Results 11 to 20 of about 3,736 (194)
HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation
Nature Communications, 2022 Binding to HSP90-CDC37 is essential for the activity of many protein kinases, but its function is unclear. Here, the authors show that HSP90-CDC37 provides a structural platform for the phosphatase PP5 to dephosphorylate a bound kinase, ‘factory ...
Jasmeen Oberoi +6 more
doaj +4 more sources
Structure of an Hsp90-Cdc37-Cdk4 complex. [PDF]
Molecular Cell, 2006 Activation of many protein kinases depends on their interaction with the Hsp90 molecular chaperone system. Recruitment of protein kinase clients to the Hsp90 chaperone system is mediated by the cochaperone adaptor protein Cdc37, which acts as a scaffold,
Frank Sobott (1355490) +17 more
core +5 more sources
Design of Disruptors of the Hsp90–Cdc37 Interface [PDF]
Molecules, 2020 The molecular chaperone Hsp90 is a ubiquitous ATPase-directed protein responsible for the activation and structural stabilization of a large clientele of proteins.
Ilda D’Annessa +10 more
doaj +5 more sources
Cdc37 goes beyond Hsp90 and kinases
Cell Stress & Chaperones, 2003 Cdc37 is a relatively poorly conserved and yet essential molecular chaperone. It has long been thought to function primarily as an accessory factor for Hsp90, notably directing Hsp90 to kinases as substrates.
Didier Picard +3 more
core +6 more sources
A role for Cdc37 in EGFRvIII biogenesis
, 2007 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 ...
Scales, Stephen
core +4 more sources
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
doaj +2 more sources
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.
David A. Agard +3 more
core +6 more sources
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 ...
Hunter, Tony, Poon, Randy Y.C.
core +4 more sources
Assembly mechanism of early Hsp90-Cdc37-kinase complexes
Science Advances, 2022 Molecular chaperones have an essential role for the maintenance of a balanced protein homeostasis. Here, we investigate how protein kinases are recruited and loaded to the Hsp90-Cdc37 complex, the first step during Hsp90-mediated chaperoning that leads ...
Abzalimov, Rinat R +4 more
core +3 more sources
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
doaj +3 more sources