Inhibition of MDM2 by hsp90 contributes to mutant p53 stabilization (Q28212970)

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L Chen

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C Li

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W Lu

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J Chen

Journal of Biological Chemistry

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language of work or name

English

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publication date

2 November 2001

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published in

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volume

276

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page(s)

40583-90

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issue

44

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cites work

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p53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding.

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Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p53-plus-ras-transformed cell lines

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The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent

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An oncogenic form of p53 confers a dominant, gain-of-function phenotype that disrupts spindle checkpoint control

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Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway

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Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association

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Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell

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Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

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The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

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Activation of an MDM2-specific caspase by p53 in the absence of apoptosis

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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

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