Novel Subunits of the Mammalian Hsp90 Signal Transduction Chaperone
- 10 March 2007
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Proteome Research
- Vol. 6 (5), 1963-1973
- https://doi.org/10.1021/pr060595i
Abstract
As one of the major cellular chaperones, Hsp90 plays diverse roles in supporting and regulating wild-type and oncogenic signal transduction proteins. Hsp90 function itself is regulated by its various nonsubstrate subunits. To define Hsp90's predominant in vivo functions and the mechanisms for regulating this function, the human Hsp90 interactome was characterized using gel-based proteomics techniques. Results show that Hsp90's most prominent association is its previously described interaction with Hsp70, a primary chaperone capable of recognizing and binding hydrophobic peptide segments. Additionally, novel human proteins discovered in this study reveal that several newly described Hsp90 associations in yeast are conserved in the human cytoplasm. Additionally, other new Hsp90 subunits imply that a great deal of Hsp90 function may be directed to the assembly, regulation, or exploitation of the tubulin-based cytoskeleton network, particularly the mitotic spindle. Keywords: Hsp90 • co-chaperone • interactome • NudC • Sgt1 • Pih1 • TPR • immunophilinThis publication has 50 references indexed in Scilit:
- Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrestExperimental Cell Research, 2006
- 17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferationOncogene, 2006
- A proteomic snapshot of the human heat shock protein 90 interactomeFEBS Letters, 2005
- Characterization of Saccharomyces cerevisiae Nop17p, a Novel Nop58p-Interacting Protein that is Involved in Pre-rRNA ProcessingJournal of Molecular Biology, 2005
- Rvb1p/Rvb2p Recruit Arp5p and Assemble a Functional Ino80 Chromatin Remodeling ComplexMolecular Cell, 2004
- Pathways of chaperone-mediated protein folding in the cytosolNature Reviews Molecular Cell Biology, 2004
- Functional proteomic screens reveal an essential extracellular role for hsp90α in cancer cell invasivenessNature, 2004
- Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approachCell Stress and Chaperones, 2004
- Identification of Tetratricopeptide Repeat 1 as an Adaptor Protein That Interacts with Heterotrimeric G Proteins and the Small GTPase RasMolecular and Cellular Biology, 2003
- Identification and Characterization of the Ubiquitously Occurring Nuclear Matrix Protein NMP 238Biochemical and Biophysical Research Communications, 1998