Abstract
HGTD-P is a hypoxia-responsive pro-apoptotic protein that transmits hypoxic signals directly to mitochondria. When overexpressed, HGTD-P induces cell death via typical mitochondrial apoptotic cascades. However, much is unknown about post-transcriptional modification and signaling networks of HGTD-P in association with cell death-regulating proteins. We performed yeast two-hybrid screening to identify the molecules involved in HGTD-P-mediated cell death pathways. In this study, we show that heat shock protein 90 physically interacts with HGTD-P and that suppression of Hsp90 activity by low concentrations of geldanamycin reduced HGTD-P-induced mitochondrial catastrophe through inhibition of mitochondrial translocation of HGTD-P.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Apoptosis*
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Benzoquinones
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Cells, Cultured
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HSP90 Heat-Shock Proteins / analysis
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HSP90 Heat-Shock Proteins / antagonists & inhibitors
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HSP90 Heat-Shock Proteins / metabolism*
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Humans
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Lactams, Macrocyclic
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Membrane Proteins
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Mitochondria / chemistry
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Mitochondria / metabolism*
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Mitochondrial Proteins / analysis
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Mitochondrial Proteins / metabolism*
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Proteasome Endopeptidase Complex / drug effects
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Proteasome Endopeptidase Complex / metabolism
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Protein Interaction Mapping
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Protein Transport
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Quinones / pharmacology
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Two-Hybrid System Techniques
Substances
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Benzoquinones
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FAM162A protein, human
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HSP90 Heat-Shock Proteins
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Lactams, Macrocyclic
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Membrane Proteins
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Mitochondrial Proteins
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Quinones
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Proteasome Endopeptidase Complex
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geldanamycin