The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal.
TLDR
The pp60v-src-hsp90 complex is stabilized by sodium molybdate with the same concentration dependence as the glucocorticoid receptor-hSp90 complex, and as with the steroid receptor heterocomplexes, vanadate and tungstate also stabilize the pp60 v- src- hsp90 interaction.About:
This article is published in Journal of Biological Chemistry.The article was published on 1992-07-15 and is currently open access. It has received 51 citations till now. The article focuses on the topics: Vanadate & Sodium molybdate.read more
Citations
More filters
Journal ArticleDOI
The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins
D A Parsell,Susan Lindquist +1 more
TL;DR: The Lon Protease, DnaK.T URNOVER of AB ERR ANT PROT EINS in E. COLI, and more.
Journal ArticleDOI
Steroid receptor interactions with heat shock protein and immunophilin chaperones.
William B. Pratt,David O. Toft +1 more
TL;DR: A historical perspective on a body of steroid receptor research dealing with the structure and physiological significance of the untransformed 9S receptor is provided, and it is shown that hsp90 itself exists in a variety of native multiprotein heterocomplexes independent of steroid receptors and other 'substrate' proteins.
Journal ArticleDOI
The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
Journal ArticleDOI
The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
TL;DR: It is becoming clear that hsp90 chaperoning is not only essential to a variety of signal transduction pathways, but is critical for proper folding, stabilization, and trafficking of an expanding list of proteins.
Journal ArticleDOI
The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase.
TL;DR: The hsp90-based chaper one system has been reconstituted from purified components, permitting detailed analysis of the molecular basis of the chaperone's role in signal transduction.
References
More filters
Journal ArticleDOI
The heat shock response.
TL;DR: This review attempts to assess the available data concerning the homology of proteins in different species, the localization of the proteins in cells, and the relationship between heat shock proteins and thermoresistance.
Journal ArticleDOI
The common 90-kd protein component of non-transformed '8S' steroid receptors is a heat-shock protein.
Maria-Grazia Catelli,Nadine Binart,I Jung-Testas,J M Renoir,Etienne-Emile Baulieu,J R Feramisco,W J Welch +6 more
TL;DR: It is demonstrated that this ubiquitous BF4‐positive 90‐kd protein is in fact the chicken 90 kd heat‐shock protein (hsp 90): it increased in heat‐shocked chick embryo fibroblasts, and displayed identical migration in two‐dimensional gel electrophoresis and the same V8 peptide map as the already described hsp 90.
Journal ArticleDOI
Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.
TL;DR: It is shown that the 90-kDa receptor-associated phosphoprotein is an abundant cytosolic protein that reacts with a monoclonal antibody that recognizes the 90 -kDa phosphop protein that binds steroid receptors in the chicken oviduct.
Journal ArticleDOI
Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor.
TL;DR: It is proposed that hsp90 is necessary but not sufficient for maintaining a competent high affinity glucocorticoid-binding site, although the 27-kDa meroreceptor fragment is not itself sufficient for a competent binding site, it is sufficient when it is associated with hsp 90.
Journal ArticleDOI
The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins
TL;DR: Sera from rabbits bearing tumors induced by Rous sarcoma virus were previously found to contain antibody to the RSV transforming protein, pp60 src, but two additional transformation-specific phosphoproteins from RSV-transformed avian cells are immunoprecipitated with these sera.