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Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Open accessAbstract
Hsp90 is a protein chaperone whose functions are focused on a specific set of target proteins. The nature of Hsp90's interactions with these proteins is poorly understood. To provide tools for examining these interactions, we have isolated eight broadly distributed temperature-sensitive (ts) point mutations in the Hsp90 gene (HSP82) of Saccharomyces cerevisiae. The mutants fall into two distinct classes. One has a classic ts phenotype, with nearly wild-type activity at 25 degrees C and a precipitous loss of function at 34 degrees C. The remaining seven mutants, in contrast, cause a general reduction in Hsp90 function and are ts because they do not provide the high level of function required for growth at high temperatures. The effects of these mutants on two target proteins, a transcription factor (glucocorticoid receptor) and a tyrosine kinase (pp60v-src), provided several insights on Hsp90 function. First, Hsp90 is not only required to help the glucocorticoid receptor achieve a hormone-activable state, it is continuously required to maintain that state. Second, Hsp90's function in the maturation of pp60v-src involves separable roles in protein accumulation and kinase activation. Thus, Hsp90 is an integral component of both the steroid receptor and kinase signaling pathways. Finally, all eight point mutants affect the activation of both the glucocorticoid receptor and pp60v-src, indicating that Hsp90 promotes the activity of these very different target proteins through common mechanisms.
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“This explains why mutations at interface I on either Hsp90 (G333, K414, K418, K419)21–23 or Hsp70 (R171, N174, D213)24 led to defective Hsp90-Hsp70 interaction, growth defects and impaired client maturation of GR, v-Src and luciferase (Fig. 1d, e, Extended Data Fig. 4c–h; see Supplementary Table 3 for equivalent yeast residue numbering).”
From Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism (2022) · cites this paper as [21]
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“SHRs, including the glucocorticoid receptor (GR), are hormone-regulated transcription factors that depend on Hsp90 for function throughout their lifetimes5–10.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [9]
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“The glucocorticoid receptor (GR) is a model client that constantly depends on Hsp90 for activity4-9.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [9]
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“VP16 and pTCA/GAL4(1-93).”
BackgroundMethodInfluentialSequencing and De Novo Assembly of the Western Tarnished Plant Bug (Lygus hesperus) Transcriptome
Hull, J. J., Geib, S. M., Fabrick, J. A., & Brent, C. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055105 · Cited by 54
“Mutations that affect Hsp90 functionality or expression have been linked to impaired high temperature growth in both yeast and vertebrate cell cultures [59–61].”
BackgroundPost-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90
Sager, R., Woodford, M. R., Backe, S. J., Makedon, A. M., Baker-Williams, A. J., DiGregorio, B. T., Loiselle, D. R., Haystead, T., Zachara, N. E., Prodromou, C., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.018 · Cited by 54
“We next used another well-established Hsp90 kinase client, v-Src (Nathan and Lindquist, 1995).”
MethodHeat-induced Oligomerization of the Molecular Chaperone Hsp90
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“…reflect a variety of Hsp90-sensitive client interactions, we took advantage of a point mutation (T101I) in the Yok27 strain that reduces the ATPase activity of Hsc82 in vitro and renders yeast hypersensitive to radicicol and GA (Kimura et al., 1994; Nathan and Lindquist, 1995; Piper et al., 2003).”
BackgroundDifferential In Vivo Regulation of Steroid Hormone Receptor Activation by Cdc37p
Fliss, A., Fang, Y., Boschelli, F., & Caplan, A. J. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.12.2501 · Cited by 50
“The strain containing the hsp82 temperature-sensitive mutant was described previously (Nathan and Lindquist, 1995; Fang et al., 1996).”
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“Dimer 60 closure is the rate-limiting step for Hsp90 ATPase activity and mutations that either 61 subtly increase or decrease ATPase rates compromise viability in yeast (21, 22).”
BackgroundInfluentialEchtenkamp, F., Gvozdenov, Z., Adkins, N. L., Zhang, Y., Lynch-Day, M. A., Watanabe, S., Peterson, C. L., & Freeman, B. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.040 · Cited by 48
“892 Molecular Cell 64, 888–899, December 1, 2016 G170D, which inactivates in 5 min at temperatures > 37 C (Nathan and Lindquist, 1995).”
BackgroundMethodInfluentialSpecification of Physiologic and Disease States by Distinct Proteins and Protein Conformations
Jarosz, D. F., & Khurana, V. (2017) · Cell · doi:10.1016/j.cell.2017.10.047 · Cited by 46
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Interaction of steroid hormone receptors with transcription factors involves chromatin remodelling
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Hsp90 Mutants Disrupt Glucocorticoid Receptor Ligand Binding and Destabilize Aporeceptor Complexes
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Thrombin Receptor Signaling to Cytoskeleton Requires Hsp90
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A switch point in the molecular chaperone Hsp90 responding to client interaction
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MethodTruman, A. W., Kristjánsdóttir, K., Wolfgeher, D. J., Ricco, N., Mayampurath, A. M., Volchenboum, S. L., Clotet, J., & Kron, S. J. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.09.028 · Cited by 41
“Cells expressing Ssa1–45 or Hsp82G170D as the sole Ssa1 or Hsp82, respectively, display temperature sensitive (ts) growth [53, 54].”
BackgroundThe heat shock proteins: Their roles as multi-component machines for protein folding
Panaretou, B., & Zhai, C. (2008) · Fungal Biology Reviews · doi:10.1016/j.fbr.2009.04.002 · Cited by 42
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“Genetic studies of Saccharomyces cerevisiae have shown clearly that hsp90 is required for normal function of the glucocorticoid receptor (GR) (38, 40).”
BackgroundCaamaño, C. A., Morano, M. I., Dalman, F. C., Pratt, W. B., & Akil, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20473 · Cited by 40
Thermoregulation in the life cycle of nematodes
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Zuehlke, A. D., Reidy, M. J., Lin, C. P. C., LaPointe, P., Alsomairy, S., Lee, D. J., Rivera-Márquez, G. M., Beebe, K. E., Prince, T. L., Lee, S., et al. (2017) · Nature Communications · doi:10.1038/ncomms15328 · Cited by 38
“26).”
The Bacterial Hsp90 Chaperone: Cellular Functions and Mechanism of Action
Wickner, S., Nguyen, T.-L. L., & Genest, O. (2021) · Annual Review of Microbiology · doi:10.1146/annurev-micro-032421-035644 · Cited by 40
Heat shock proteins in cell signaling and cancer
Lang, B. J., Prince, T. L., Okusha, Y., Bunch, H., & Calderwood, S. K. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119187 · Cited by 39
A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand
Backe, S. J., Sager, R., Regan, B., Sit, J., Major, L., Bratslavsky, G., Woodford, M. R., Bourboulia, D., & Mollapour, M. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111039 · Cited by 40
“Our data show that expression of FNIP1 and FNIP2, individually and in combination, enhances the activity of the kinase clients v-Src (Nathan and Lindquist, 1995) and Slt2 (Truman et al., 2006) (measured by RLM1-lacZ reporter) (Figures 3A and 3B; Table S2).”
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
Rehn, A., Lawatscheck, J., Jokisch, M.-L., Mader, S. L., Luo, Q., Tippel, F., Blank, B., Richter, K., Lang, K., Kaila, V. R. I., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15048-8 · Cited by 38
Chaperoning STAT3/5 by Heat Shock Proteins: Interest of Their Targeting in Cancer Therapy
Jégo, G., Hermetet, F., Girodon, F., & Garrido, C. (2019) · Cancers · doi:10.3390/cancers12010021 · Cited by 38
“Accordingly, v-Src kinase activity depends strongly on HSP90 [74,94].”
Backgroundp50 Cdc37 Can Buffer the Temperature-Sensitive Properties of a Mutant of Hck
Scholz, G. M., Hartson, S. D., Cartledge, K., Hall, N. E., Shao, J., Dunn, A. R., & Matts, R. L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6984-6995.2000 · Cited by 38
“This Hsp90 mutant exhibits almost wild-type activity when the cells are grown at 25°C but displays significantly reduced activity at 34°C (34).”
BackgroundThe Molecular Chaperone Hsp90 Mediates Heme Activation of the Yeast Transcriptional Activator Hap1
Lee, H. C., Hon, T., & Li, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106951200 · Cited by 38
Aumais, J. P., Lee, H. S., Lin, R., & White, J. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.18.12229 · Cited by 37
Role of Chaperones in Nuclear Translocation
Heinlein, C. A., & Chang, C. (2001) · Endocrine · doi:10.1385/endo:14:2:143 · Cited by 37
Xu, Z., Pal, J. K., Thulasiraman, V., Hahn, H. P., Chen, J.-J., & Matts, R. L. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00461.x · Cited by 37
Hombach, A., Bartsch, K., Smirlis, D., Rosenqvist, H., MacDonald, A., Dingli, F., Loew, D., Späth, G. F., Rachidi, N., Wiese, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-41640-0 · Cited by 34
Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation
Biebl, M. M., Riedl, M., & Büchner, J. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108063 · Cited by 36
Armstrong, H., Wolmarans, A., Mercier, R., Mai, B., & LaPointe, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049322 · Cited by 36
“Of the Hsp82p mutants identified that confer ts phenotypes to yeast, only Hsp82p is thought to be thermolabile [34] and biochemical studies have confirmed that several of these Hsp82p mutants do not lose activity at elevated temperatures [22,37].”
BackgroundMethodInfluentialHjorth‐Sørensen, B., Hoffmann, E. R., Lissin, N. M., Sewell, A. K., & Jakobsen, B. K. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02279.x · Cited by 36
“In a Dhsc82Dhsp82 background, cells carrying hsp82, a temperature-sensitive allele of HSP82, exhibit growth arrest at 348C and die after a few hours' incubation (Nathan and Lindquist, 1995; Nathan et al., 1997).”
BackgroundFlom, G. A., Weekes, J., & Johnson, J. L. (2005) · Current Genetics · doi:10.1007/s00294-005-0580-6 · Cited by 34
“Plasmids Yep24-HSC82, Yep24-HSP82, pTGPD-Hsp82 and pTGPDHsp82-G313S were generous gifts of Susan Lindquist (Borkovich et al. 1989; Nathan and Lindquist 1995).”
BackgroundResultInfluentialHwang, D., Alevizos, I., Schmitt, W. A., Misra, J., Ohyama, H., Todd, R., Mahadevappa, M., Warrington, J. A., Stephanopoulos, G., Wong, D. T., et al. (2003) · Oral Oncology · doi:10.1016/s1368-8375(02)00108-2 · Cited by 34
“Hsp90 is essential for Raf function in vivo [31,32].”
BackgroundPullen, L., & Bolon, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.223131 · Cited by 32
Heterozygous Yeast Deletion Collection Screens Reveal Essential Targets of Hsp90
Franzosa, E. A., Albanèse, V., Frydman, J., Xia, Y., & McClellan, A. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028211 · Cited by 31
“To this end, ribosome profiling experiments were conducted with yeast containing either wild-type or T101I mutant Hsp90 [54].”
MethodMercier, R., Wolmarans, A., Schubert, J., Neuweiler, H., Johnson, J. L., & LaPointe, P. (2019) · Nature Communications · doi:10.1038/s41467-019-09299-3 · Cited by 31
Wang, L. (2004) · Microbiology · doi:10.1099/mic.0.27162-0 · Cited by 31
HSP90 Controls SIR2 Mediated Gene Silencing
Laskar, S., Bhattacharyya, M. K., Shankar, R., & Bhattacharyya, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023406 · Cited by 29
“episomaly in the cell [29].”
Bali, M., Zhang, B., Morano, K. A., & Michels, C. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309536200 · Cited by 30
Panaretou, B., SINCLAIR, K. E., Prodromou, C., Johal, J., Pearl, L. H., & Piper, P. W. (1999) · Microbiology · doi:10.1099/00221287-145-12-3455 · Cited by 30
“C. albicans Hsp90 is therefore fully functional with regard to its ability to participate in steroid responsive activation of mammalian GR protein expressed in S. cerevisiae, an activation that is strictly dependent on Hsp90 function (Caplan, 1997; Nathan & Lindquist, 1995; Pratt & Dittmar, 1998).”
BackgroundBipartite Role of Heat Shock Protein 90 (Hsp90) Keeps CRAF Kinase Poised for Activation
Mitra, S., Ghosh, B., Gayen, N., Roy, J., & Mandal, A. K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.746420 · Cited by 28
“Hsp90 yeast strains used were p82 (W3031A hsc82:: LEU2 hsp82::LEU2 HSP82::HIS3), G170D (W3031A hsc82::LEU2 hsp82::LEU2 hsp82, G170D::HIS3), and G313N (W303 1A hsc82::LEU2 hsp82::LEU2 hsp82, G313S::HIS3) (113).”
The role of HSP90 in evolution
Yahara, I. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00271.x · Cited by 29
“In addition, mutations induced in proteins which interact with HSP90-dependent proteins may also be suppressed via a buffering action of HSP90 through the potential for conformational flexibility exhibited by HSP90dependent proteins.”
BackgroundCooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling
Cox, M. B., & Miller, C. A. (2004) · Cell Stress and Chaperones · doi:10.1379/460.1 · Cited by 29
Yang, X.-X., Maurer, K. C. T., Molanus, M., Mager, W. H., Siderius, M. H., & van der Vies, S. M. (2006) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2006.00026.x · Cited by 28
“…hsp82T22I W303 1A hsc82::LEU2 hsp82::LEU2 hsp82,T22I::HIS3 Nathan & Lindquist (1995) hsp82A41V W303 1A hsc82::LEU2 hsp82::LEU2 hsp82,A41V::HIS3 Nathan & Lindquist (1995) hsp82G81S W303 1A hsc82::LEU2 hsp82::LEU2 hsp82,G81S::HIS3 Nathan & Lindquist (1995) hsp82T101I W303 1A hsc82::LEU2…”
BackgroundInfluentialMolecular mechanisms of chaperone‐directed protein folding: Insights from atomistic simulations
Castelli, M., Magni, A., Bonollo, G., Pavoni, S., Frigerio, F., Oliveira, A. S. F., Cinquini, F., Serapian, S. A., & Colombo, G. (2023) · Protein Science · doi:10.1002/pro.4880 · Cited by 28
“In this context, mutations at the Hsp90 NTD /Hsp70 NBD interface have been observed to impair client (GR, v-Src, and luciferase) maturation (Bohen & Yamamoto, 1993; Doyle et al., 2019; Genest et al., 2015; Kravats et al., 2018; Nathan & Lindquist, 1995).”
BackgroundWright, C. M., Fewell, S. W., Sullivan, M. L. G., Pipas, J. M., Watkins, S. C., & Brodsky, J. L. (2007) · Genetics · doi:10.1534/genetics.106.066274 · Cited by 27
“It is important to mention that the G170D and G313N mutations are in the Hsp82 ATPase domain and middle region, respectively (Nathan and Lindquist 1995; Fliss et al. 2000), and have been shown to affect protein stability and Hsp82p client protein activation (Bohen 1995; Lee et al. 2002; Youker et…”
BackgroundStress-mediated tuning of developmental robustness and plasticity in flies
Elgart, M., Snir, O., & Soen, Y. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.08.004 · Cited by 24
“Another remarkable example of an environmentally-regulated decanalization has been given by stress-induced suppression of Hsp90 [18], a chaperone that keeps many unstable signal transducers and developmental regulators poised for activation [55,56].”
BackgroundSuhane, T., Laskar, S., Advani, S., Roy, N., Varunan, S. M., Bhattacharyya, D., Bhattacharyya, S., & Bhattacharyya, M. K. (2014) · Eukaryotic Cell · doi:10.1128/ec.00159-14 · Cited by 26
“The temperature-sensitive iG170Dhsp82 strain (35) was used to investigate the effect of the abrogation of both Hsp82 and Hsc82 functions on DNA damage sensitivity.”
BackgroundMethodInfluentialMolecular Mechanisms of Clucocorticoid Resistance/Hypersensitivity: Potential Clinical Implications
Chrousos, G. P., de Castro, M., Leung, D. Y. M., Webster, E., Kino, T., Bamberger, C. M., Elliot, S. J., Stratakis, C. A., & Karl, M. (1996) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm/154.2_pt_2.s39 · Cited by 26
Heat shock and developmental expression of hsp83 in the filarial nematode Brugia pahangi
Thompson, F., Cockroft, A. C., Wheatley, I., Britton, C., & Devaney, E. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02525.x · Cited by 25
Neckers, L., Mimnaugh, E. G., & Schulte, T. W. (1999) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-58259-2_2 · Cited by 25
Glucose intake hampers PKA-regulated HSP90 chaperone activity
Chen, Y., Jiang, P.-H., Chen, H.-M., Chen, C., Wang, Y.-T., Chen, Y., Yu, C., & Teng, S. (2018) · eLife · doi:10.7554/elife.39925 · Cited by 21
TMEM127 suppresses tumor development by promoting RET ubiquitination, positioning, and degradation
Guo, Q., Cheng, Z., Gonzalez‐Cantu, H., Rotondi, M. L., Huelgas‐Morales, G., Ethiraj, P., Qiu, Z., Lefkowitz, J., Song, W., Landry, B. N., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113070 · Cited by 24
Surfome analysis of a wild-type wine Saccharomyces cerevisiae strain
Braconi, D., Amato, L., Bernardini, G., Arena, S., Orlandini, M., Scaloni, A., & Santucci, A. (2011) · Food Microbiology · doi:10.1016/j.fm.2011.04.009 · Cited by 24
“, 2009), whereas others provided evidences of an altered cell shape after mutations in rpl27a (Nathan and Lindquist, 1995), rpl3 (Rosado et al.”
BackgroundHorvat, N. K., Armstrong, H., Lee, B. L., Mercier, R., Wolmarans, A., Knowles, J., Spyracopoulos, L., & LaPointe, P. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.04.002 · Cited by 24
Steroid Hormone Receptors and Heat Shock Proteins
Gehring, U. (1998) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60925-5 · Cited by 24
No stress – Hsp90 and signal transduction inLeishmania
Hombach, A., & Clos, J. (2014) · Parasitology · doi:10.1017/s0031182013002151 · Cited by 24
“Hsp90-dependent client proteins play crucial roles in cellular signal transduction, cell cycle control and transcription regulation (Sanchez et al. 1987; Nathan and Lindquist, 1995; Buchner, 1999; Pratt and Toft, 2003).”
BackgroundGenetically recombinant antibodies: new therapeutics against candidiasis
Burnie, J., & Matthews, R. (2004) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.4.2.233 · Cited by 23
Folding and stability of the ligand‐binding domain of the glucocorticoid receptor
McLaughlin, S. H., & Jackson, S. (2002) · Protein Science · doi:10.1110/ps.5000102 · Cited by 23
“…for the glucocorticoid receptor to achieve a high-affinity ligand binding which is capable of activation, but it is continuously required to maintain that state (Picard et al. 1990; Nathan and Lindquist 1995; Nathan et al. 1997) as the receptor cycles between free and chaperone-bound states.”
BackgroundNichols, M., Rientjes, J. M. J., Logie, C., & Stewart, A. F. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.7.9944 · Cited by 23
Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase
Nardai, G., Schnaider, T., Sőti, C., Ryan, M. T., Høj, P. B., Somogyi, J., & Csermely, P. (1996) · Journal of Biosciences · doi:10.1007/bf02703107 · Cited by 22
Heat shock protein 90 in retinal ganglion cells: Association with axonally transported proteins
Bernstein, S. L., RUSSELL, P., WONG, P. W. K., Fishelevich, R., & Smith, L. E. H. (2001) · Visual Neuroscience · doi:10.1017/s0952523801183094 · Cited by 22
“HSP90 protein associations can also alter intracellular protein activation and function (Picard et al., 1990; Xu & Lindquist, 1993; Nathan & Lindquist, 1995).”
Backgroundα‐Complemented β‐galactosidase
Abbas‐Terki, T., & Picard, D. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00881.x · Cited by 22
Flom, G. A., Langner, E., & Johnson, J. L. (2012) · Current Genetics · doi:10.1007/s00294-012-0373-7 · Cited by 21
The Heat Shock Gene, htpG , and Thermotolerance in the Cyanobacterium, Synechocystis sp. PCC 6803
Fang, F., & Barnum, S. R. (2003) · Current Microbiology · doi:10.1007/s00284-002-4015-z · Cited by 21
“In eukaryotes, HSP90 has molecular chaperone activity, and plays a critical role in eukaryotic signal transduction [12, 16].”
BackgroundHsp70- and Hsp90-mediated proteasomal degradation underlies TPIsugarkill pathogenesis in Drosophila
Hrizo, S., & Palladino, M. J. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.08.011 · Cited by 21
Matsumoto, S., Tanaka, E., Nemoto, T., Ono, T., Takagi, T., Imai, J., Kimura, Y., Yahara, I., Kobayakawa, T., Ayuse, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203038200 · Cited by 21
Selection for robust metabolism in domesticated yeasts is driven by adaptation to Hsp90 stress
Patel, D., Amiji, H., Shropshire, W., Condic, N., Lermi, N. O., Sabha, Y., John, B., Hanson, B., & Karras, G. I. (2024) · Science · doi:10.1126/science.adi3048 · Cited by 20
Morita, T., Yamaguchi, H., Amagai, A., & Maeda, Y. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.10.010 · Cited by 20
Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding
Cox, M. B., & Johnson, J. L. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7477-1_28 · Cited by 21
HSP90α Gene Expression May Be a Conserved Feature of Vertebrate Somitogenesis
Sass, J. B., & Krone, P. H. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3572 · Cited by 20
Khurana, N., Laskar, S., Bhattacharyya, M. K., & Bhattacharyya, S. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-12-0867 · Cited by 19
“…shows that glycine at position 170 occupies a conformationally restricted position (Prodromou et al., 1997), and mutation of glycine to aspartic acid completely destabilizes the structure of Hsp90 and results in complete loss of function at nonpermissive temperature (Nathan and Lindquist, 1995).”
Influential
Metadata
- Authors
- Nathan, D. F., & Lindquist, S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Lindquist, Susan
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1995-07
- Volume
- 15
- Issue
- 7
- Pages
- 3917-3925
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC230631
- OpenAlex
- W2101287778
- Cited by
- 423
- References
- 56
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 8 · 2023: 7 · 2022: 7 · 2021: 12 · 2020: 14 · 2019: 14 · 2018: 9 · 2017: 8 · 2016: 11 · 2015: 5 · 2014: 14 · 2013: 11 · 2012: 15
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (5f32gm014745-03)
- National Institute of General Medical Sciences (GM14745-02)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- HSP90, temperature-sensitive mutants, glucocorticoid receptor, pp60v-src, tyrosine kinase, steroid receptor signaling, kinase activation, Saccharomyces cerevisiae
- MeSH terms
- DNA Mutational Analysis, Hot Temperature, Heat-Shock Proteins, Phenotype, Protein Binding, Receptors, Glucocorticoid, Saccharomyces cerevisiae, Oncogene Protein pp60(v-src), Point Mutation, HSP90 Heat-Shock Proteins, Saccharomyces cerevisiae Proteins
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