Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion.
PLoS ONE, 2012 Cdc37 is a 50 kDa molecular chaperone which targets intrinsically unstable protein kinases to the molecular chaperone HSP90. It is also an over-expressed oncoprotein that mediates carcinogenesis and maintenance of the malignant phenotype by stabilizing ...
Avraam El Hamidieh +2 more
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Koumine exerts its anti-colorectal cancer effects by disrupting the interaction between HSP90 and CDC37, thereby downregulating downstream signaling pathways [PDF]
Frontiers in OncologyBackgroundKoumine, a principal bioactive alkaloid derived from the traditional Chinese herb Gelsemium elegans, has demonstrated broad cytotoxic activity against various cancer cell lines. However, its specific anti-tumor efficacy and underlying molecular
HaiLing Lin +6 more
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Integrating Single-Cell Transcriptomics and Mendelian Randomization to Identify RAC1 as a Causal Metabolic Driver of Pericyte Dysfunction in Systemic Sclerosis. [PDF]
Mediators InflammBackground Systemic sclerosis (SSc) is an autoimmune disease characterized by vascular injury and progressive fibrosis. Although microvascular injury is an inciting event and pericytes are recognized as a major source of myofibroblasts, the precise phenotypic heterogeneity of pericytes in the SSc microenvironment and the genetic mechanisms driving ...
Wang X, Zhang Z, Jiang E, Zhang M, Hu G.
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Cdc37: a protein kinase chaperone?
Trends in Cell Biology, 1997 The activity of most protein kinases is highly regulated, typically via phosphorylation and/or subunit association. However, the folding of protein kinases into an active state or a form capable of activation is now emerging as another important step through which they can be regulated.
Hunter, Tony R., Poon, Randy Yat Choi
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A role for Cdc37 in EGFRvIII biogenesis
, 2013 The mutant epidermal growth factor receptor, EGFRvIII, is associated with tumour aggressiveness and drug resistance in glioblastoma. Our lab has shown that the molecular chaperone Hsp90 interacts with nascent EGFRvIII, and that EGFRvIII expression and function is dependent upon Hsp90 activity.
Scales, Stephen
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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches [PDF]
Trends in Biochemical Sciences, 2017 The Hsp90/Cdc37 chaperone system interacts with and supports 60% of the human kinome. Not only are Hsp90 and Cdc37 generally required for initial folding, but many kinases rely on the Hsp90/Cdc37 throughout their lifetimes. A large fraction of these 'client' kinases are key oncoproteins, and their interactions with the Hsp90/Cdc37 machinery are crucial
Verba, Kliment A, Agard, David A
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Molecular mechanism of PINK1 regulation by the Hsp90 machinery [PDF]
Nature CommunicationsHundreds of human kinases, including PINK1—a protein kinase associated with familial Parkinson’s disease—are regulated by Hsp90 and its cochaperones. While previous studies have elucidated the mechanism of kinase loading into the Hsp90 machinery, the ...
Xuyang Tian +7 more
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Therapeutic Potential of the Hsp90/Cdc37 Interaction in Neurodegenerative Diseases
Frontiers in Neuroscience, 2019 Alzheimer’s, Huntington’s, and Parkinson’s are devastating neurodegenerative diseases that are prevalent in the aging population. Patient care costs continue to rise each year, because there is currently no cure or disease modifying treatments for these ...
Liam Gracia +3 more
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AURKB/CDC37 complex promotes clear cell renal cell carcinoma progression via phosphorylating MYC and constituting an AURKB/E2F1-positive feedforward loop [PDF]
Cell Death and DiseaseAs the second most common malignant tumor in the urinary system, renal cell carcinoma (RCC) is imperative to explore its early diagnostic markers and therapeutic targets.
Fang Li +11 more
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The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically
Biological Chemistry, 2002 Cdc37 associates with the heat-shock protein 90 (Hsp90) molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. Cdc37 has been proposed to be a specificity factor for Hsp90, directing it notably towards kinases.
Abbas-Terki, Toufik +3 more
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