Genetics and Genomics, 2002The Cdc37 protein in Saccharomyces cerevisiae is thought to be a kinase-targeting subunit of the chaperone Hsp90. In a genetic screen, four protein kinases were identified as interacting with Cdc37 - Cdc5, Cdc7, Cdc15 and Cak1. This result underlines the importance of Cdc37 for the folding of protein kinases.
M, Mort-Bontemps-Soret +2 more
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The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases
Current Drug Targets, 2022Abstract: Heat shock protein (Hsp) 90 is an ATP-dependent chaperone and plays a vital role in the folding, maturation, and stability of a protein. Hsp90 and its client proteins have become targets of various diseases through the regulation of disease-related proteins.
Xuerong, Zhang +5 more
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Role of Cdc37 in Breast Cancer
1999Abstract : Estrogen is a key hormonal regulator of mammary epithelial cell growth. Thus, understanding the mechanisms of estrogen-mediated growth regulation is key to understanding to understanding growth disregulation in breast cancer. Current information indicates that estrogen regulates cell growth by activating the Raf-l/Mek/MAP kinase pathway and ...
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Hsp90 and Cdc37 – a chaperone cancer conspiracy
Current Opinion in Genetics & Development, 2005The Hsp90 molecular chaperone system is involved in the activation of an important set of cell regulatory proteins, including many whose disregulation drives cancer. Recruitment of protein kinases to the Hsp90 system is mediated by the co-chaperone adaptor Cdc37 -- an essential protein whose overexpression is itself, oncogenic.
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Role of Cdc37 in Breast Cancer
1998Abstract : P50CdC37 is a recently discovered gene which functions in the establishment of protein kinase signaling pathways by functioning in complex with molecular chaperone Hsp9O. The proposed mode of function of Cdc37/Hsp9O complex is that Cdc37 targets intrinsically unstable kinases to the complex with Hsp9O, and this transient interaction of newly
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