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HSP90AA1 — TP53
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
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IRef Biogrid Interaction:
TP53
—
HSP90AA1
(physical association, affinity chromatography technology)
Wang et al., J Cell Biochem 2011*
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IRef Biogrid Interaction:
TP53
—
HSP90AA1
(direct interaction, enzymatic study)
Burch et al., J Mol Biol 2004*
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IRef Biogrid Interaction:
TP53
—
HSP90AA1
(physical association, affinity chromatography technology)
Taipale et al., Cell 2012
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IRef Biogrid Interaction:
TP53
—
HSP90AA1
(physical association, affinity chromatography technology)
Wang et al., J Biol Chem 2003*
-
IRef Biogrid Interaction:
TP53
—
HSP90AA1
(physical association, affinity chromatography technology)
Akakura et al., J Biol Chem 2001*
-
IRef Biogrid Interaction:
TP53
—
HSP90AA1
(physical association, affinity chromatography technology)
Peng et al., J Biol Chem 2001*
-
IRef Biogrid Interaction:
TP53
—
HSP90AA1
(physical association, affinity chromatography technology)
Nagata et al., Oncogene 1999*
-
IRef Dip Interaction:
TP53
—
HSP90AA1
(direct interaction, nuclear magnetic resonance)
Park et al., Nature structural & molecular biology 2011*
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IRef Hprd Interaction:
TP53
—
HSP90AA1
(in vivo)
Peng et al., J Biol Chem 2001*, Wang et al., J Biol Chem 2003*
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IRef Ophid Interaction:
TP53
—
HSP90AA1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Walerych et al., J Biol Chem 2004
:
A minor decrease in p53 protein level following the treatment of human fibroblasts with the inhibitors suggests the potential
involvement of
Hsp90 in the stabilization of wild-type
p53 ... To support our in vivo findings, we used a reconstituted system with highly purified recombinant proteins to examine the
effects of
Hsp90 on wild-type
p53 binding to the p21 promoter sequence
Müller et al., J Biol Chem 2004
:
Hsp90 regulates the activity of wild type
p53 under physiological and elevated temperatures
Naoe et al., Cancer Sci 2006
(Hematologic Neoplasms...) :
Nucleophosmin (NPM) is a nucleolar phosphoprotein that plays multiple roles in ribosome assembly and transport, cytoplasmic-nuclear trafficking,
centrosome duplication and
regulation of
p53
Bergstralh et al., Exp Cell Res 2007
(Lung Neoplasms) :
Mass spectroscopy identified the protein as nucleophosmin/B23 (NPM), a multifunctional protein with diverse roles : ribosome biosynthesis,
p53 regulation , nuclear-cytoplasmic shuttling, and
centrosome duplication
Habib et al., Arch Biochem Biophys 2009
(MAP Kinase Signaling System) :
p53 regulates
Hsp90beta during arsenite induced cytotoxicity in glutathione-deficient cells ... In addition,
p53 transcriptionally
repressed Hsp90beta gene expression
Walerych et al., Oncogene 2009
:
Hsp90 stabilizes the binding of
p53 to the promoter sequence at 37 degrees C, whereas under heat-shock conditions the requirement for the Hsp70-Hsp40 system and its cooperation with Hsp90 increases
Regan et al., Int J Oncol 2011
(Neuroblastoma) :
Hsp90 inhibition
increases p53 expression and destabilizes MYCN and MYC in neuroblastoma ... It was found that
Hsp90 inhibition in neuroblastoma cell lines
resulted in significant growth suppression, a decrease in MYCN and MYC expression, and an increase in the expression of
p53
Banu et al., Toxicol Appl Pharmacol 2011
:
Our data indicated that CrVI : ( i ) induced DNA fragmentation and increased apoptosis, ( ii ) increased cytochrome c release from the mitochondria to cytosol, ( iii ) downregulated anti-apoptotic Bcl-2, Bcl-XL, HSP70 and
HSP90 ; upregulated pro-apoptotic BAX and BAD, ( iv ) altered translocation of Bcl-2, Bcl-XL, BAX, BAD, HSP70 and HSP90 to the mitochondria, ( v ) upregulated p-ERK and p-JNK, and selectively translocated p-ERK to the mitochondria and nucleus, ( vi ) activated caspase-3 and PARP, and ( vii ) increased phosphorylation of
p53 at ser-6, ser-9, ser-15, ser-20, ser-37, ser-46 and ser-392,
increased p53 transcriptional activation, and downregulated MDM-2
Mantel et al., Blood 1999
(Polyploidy) :
p53 has already been implicated in
centrosome regulation