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Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
Open accessAbstract
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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“Apart from this early landmark study and related studies in yeast during the same period (33, 34), there had been limited in vitro and in vivo studies that support existence”
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“These mostly regulatory proteins include telomerase, nitric oxide synthase and various transcription factors such as p53 (Abravaya et al., 1992; Xu & Lindquist, 1993; Kosano et al., 1998; Whitesell et al., 1998; Sato et al., 2001).”
BackgroundMichail, X., Kontogiannatos, D., Syriou, V., & Kourti, A. (2012) · Ecotoxicology · doi:10.1007/s10646-012-0980-6 · Cited by 13
Yan, F., Liu, X., Zhang, S., Zhang, Q., & Chen, J. (2019) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13623 · Cited by 12
“…development of the new state in a different way and release the chaotic kinase activity to promote carcinogenesis, rather than hindering the impact of new mutations in cancer cells (Fabio Falsone, Leptihn, Osterauer, Haslbeck, & Buchner, 2004; Xu & Lindquist, 1993; Xu, Singer, & Lindquist, 1999).”
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“In vivo studies revealed that HSP90 functions as a molecular chaperone for specific substrate proteins, the classical examples being steroid hormone receptors and signaling protein kinases (Picard et al., 1990; Xu and Lindquist, 1993).”
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“Yeast Hsp90 is 60% identical to the human isoform Hsp90α and has been used as a model to investigate Hsp90 dependence of human Src variants (Boczek et al., 2015; Chen et al., 2006; Xu & Lindquist, 1993).”
MethodEvidence for interaction between Hsp90 and the ER membrane complex
Kudze, T., Mendez‐Dorantes, C., Jalloh, S., & McClellan, A. J. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0908-z · Cited by 12
The muscle-specific chaperone protein melusin is a potent cardioprotective agent
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“Nascent v-Src is found in a highmolecular-weight complex consisting of Hsp90, Hsp70, Hsp40, Cdc37, Sti1 (Hop1), Aha1, among others (Dey et al. 1996a, b; Kimura et al. 1995, 1997; Chang et al. 1997; Xu and Lindquist 1993; Lotz et al. 2003).”
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“…kinase v-SRC leads to toxicity in yeast (Brugge et al, 1987; Kornbluth et al, 1987) — an established result that has been replicated several times (Xu and Lindquist, 1993; Boschelli et al, 1993; Florio et al, 1994; Trager and Martin, 1997) and demonstrated in the fi ssion yeast Schizosaccharomyces…”
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“And SRC is a client of Hsp90 18,19 (Figure 6A).”
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Steroid Hormone Receptor Families
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“To ensure that the variation in expression profiles was not caused by different sensitivities to GdA in different strains, we assayed the Hsp90 activity by measuring the kinase activity of v-Src, a well-known Hsp90 client (Xu and Lindquist 1993), with or without GdA treatments (Supplemental Fig.”
MethodHuo, Y., Karnawat, R., Liu, L., Knieß, R. A., Groß, M., Chen, X., & Mayer, M. P. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168772 · Cited by 5
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“…of Hsps regulate the activity of signaling proteins including a number of protein kinases, NO synthetase, and several transcription factors (Neupert et al. 1990; Abravaya et al. 1992; Xu and Lindquist 1993; Melnick and Argon 1995; Whitesell et al. 1998; Hartl et al. 2011; Kumar et al. 2022).”
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BackgroundSobich, J., Wrońska, A. K., Kaczmarek, A., & Boguś, M. I. (2023) · The European Zoological Journal · doi:10.1080/24750263.2023.2276353 · Cited by 4
“In normal conditions, D. melanogaster HSF and vertebrate HSF1 occur as monomers in complex with Hsp90 in the cell, like many other transcription factors whose activity is regulated with similar chaperones (Abravaya et al. 1992; Xu & Lindquist 1993; Whitesell et al. 1998; Kosano et al. 1998).”
BackgroundCoumailleau, P., Bonnanfant‐Jais, M., Lainé, M., & Angelier, N. (1997) · Development Genes and Evolution · doi:10.1007/s004270050069 · Cited by 4
“... 1993; Bohen and Yamamoto 1994), basic helix-loop-helix (bHLH) transcription factors (Shaknovich et al. 1992; Hankinson 1995; Mc Guire et al. 1995), tubulin (Sanchez et al. 1988), actin (Koyasu et al. 1986), calmodulin (Nishida et al. 1986), normal cellular serine/threonine kinases (Matts and Hurst 1989; Walker et…”
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(2014) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608058624114010009 · Cited by 4
“Hsp90 functions in protein folding, aggregation inhibition, transcriptional regulation, signal transduction, and facilitation in transportation [27-31].”
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Morimoto, R. I., & Nollen, E. A. A. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50672-0 · Cited by 4
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Nollen, E. A. A., & Morimoto, R. I. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm1261 · Cited by 3
HSP90 buffers newly induced mutations in massively mutated plant linesPreprint
Mason, G. A., Carlson, K. D., Press, M. O., Bubb, K. L., & Queitsch, C. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/355735 · Cited by 3
“Similarly, recurrent HSP90dependent variants in oncogenes are highly sequence-specific and rare (60, 64-66).”
BackgroundA stress response that allows highly mutated eukaryotic cells to survive and proliferatePreprint
Zabinsky, R. A., Mares, J., She, R., Zeman, M. K., Silvers, T. R., & Jarosz, D. F. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/515460 · Cited by 2
“To assess Hsp90 activity in the MA lineages, we measured the activity of the Hsp90-dependent tyrosine kinase v-Src from the transforming Rous Sarcoma Virus (Xu and Lindquist, 1993; Zabinsky et al., 2018).”
BackgroundMethodA fluorescence‐based sensor for calibrated measurement of protein kinase stability in live cells
Paul, J. W., Muratcioğlu, S., & Kuriyan, J. (2024) · Protein Science · doi:10.1002/pro.5023 · Cited by 2
“Experiments in yeast revealed that two conserved chaperones, heat shock protein 90 (HSP90) and a co-chaperone, cell division cycle protein 37 (CDC37), bind to and preserve the activity of oncogenic v-Src, expressed heterologously in yeast, but do not bind to c-Src (Xu & Lindquist, 1993).”
BackgroundHsp70-Hsp90 organising protein (HOP/STIP1) is required for KSHV lytic replication
Kirigin, E., Okpara, M. O., Matandirotya, L., Ruck, J.-L., Weaver, F., Jackson, Z., Chakraborty, A., Veale, C. G. L., Whitehouse, A., & Edkins, A. L. (2024) · Journal of General Virology · doi:10.1099/jgv.0.002053 · Cited by 5
“Examples from viral host protein mimics demonstrate that viral proteins are often more sensitive to perturbations in proteostasis than host proteins [67].”
Chaperones in the Morphogenesis of Viruses
Mayer, M. P. (2009) · Heat shock proteins · doi:10.1007/978-90-481-2976-8_4 · Cited by 2
“Examples supporting this hypothesis are found in the field of oncology: the oncogenic viral Src kinase is more dependent on Hsp90 than its cellular counterpart [ 98 ] and many oncogenic mutant proteins including ErbB2, Her2, Bcl-Abl, Raf variants, dominant negative p53 variants, are dependent on Hsp70 and Hsp90 [99, 1…”
BackgroundRole of HSP60 in Steroidogenesis and Reproduction
Olvera-Sánchez, S., Monreal‐Flores, J., Flores-Herrera, Ó., & Martı́nez, F. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23154-5_20 · Cited by 2
Heat Shock Proteins and the Regulation of Heat Shock Gene Expression in Eukaryotes
Kabakov, A. E., & Gabai, V. L. (1997) · Springer eBooks · doi:10.1007/978-1-4615-6007-4_1 · Cited by 2
Garbuz, D. G., & Evgen’ev, M. B. (2017) · Генетика · doi:10.7868/s0016675817010064 · Cited by 2
The Pivotal Role of CK2 in the Kinome‐Targeting Hsp90 Chaperone Machinery
Miyata, Y. (2013) · doi:10.1002/9781118482490.ch7 · Cited by 2
Immunomodulation by Endogenous Stress Response Proteins
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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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