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An acetylation site in the middle domain of Hsp90 regulates chaperone function.
The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties*
- S. Felts, B. Owen, P. Nguyen, J. Trepel, D. Donner, D. Toft
- BiologyJournal of Biological Chemistry
- 4 February 2000
TRAP1 has functions that are distinct from those of hsp90, and immunofluorescence data show that human TRAP1 is localized to mitochondria, supported by the existence of mitochondrial localization sequences in the amino termini of both the human and Drosophila proteins.
Chaperoning Checkpoint Kinase 1 (Chk1), an Hsp90 Client, with Purified Chaperones*
- Sonnet J. H. Arlander, S. Felts, J. Wagner, B. Stensgard, D. Toft, L. Karnitz
- Biology, Computer ScienceJournal of Biological Chemistry
- 3 February 2006
New insights are provided into Hsp90-dependent chaperoning of a client kinase and a novel, biochemically tractable model system is identified that will be useful to further dissect the HSp90- dependent chaperoned of this important and ubiquitous class of Hsp 90 clients.
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies.
The findings suggest that p23 functions at one or more late steps in IR-mediated signal transduction, perhaps including receptor recycling and/or reversal of the response.
A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion
Data indicate that cell surface H Sp90 plays an important role in modulating cancer cell migration that is independent of the function of the intracellular Hsp90 pool, and that small molecule inhibitors of surface HSp90 may provide a new approach to targeting the metastatic phenotype.
Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer.
It is discovered that small-cell lung carcinoma is a distinctive cellular system in which apoptosis is mainly regulated by Hsp90, and this results provide important evidence for a transformation-specific interplay between chaperones in regulating apoptosis in malignant cells.
Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone*
- A. J. Weaver, W. Sullivan, S. Felts, B. Owen, D. Toft
- BiologyThe Journal of Biological Chemistry
- 28 July 2000
A crystal structure of human p23 lacking 35 residues at the COOH terminus is solved and the structure reveals a disulfide-linked dimer with each subunit containing eight β-strands in a compact antiparallel β-sandwich fold.
GCUNC-45 Is a Novel Regulator for the Progesterone Receptor/hsp90 Chaperoning Pathway
Overexpression and knockdown experiments show GCUNC-45 to be a positive factor in promoting PR function in the cell, and a new cochaperone binding site near the N terminus of hsp90 is revealed, adding insight on the role of FKBP52.
p23, a simple protein with complex activities
Abstract p23 is a small but important cochaperone for the Hsp90 chaperoning pathway. It appears to facilitate the adenosine triphosphate–driven cycle of Hsp90 binding to client proteins. It enters at…
Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones.
The radicicol-binding site appears to be specific to and is conserved in all members of the Hsp90 family of molecular chaperones from bacteria to mammals, but is not present in other molecular chapers with nucleotide-binding domains.