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TNF receptor-associated protein 1

TRAP1, Hsp75
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. TRAP1 is a mitochondrial HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and endoplasmic reticulum (HSP90B1; MIM 191175) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM, Aug 2008] (from NCBI)
Top mentioned proteins: Hsp90, CAN, V1a, HSP70, TRAF2
Papers on TRAP1
Benzyl isothiocyanate alters the gene expression with cell cycle regulation and cell death in human brain glioblastoma GBM 8401 cells.
Chung et al., Laizhou, China. In Oncol Rep, Feb 2016
We also found that expression of 182 genes was downregulated and two genes were associated with receptor for cell responses to stimuli, the EGF containing fibulin-like extracellular matrix protein 1 (EFEMP1) was inhibited 2.01-fold and the TNF receptor-associated protein 1 (TRAP1) was inhibited 2.08-fold.
Downregulation of TRAP1 sensitizes glioblastoma cells to temozolomide chemotherapy through regulating metabolic reprogramming.
Zhao et al., Takarazuka, Japan. In Neuroreport, Jan 2016
Here, we show that the tumor necrosis factor receptor-associated protein 1 (TRAP1) is crucial for the Warburg effect in human glioblastoma multiforme (GBM).
Tumor Necrosis Factor Receptor-associated Protein 1 (TRAP1) Mutation and TRAP1 Inhibitor Gamitrinib-triphenylphosphonium (G-TPP) Induce a Forkhead box O (FOXO)-dependent Cell Protective Signal from Mitochondria.
Koh et al., Seoul, South Korea. In J Biol Chem, Jan 2016
UNASSIGNED: Tumor necrosis factor receptor (TNFR)-associated protein 1 (TRAP1), a mitochondrial Hsp90 family chaperone, has been identified as a critical regulator of cell survival and bioenergetics in tumor cells.
Differential submitochondrial localization of PINK1 as a molecular switch for mediating distinct mitochondrial signaling pathways.
Li et al., Atlanta, United States. In Cell Signal, Dec 2015
Under normal physiological conditions, PINK1 colocalizes with its substrate TRAP1 in the cristae membrane and intracristae space.
Aberrantly upregulated TRAP1 is required for tumorigenesis of breast cancer.
Wei et al., Beijing, China. In Oncotarget, Nov 2015
UNASSIGNED: Tumor necrosis factor receptor-associated protein 1 (TRAP1) is abnormally expressed in many cancers.
Proteomic Characterization of Annexin l (ANX1) and Heat Shock Protein 27 (HSP27) as Biomarkers for Invasive Hepatocellular Carcinoma Cells.
Chang et al., Taiwan. In Plos One, 2014
Notably, Annexin 1 (ANX1), ANX-2, vimentin and stress-associated proteins, such as GRP78, HSP75, HSC-70, protein disulfide isomerase (PDI), and heat shock protein-27 (HSP27), were exclusively up-regulated in SK-Hep-1 cells.
Differential expression of heat shock protein 90 isoforms in small cell lung cancer.
Lee et al., Ch'angwŏn, South Korea. In Int J Clin Exp Pathol, 2014
Heat shock protein 90 (HSP90), a molecular chaperone, plays important roles in cellular protection against various stressful stimuli and in the regulation of cellular growth and apoptosis.
Expression of tumor necrosis factor receptor-associated protein 1 and its clinical significance in kidney cancer.
Wang et al., Guangzhou, China. In Int J Clin Exp Pathol, 2014
OBJECTIVE: To investigate the expression and clinical significance of TRAP1 (tumor necrosis factor receptor-associated protein 1) in kidney cancer.
TRAP1 revisited: novel localizations and functions of a 'next-generation' biomarker (review).
Esposito et al., Reggio nell'Emilia, Italy. In Int J Oncol, 2014
In the last decade, the identification and characterization of novel molecular mechanisms and pathways involving the heat shock protein TRAP1/HSP75 in cancers and other diseases enhanced the scientific interest.
Mitochondrial oxidative phosphorylation TRAP(1)ped in tumor cells.
Picard et al., Padova, Italy. In Trends Cell Biol, 2014
Recently several independent groups identified tumor necrosis factor receptor-associated protein 1 (TRAP1), a mitochondrial molecular chaperone of the heat shock protein 90 (Hsp90) family, as a key modulator of mitochondrial respiration.
Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson's disease.
Papavassiliou et al., Athens, Greece. In Neuromolecular Med, 2014
The E3 ubiquitin ligase Parkin, the protease presenilin-associated rhomboid-like serine protease, the tyrosine kinase c-Abl, the protein kinase MARK2, the protease HtrA2, and the tumor necrosis factor receptor-associated protein 1 (TRAP1) provide different steps of control in protection against oxidative stress.
Inhibition of the mitochondrial Hsp90 chaperone network: a novel, efficient treatment strategy for cancer?
Siegelin, New York City, United States. In Cancer Lett, 2013
Among its distribution Hsp90 is also localized within mitochondria of neoplastic cells of various origin, interacting with another chaperone, TRAP1 (Tumor necrosis factor type 1 receptor-associated protein or Heat-shock-protein 75) to antagonize the cell death promoting properties of the matrix protein, Cyclophilin-D.
The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase.
Rasola et al., Padova, Italy. In Cell Metab, 2013
We report that the mitochondrial chaperone TRAP1, which is induced in most tumor types, is required for neoplastic growth and confers transforming potential to noncancerous cells.
PINK1 as a molecular checkpoint in the maintenance of mitochondrial function and integrity.
Chung et al., Pusan, South Korea. In Mol Cells, 2012
PINK1 also directly phosphorylates the mitochondrial proteins Miro and TRAP1, subsequently inhibiting mitochondrial transport and mitochondrial oxidative damage, respectively.
TRAP1 and the proteasome regulatory particle TBP7/Rpt3 interact in the endoplasmic reticulum and control cellular ubiquitination of specific mitochondrial proteins.
Esposito et al., Napoli, Italy. In Cell Death Differ, 2012
The proposed TRAP1 network has an impact in vivo, as it is conserved in human colorectal cancers, is controlled by ER-localized TRAP1 interacting with TBP7 and provides a novel model of the ER-mitochondria crosstalk.
The mitochondrial chaperone protein TRAP1 mitigates α-Synuclein toxicity.
Schulz et al., Aachen, Germany. In Plos Genet, 2012
alpha-Synuclein toxicity is intimately connected to mitochondrial dysfunction and that toxicity reduction in fly and rat primary neurons and human cell lines can be achieved using overexpression of the mitochondrial chaperone TRAP1
Conditional deletion of TGF-βR1 using Langerin-Cre mice results in Langerhans cell deficiency and reduced contact hypersensitivity.
Clausen et al., Rotterdam, Netherlands. In J Immunol, 2011
In the absence of Langerhans cells (LC), contact hypersensitivity (CHS) reactions in langerin-positive dendritic cell-specific TGF-betaR1-deficient mice are diminished, providing further evidence against a regulatory role for LC in CHS.
Mitochondrial TRAP1 regulates the unfolded protein response in the endoplasmic reticulum.
Tohyama et al., Suita, Japan. In Neurochem Int, 2011
Mitochondria could be a potential regulator of the unfolded protein response in the endoplasmic reticulum via mitochondrial TRAP1.
HSP75 protects against cardiac hypertrophy and fibrosis.
Lin et al., Wuhan, China. In J Cell Biochem, 2011
HSP75 likely reduces the hypertrophy and fibrosis induced by pressure overload through blocking TAK/P38, JNK, and AKT signaling pathways
Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network.
Altieri et al., Worcester, United States. In Cell, 2007
Molecular chaperones, especially members of the heat shock protein 90 (Hsp90) family, are thought to promote tumor cell survival, but this function is not well understood.
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