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Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
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During or immediately after synthesis in vertebrate cells, the oncogenic protein-tyrosine kinase pp60v-src associates with the approximately 90-kDa heat-shock protein (hsp90). In this complex, pp60v-src is not functional as a kinase. When pp60v-src is subsequently found inserted into the plasma membrane, it is active as a kinase and is no longer associated with hsp90. We have taken advantage of genetic manipulations possible in Saccharomyces cerevisiae to investigate the function and specificity of the association between hsp90 and pp60v-src. Expression of pp60v-src is known to be toxic to S. cerevisiae cells. We find that this toxicity is due to a very specific effect on growth, arrest at a particular point in the cell cycle. In cells expressing v-src, a mutation that lowers the level of hsp90 expression (i) relieves cell cycle arrest and rescues growth, (ii) reduces the level of tyrosine phosphorylation mediated by pp60v-src, (iii) changes the pattern of tyrosine phosphorylation, and (iv) reduces the concentration of pp60v-src. We conclude that hsp90 does not simply suppress pp60v-src kinase activity during transit to the plasma membrane, as previously suggested, but also stabilizes the protein and affects both its activity and specificity. This function of hsp90 is highly selective for pp60v-src: the same hsp90 mutation has no effect on the activity or specificity of the exogenous pp160v-abl tyrosine kinase; similarly, it does not affect the specificity and has only a very small effect on the activity of the exogenous pp60c-src kinase.
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“This role as a potentiator for genetic variation has been observed in fungi as well as mammalian cancer cells20,88,135,136.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [136]
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“Second, Hsp90 can enable the phenotypic effects of new mutations either by stabilizing mutant regulators or by stabilizing non-mutant regulators that mediate signalling required for adaptation.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [136]
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The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
Wandinger, S. K., Suhre, M. H., Wegele, H., & Büchner, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600930 · Cited by 160
“their active state (Xu and Lindquist, 1993; Nathan and Lindquist, 1995; Nathan et al, 1997).”
BackgroundConservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae.
Chang, H.-C., & Lindquist, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31486-2 · Cited by 158
Self-citationTumor Selectivity of Hsp90 Inhibitors: The Explanation Remains Elusive
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Molecular chaperones: The busy life of Hsp90
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“v-Src and c-Src require Hsp90 for maturation of their catalytic activity, and c-Src also needs Hsp90 in order to be a substrate for the regulatory kinase Csk [11,12].”
SBA1 Encodes a Yeast Hsp90 Cochaperone That Is Homologous to Vertebrate p23 Proteins
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Inhibition of Hsp90: a new strategy for inhibiting protein kinases
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“v-Src, c-Src [51] v-Fes, c-Fes, v-Fps, v-Ros, v-Yes Lck, v-Fgr, c-Fgr v-Abl, c-Abl [52,53] Wee1 [56,57] Sevenless c-Met [58] p75-v-erbA p185erbB2 [50] Insulin, ILGF, EGF, PDGF receptors”
BackgroundThe Plasticity of the Hsp90 Co-chaperone System
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“Hsp90 is thought to direct the folding of Src kinases into the inactive conformation, which prevents their degradation (Xu and Lindquist, 1993; Xu et al., 1999).”
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The heat shock protein 83 (Hsp83) is required for Raf‐mediated signalling in Drosophila
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“…Raf This spatial restriction can be overcome either by ectopicand casein kinase II (Miyata and Yahara, 1992; Stancato expression of Boss or by direct activation of Sev in theet al., 1993; Xu and Lindquist, 1993; Wartmann and Davis, cone cell precursors (Basler et al., 1991; Van Vactor et al.,1994).”
BackgroundHormone-dependent Transactivation by the Human Androgen Receptor Is Regulated by a dnaJ Protein
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Hsp90 modulates the stability of MLKL and is required for TNF-induced necroptosis
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“Hsp90 has been implicated in the stabilization of a number of kinases, including pp60v-src and Raf-1.(18,19) Loss of Hsp90 function results in their destabilization and rapid degradation by the ubiquitin–proteasome pathway.”
BackgroundThe Yeast Hsp110 Family Member, Sse1, Is an Hsp90 Cochaperone
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The Turn Motif Is a Phosphorylation Switch That Regulates the Binding of Hsp70 to Protein Kinase C
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Morano, K. A., & Thiele, D. J. (1999) · Europe PMC (PubMed Central) · Cited by 134
Physical Interaction of Mammalian CDC37 with CDK4
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Metadata
- Authors
- Xu, Y., & Lindquist, S.
- Affiliations
- University of Chicago (US)
- Howard Hughes Medical Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1993-08
- Volume
- 90
- Issue
- 15
- Pages
- 7074-7078
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC47078
- OpenAlex
- W2085643470
- Cited by
- 416
- References
- 33
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 10 · 2023: 7 · 2022: 2 · 2021: 5 · 2020: 5 · 2019: 11 · 2018: 11 · 2017: 13 · 2016: 10 · 2015: 5 · 2014: 14 · 2013: 5 · 2012: 12
- FWCI
- 5.67
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Chicago
- National Institutes of Health
- National Institute of General Medical Sciences (GM-25874)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- HSP90, pp60v-src, tyrosine kinase, kinase activation, protein stability, cell cycle arrest, tyrosine phosphorylation, oncogenic kinase, Src kinase, Saccharomyces cerevisiae, kinase specificity
- MeSH terms
- Cell Cycle, Chromosome Deletion, Genes, Fungal, Heat-Shock Proteins, Phosphoproteins, Recombinant Proteins, Saccharomyces cerevisiae, Tyrosine, Oncogene Protein pp60(v-src), Gene Expression, Mutagenesis, Insertional, Oncogene Proteins v-abl, Proto-Oncogene Proteins pp60(c-src), Phosphotyrosine
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