@article{e4111170c99c41e7b31d3f22392462b2,
title = "Evidence for chaperone heterocomplexes containing both Hsp90 and VCP",
abstract = "With assistance from co-chaperone partner proteins, Hsp90 plays an essential positive role in supporting the structure and function of numerous client proteins in vivo. Hsp90's co-chaperone partnerships are believed to regulate and/or target its function. Here we describe associations between Hsp90 chaperone machinery and another chaperone, the 97-kDa valosin-containing protein VCP. Coimmunoadsorption assays indicate that VCP occurs in one or more native heterocomplexes containing Hsp90 and the Hsp90 partner proteins Cdc37, FKBP52, and p23. Functional characterizations indicate that VCP is not an Hsp90 substrate, but rather demonstrate the biochemical hallmarks of an Hsp90 co-chaperone. Potential roles for a collaboration between for Hsp90 and VCP are discussed.",
keywords = "Cdc37, Chaperone, FKBP52, Hsp90, VCP, Valosin, p23",
author = "Thomas Prince and Jieya Shao and Matts, {Robert L.} and Hartson, {Steven D.}",
note = "Funding Information: This work was supported by the National Institute of Environmental Health Science (ES011992 to S.D.H.), the National Institute of General Medicine (GM51608 to R.L.M.), and the Oklahoma Agricultural Experiment Station (Project 1975). The authors acknowledge contributions from web-based resources maintained by Dr. Didier Picard (University of Geneva, Switzerland) for tracking Hsp90 literature and Hsp90{\textquoteright}s protein associates ( http://www.picard.ch/downloads/downloads.htm ). The authors are grateful for generous antibody gifts from Dr. David Toft (Mayo Clinic, Rochester, MN) and Dr. David Smith (Mayo Clinic, Scottsdale, Arizona). Other antibodies were produced by Drs. Murali Bandela and Francisca Neethling (Hybridoma Center for the Agricultural and Biological Sciences, Oklahoma State University). The authors also acknowledge instrumentation and services provided by the Recombinant DNA/Protein Resource Facility at Oklahoma State University.",
year = "2005",
month = jun,
day = "17",
doi = "10.1016/j.bbrc.2005.04.047",
language = "English",
volume = "331",
pages = "1331--1337",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
number = "4",
}