Cargando…
Silencing the cochaperone CDC37 destabilises kinase clients and sensitises cancer cells to HSP90 inhibitors
The cochaperone CDC37 promotes association of HSP90 with the protein kinase subset of client proteins to maintain their stability and signalling functions. HSP90 inhibitors induce depletion of clients, which include several oncogenic kinases. We hypothesised that the targeting of CDC37 using siRNAs...
Autores principales: | Smith, Jennifer R., Clarke, Paul A., de Billy, Emmanuel, Workman, Paul |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2635547/ https://www.ncbi.nlm.nih.gov/pubmed/18931700 http://dx.doi.org/10.1038/onc.2008.380 |
Ejemplares similares
-
Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins
por: Smith, Jennifer R., et al.
Publicado: (2013) -
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
por: Li, Ting, et al.
Publicado: (2018) -
Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37
por: Vaughan, Cara K., et al.
Publicado: (2008) -
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
por: Bachman, Ashleigh B., et al.
Publicado: (2018) -
Assembly mechanism of early Hsp90-Cdc37-kinase complexes
por: Keramisanou, Dimitra, et al.
Publicado: (2022)