Cited by 416Heat shock proteins researchProtein Kinase Regulation and GTPase SignalingCancer-related Molecular Pathways

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

Heat-shock protein hsp90 governs the activity of pp60v-src kinase.

Open access

Xu, Y, Lindquist, S·1993·Proceedings of the National Academy of Sciences

Open this paper in CoChat — free account

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1073/pnas.90.15.7074

Cites

34 of 34 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Transformation of intact yeast cells treated with alkali cations
Ito, H., Fukuda, Y., Murata, K., & Kimura, A. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.163-168.1983 · Cited by 7,518
THE HEAT-SHOCK PROTEINS
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,304
Self-citation
[12] One-step gene disruption in yeast
Rothstein, R. J. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)01015-0 · Cited by 3,282
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
Koch, C. A., Anderson, D. H., Moran, M. F., Ellis, C. A., & Pawson, T. J. (1991) · Science · doi:10.1126/science.1708916 · Cited by 1,868
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787
Self-citation
hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.
Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
Self-citation
Steroid receptors and their associated proteins
Smith, D. F., & Toft, D. O. (1993) · Molecular Endocrinology · doi:10.1210/mend.7.1.8446107 · Cited by 549
Peptides and Protein Phosphorylation
Kemp, B. E. (2018) · CRC Press eBooks · doi:10.1201/9781351075442 · Cited by 522
Hsp90 chaperones protein folding in vitro
Wiech, H., Büchner, J., Zimmermann, R., & Jakob, U. (1992) · Nature · doi:10.1038/358169a0 · Cited by 505
Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses
Lipsich, L. A., Lewis, A., & Brugge, J. S. (1983) · Journal of Virology · doi:10.1128/jvi.48.2.352-360.1983 · Cited by 494

Flagged first, then by citations

Show all 33 references

Research works printed but not linked: 4

[3]Shilo, B. Z. & Weinberg, R. A. (1981) Proc. Natl. Acad. Sci. USA 78, 6789–6792.
[8]Iba, H., Takeya, T., Cross, F. R., Hanafusa, T. & Hanafusa, H. (1984) Proc. Natl. Acad. Sci. USA 81, 4424–4428.
[13]Oppermann, H., Levinson, W. & Bishop, J. M. (1981) Proc. Natl. Acad. Sci. USA 78, 1067–1071.
[24]Kornbluth, S., Jove, R. & Hanafusa, H. (1987) Proc. Natl. Acad. Sci. USA 84, 4455–4459.

Sorted by citations

Items 201–300 of 416

Oncogenic Mutations Reduce the Stability of Src Kinase
Falsone, S. F., Leptihn, S., Osterauer, A., Haslbeck, M., & Büchner, J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.091 · Cited by 51
28-kDa Mammalian Heat Shock Protein, a Novel Substrate of a Growth Regulatory Protease Involved in Differentiation of Human Leukemia Cells
Spector, N. L., Hardy, L., Ryan, C., Miller, W. H., Humes, J. L., Nadler, L. M., & Luedke, E. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1003 · Cited by 51
Hsp90 is essential in the filarial nematode Brugia pahangi
Devaney, E., O’Neill, K., Harnett, W., Whitesell, L. J., & Kinnaird, J. H. (2005) · International Journal for Parasitology · doi:10.1016/j.ijpara.2005.01.007 · Cited by 50
Suppression of v-Src Transformation by Andrographolide via Degradation of the v-Src Protein and Attenuation of the Erk Signaling Pathway
Liang, F.-P., Lin, C., Kuo, C., Chao, H., & Fu, S.-L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705877200 · Cited by 50
Hsp90 Nuclear Accumulation in Quiescence Is Linked to Chaperone Function and Spore Development in Yeast
Tapia, H., & Morano, K. A. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-05-0376 · Cited by 50
“We tested these two scenarios by assaying the ability of hsp82-I578F to support activation and function of the mammalian Hsp90 client tyrosine kinase v-Src in yeast (Xu and Lindquist, 1993).”
BackgroundMethodInfluential
Degradation of Heterotrimeric Gαo Subunits via the Proteosome Pathway Is Induced by the hsp90-specific Compound Geldanamycin
Busconi, L., Guan, J., & Denker, B. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.1565 · Cited by 50
Clustered cysteine residues in the kinase domain of v-Src: critical role for protein stability, cell transformation and sensitivity to herbimycin A
Senga, T., Miyazaki, K., Machida, K., Iwata, H., Matsuda, S., Nakashima, I., & Hamaguchi, M. (2000) · Oncogene · doi:10.1038/sj.onc.1203296 · Cited by 49
“Fifth, herbimycin A inhibited the complex formation of v-Src with HSP90 (Whitesell et al., 1994) which seemed to govern v-Src activity in yeast-system (Xu and Lindquist, 1993).”
Background
Modular Folding and Evidence for Phosphorylation-induced Stabilization of an hsp90-dependent Kinase
Hartson, S. D., Ottinger, E. A., Huang, W., Bárány, G., Burn, P., & Matts, R. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.14.8475 · Cited by 48
Expression of the Hsp83 gene in response to diapause and thermal stress in the moth Sesamia nonagrioides
Gkouvitsas, T., Kontogiannatos, D., & Kourti, A. (2009) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2009.00922.x · Cited by 48
“Hsp90s are distinguished from other chaperones in that most of the known substrates are signal transduction proteins, the classical examples being steroid hormone receptors and signaling kinases (Picard et al., 1990; Xu & Lindquist, 1993).”
Background
Ligand Binding, Unbinding, and Allosteric Effects: Deciphering Small-Molecule Modulation of HSP90
D’Annessa, I., Raniolo, S., Limongelli, V., Marino, D. D., & Colombo, G. (2019) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.9b00319 · Cited by 48
Protein stability and degradation in health and disease
Clausen, L., Abildgaard, A. B., Gersing, S. K., Stein, A., Lindorff‐Larsen, K., & Hartmann‐Petersen, R. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.09.002 · Cited by 56
Hyperthermia-induced HSP expression correlates with improved rat renal isograft viability and survival in kidneys harvested from non-heart-beating donors
Redaelli, C., Wagner, M., Kulli, C., Tian, Y., Kubulus, D., Mazzucchelli, L., Wagner, A. C. C., & Schilling, M. K. (2001) · Transplant International · doi:10.1007/s001470100000 · Cited by 47
Synergistic interaction between 17‐AAG and phosphatidylinositol 3‐kinase inhibition in human malignant glioma cells
Premkumar, D. R., Arnold, B. A., Jane, E. P., & Pollack, I. F. (2005) · Molecular Carcinogenesis · doi:10.1002/mc.20152 · Cited by 47
Reappraisal of the Role of Heat Shock Proteins as Regulators of Steroid Receptor Activity
Ylikomi, T. J., Wurtz, J., Syvälä, H., Passinen, S., Pekki, A., Haverinen, M., Bläuer, M., Tuohimaa, P., & Gronemeyer, H. (1998) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409239891204279 · Cited by 45
Induction of heat-shock (stress) protein gene expression by selected natural and anthropogenic disturbances in the octocoral Dendronephthya klunzingeri
Wiens, M., Ammar, M. S. A., Nawar, A. H., Koziol, C., Hassanein, H. M. A., Eisinger, M., Müller, I. M., & Müller, W. E. G. (2000) · Journal of Experimental Marine Biology and Ecology · doi:10.1016/s0022-0981(99)00167-7 · Cited by 45
Hsp90 Mutants Disrupt Glucocorticoid Receptor Ligand Binding and Destabilize Aporeceptor Complexes
Bohen, S. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.49.29433 · Cited by 45
Overexpression of HSP-70 Attenuates Increases in [Ca2+]iand Protects Human Epidermoid A-431 Cells after Chemical Hypoxia
Kiang, J. G., Ding, X. Z., & McClain, D. E. (1998) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1997.8364 · Cited by 45
Thrombin Receptor Signaling to Cytoskeleton Requires Hsp90
Pai, K. S., Mahajan, V. B., Lau, A., & Cunningham, D. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104212200 · Cited by 45
Cell cycle control by daf‐21/Hsp90 at the first meiotic prophase/metaphase boundary during oogenesis in Caenorhabditis elegans
Inoue, T., Hirata, K., Kuwana, Y., Fujita, M., Miwa, J., Roy, R., & Yamaguchi, Y. (2006) · Development Growth & Differentiation · doi:10.1111/j.1440-169x.2006.00841.x · Cited by 44
Hrp12, a novel heat-responsive, tissue-specific, phosphorylated protein isolated from mouse liver
Samuel, S. J., Tzung, S.-P., & Cohen, S. A. (1997) · Hepatology · doi:10.1002/hep.510250525 · Cited by 44
Heat induced stress proteins and the concept of molecular chaperones
Forreiter, C., & Nover, L. (1998) · Journal of Biosciences · doi:10.1007/bf02936122 · Cited by 44
Progress and prospects for targeting Hsp90 to treat fungal infections
Veri, A. O., & Cowen, L. E. (2014) · Parasitology · doi:10.1017/s0031182013002072 · Cited by 46
“For example, oncogenic mutations in the cellular Src tyrosine kinase (c-Src) often involve truncation of the inhibitory domain, rendering the mutant v-Src protein hyperactive and contingent upon Hsp90 for stability and function (Xu and Lindquist, 1993; Xu et al. 1999; Falsone et al. 2004).”
Background
Heat shock protein 90 inhibitor 17‐allylamino‐17‐demethoxygeldanamycin potentiates the radiation response of tumor cells grown as monolayer cultures and spheroids by inducing apoptosis
Machida, H., Nakajima, S., Shikano, N., Nishio, J., Okada, S., Asayama, M., Shirai, M., & Kubota, N. (2005) · Cancer Science · doi:10.1111/j.1349-7006.2005.00125.x · Cited by 43
The Identification of Wos2, a p23 Homologue That Interacts With Wee1 and Cdc2 in the Mitotic Control of Fission Yeasts
Muñoz, M. J., Bejarano, E. R., Daga, R. R., & Jiménez, J. (1999) · Genetics · doi:10.1093/genetics/153.4.1561 · Cited by 43
Hsp90
Jarosz, D. F. (2015) · Advances in cancer research · doi:10.1016/bs.acr.2015.11.001 · Cited by 41
Регуляция экспрессии генов теплового шока в ответ на стрессовые воздействия, "Молекулярная биология"
Garbuz, D. G. (2017) · Molecular Biology · doi:10.7868/s0026898417020100 · Cited by 42
Involvement of human heat shock protein 90α in nicotine‐induced apoptosis
Wu, Y., Kita, K., & Suzuki, N. (2002) · International Journal of Cancer · doi:10.1002/ijc.10449 · Cited by 42
Heat-shock proteins and platelet function
Polanowska‐Grabowska, R. (2000) · Platelets · doi:10.1080/09537100075742 · Cited by 42
Aldosterone rapidly activates Src kinase in M‐1 cells involving the mineralocorticoid receptor and HSP84
Braun, S., Lösel, R., Wehling, M., & Boldyreff, B. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.06.031 · Cited by 42
Environmental Adaptations: Desiccation Tolerance
Schill, R. O., & Hengherr, S. (2018) · Zoological monographs · doi:10.1007/978-3-319-95702-9_10 · Cited by 42
Andrographolide downregulates the v-Src and Bcr-Abl oncoproteins and induces Hsp90 cleavage in the ROS-dependent suppression of cancer malignancy
Liu, S.-H., Lin, C., Liang, F.-P., Chen, P., Kuo, C., Alam, M. M., Maiti, B., Hung, S., Chi, C., Sun, C., et al. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.10.014 · Cited by 42
“essential for the maturation and stability of the v-Src oncoprotein and therefore for sustaining v-Src-mediated cellular transformation [13–15].”
BackgroundResult
Opposite effects of the Hsp90 inhibitor Geldanamycin: induction of apoptosis in PC12, and differentiation in N2A cells
López-Maderuelo, D., Fernández-Renart, M., Moratilla, C., & Renart, J. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02130-5 · Cited by 40
Identification and Characterization of Harc, a Novel Hsp90-associating Relative of Cdc37
Scholz, G. M., Cartledge, K., & Hall, N. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103889200 · Cited by 40
Transient Acquired Thermotolerance in Drosophila, Correlated with Rapid Degradation of Hsp70 During Recovery
Danxi, L., & Duncan, R. F. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0454e.x · Cited by 39
Tanespimycin as Antitumor Therapy
Dimopoulos, M. A., Mitsiades, C. S., Anderson, K. C., & Richardson, P. G. G. (2011) · Clinical Lymphoma Myeloma & Leukemia · doi:10.3816/clml.2011.n.002 · Cited by 39
Induction of Nitric Oxide Synthase-Dependent Telomere Shortening after Functional Inhibition of Hsp90 in Human Tumor Cells
Compton, S. A., Elmore, L. W., Haydu, K., Jackson‐Cook, C. K., & Holt, S. E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1452-1462.2006 · Cited by 41
“While there is evidence to suggest some overlap in function (33, 48), there are also some Hsp90 isoformspecific functions as well (9).”
Background
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
Transcriptomic Profiling of Differential Responses to Drought in Two Freshwater Mussel Species, the Giant Floater Pyganodon grandis and the Pondhorn Uniomerus tetralasmus
Luo, Y., Li, C., Landis, A. G., Wang, G., Stoeckel, J. A., & Peatman, E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089481 · Cited by 39
“regulation of steroid hormone receptors [36], protein translocation [31] and regulation in cell cycle and proliferation [37-42].”
Background
Synergistic promotion of breast cancer cells death by targeting molecular chaperone GRP78 and heat shock protein 70
Li, M., Wang, J., Jing, J., Hua, H. M., Luo, T. L., Xu, L., Wang, R., Liu, D., & Jiang, Y. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00575.x · Cited by 38
“In addition to hormone receptors, another important set of client proteins of both HSP70 and HSP90 is protein kinases, such as c-raf, c-src and the receptor tyrosine kinase ErbB2 [17, 18].”
Background
Transient Acquired Thermotolerance in Drosophila, Correlated with Rapid Degradation of Hsp70 During Recovery
Danxi, L., & Duncan, R. F. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20719.x · Cited by 38
The development and evolution of crossveins in insect wings
Marcus, J. M. (2001) · Journal of Anatomy · doi:10.1046/j.1469-7580.2001.19910211.x · Cited by 65
p50 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
“Both pharmacological and genetic approaches have been utilized to investigate the relationship between chaperone machinery containing the 90-kDa heat shock protein Hsp90 and the biogenesis of catalytically active Src family kinases (15, 16, 52, 55, 56).”
Background
The Role of the 90‐kDa Heat‐Shock Protein and its Associated Cohorts in Stabilizing the Heme‐Regulated Eif‐24Al Kinase in Reticulocyte Lysates during Heat Stress
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
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
Heat shock protein‐90 dampens and directs signaling stimulated by insulin‐like growth factor‐1 and insulin
Meares, G. P., Zmijewska, A. A., & Jope, R. S. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.026 · Cited by 35
The Co-Chaperone Hch1 Regulates Hsp90 Function Differently than Its Homologue Aha1 and Confers Sensitivity to Yeast to the Hsp90 Inhibitor NVP-AUY922
Armstrong, H., Wolmarans, A., Mercier, R., Mai, B., & LaPointe, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049322 · Cited by 36
“These clients include steroid hormone receptors, kinases and ion channels [2,3,4,5,6,7,8,9].”
Background
Disruption of protein function by pathogenic mutations: common and uncommon mechanisms
Taipale, M. (2018) · Biochemistry and Cell Biology · doi:10.1139/bcb-2018-0007 · Cited by 35
“However, in cells, v-Src is stabilized by Hsp90 and its oncogenic properties are strictly dependent on Hsp90 function (Whitesell et al. 1994; Xu and Lindquist, 1993).”
Background
Heterologous Hsp90 promotes phenotypic diversity through network evolution
Koubková-Yu, T. C.-T., Chao, J.-C., & Leu, J. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2006450 · Cited by 35
Expression of the Tribolium castaneum (Coleoptera: Tenebrionidae) hsp83 gene and its relation to oogenesis during ovarian maturation
Xu, J., Shu, J., & Zhang, Q. (2010) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/s1673-8527(09)60071-0 · Cited by 35
Proteomics: a strategy to understand the novel targets in protein misfolding and cancer therapy
Nagathihalli, N. S., Singh, O. V., & Merchant, N. B. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.70 · Cited by 34
Thr90 phosphorylation of Hsp90α by protein kinase A regulates its chaperone machinery
Wang, X., Lu, X., Song, X., Zhuo, W., Jia, L., Jiang, Y., & Luo, Y. (2011) · Biochemical Journal · doi:10.1042/bj20110855 · Cited by 34
Grb7 signal transduction protein mediates metastatic progression of esophageal carcinoma
Tanaka, S., Sugimachi, K., Kawaguchi, H., Saeki, H., Ohno, S., Wands, J. R., & Sugimachi, K. (2000) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(200006)183:3 · Cited by 55
Zebrafish chaperone protein GP96 is required for otolith formation during ear development
Sumanas, S., Larson, J. D., & Bever, M. M. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00322-1 · Cited by 34
“Most of its known substrates are signal transduction proteins, the classical examples being steroid hormone receptors and signaling kinases (Picard et al., 1990; Xu and Lindquist, 1993; Young et al., 2001).”
Background
Cooperative inhibitory effect of ZD1839 (Iressa) in combination with 17‐AAG on glioma cell growth
Premkumar, D. R., Arnold, B. A., & Pollack, I. F. (2006) · Molecular Carcinogenesis · doi:10.1002/mc.20141 · Cited by 33
“Ansamycins tightly bind to a pocket in HSP90 conformational maturation of several important signaling proteins [35], including steroid receptors [36], the serine kinase Raf [37], and the tyrosine kinase v-src [38].”
Background
STRESS PROTEINS: NOMENCLATURE, DIVISION AND FUNCTIONS
Kopeček, P., Altmannová, K., & Weigl, E. (2001) · Biomedical Papers · doi:10.5507/bp.2001.010 · Cited by 33
Aberrant protein phosphorylation at tyrosine is responsible for the growth-inhibitory action of pp60v-src expressed in the yeast Saccharomyces cerevisiae.
Florio, M., Wilson, L. K., Trager, J. B., Thorner, J. W., & Martin, G. S. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.3.283 · Cited by 33
Benzo[a]pyrene-3,6-dione inhibited VEGF expression through inducing HIF-1α degradation
Li, Z., Liu, L.-Z., Shi, X., Fang, J. S., & Jiang, B. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.178 · Cited by 32
Ydj1 Protects Nascent Protein Kinases from Degradation and Controls the Rate of Their Maturation
Mandal, A. K., Nillegoda, N. B., Chen, J. A., & Caplan, A. J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00543-08 · Cited by 32
“In addition to the folding of nascent kinases, molecular chaperones also function to maintain the mature state of mutant kinases, such as oncogenic forms of Src or Lck (26, 53).”
Background
Preferential Sensitization of Tumor Cells to Radiation by Heat Shock Protein 90 Inhibitor Geldanamycin
Matsumoto, Y., Machida, H., & Kubota, N. (2005) · Journal of Radiation Research · doi:10.1269/jrr.46.215 · Cited by 32
Heat shock protein 90 (Hsp90) regulates the stability of transforming growth factor β-activated kinase 1 (TAK1) in interleukin-1β-induced cell signaling
Shi, L., Zhang, Z., Fang, S., Xu, J., Liu, J., Shen, J., Fang, F., Luo, L., & Yin, Z. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.07.019 · Cited by 34
Inside the Hsp90 inhibitors binding mode through induced fit docking
Lauria, A., Ippolito, M., & Almerico, A. M. (2008) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2008.11.004 · Cited by 31
The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function
Cox, M. B., & Johnson, J. L. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-295-3_4 · Cited by 32
The Hsp90 Molecular Chaperone Complex Regulates Maltose Induction and Stability of the Saccharomyces MAL Gene Transcription Activator Mal63p
Bali, M., Zhang, B., Morano, K. A., & Michels, C. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309536200 · Cited by 30
PKCϵ Is a Unique Regulator for hsp90β Gene in Heat Shock Response
Wu, J., Xiao, L., Cheng, X.-K., Cui, L., Wu, N., & Shen, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305537200 · Cited by 30
The pleiotropic deubiquitinase Ubp3 confers aneuploidy tolerancePreprint
Sheltzer, J. M., Dodgson, S. E., Santaguida, S., Sheltzer, J., & Amon, A. (2016) · Genes & Development · doi:10.1101/gad.287474.116 · Cited by 29
“Assessment of the in vivo folding of the Hsp90 substrate Src tyrosine kinase can be achieved by inducing expression of either c-src, which does not affect proliferation of yeast cells, or v-src,whose overexpression is lethal in yeast (Xu and Lindquist 1993).”
Background
Post-embryonic functions of HSP90 in Tribolium castaneum include the regulation of compound eye development
Knorr, E., & Vilcinskas, A. (2011) · Development Genes and Evolution · doi:10.1007/s00427-011-0379-z · Cited by 29
Tissue-specific expression of inducible and constitutive Hsp70 isoforms in the western painted turtle
Scott, M. A., Locke, M., & Buck, L. T. (2002) · Journal of Experimental Biology · doi:10.1242/jeb.00107 · Cited by 29
“Many heat-shock proteins are considered ATP-dependent molecular chaperones and thus recognize unfolded, misfolded and aggregated proteins (Welch, 1992; Xu and Lindquist, 1993).”
Background
Heat shock protein 90β stabilizes focal adhesion kinase and enhances cell migration and invasion in breast cancer cells
Xiong, X., Wang, Y., Liu, C., Lu, Q., Liu, T., Chen, G., Rao, H., & Luo, S. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.05.018 · Cited by 28
The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae
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
“Both proteins are able to substitute Hsp90 functionality in the activation of heterologously expressed mammalian p60v-Src or the steroid hormone receptor (Picard et al., 1990; Xu & Lindquist, 1993).”
Background
Hsp90 dependence of a kinase is determined by its conformational landscape
Luo, Q., Boczek, E. E., Wang, Q., Büchner, J., & Kaila, V. R. I. (2017) · Scientific Reports · doi:10.1038/srep43996 · Cited by 26
Active Participation of Hsp90 in the Biogenesis of the Trimeric Reovirus Cell Attachment Protein ς1
Gilmore, R., Coffey, M. C., & Lee, P. W. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.15227 · Cited by 26
The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart.
Scholz, G. M., Hartson, S. D., Cartledge, K., Volk, L. J., Matts, R. L., & Dunn, A. R. (2001) · PubMed · Cited by 26
Geldanamycin Anisimycins Activate Rho and Stimulate Rho- and ROCK-Dependent Actin Stress Fiber Formation
Amiri, A., Noei, F., Feroz, T., & Lee, J. M. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0362 · Cited by 26
Heat-shock protein 90 inhibitors in antineoplastic therapy: is it all wrapped up?
Isaacs, J. S. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.6.569 · Cited by 26
Peptidylprolylisomerases, Protein Folders, or Scaffolders? The Example of FKBP51 and FKBP52
Rein, T. (2020) · BioEssays · doi:10.1002/bies.201900250 · Cited by 25
Geldanamycin Interferes with the 90-kDa Heat Shock Protein, Affecting Lipopolysaccharide-Mediated Interleukin-1 Expression and Apoptosis within Macrophages
Hsu, H.-Y., Wu, H.-L., Tan, S.-K., Li, V. P.-H., Wang, W.-T., Hsu, J., & Cheng, C.-H. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.024240 · Cited by 25
“The inhibitory effects of GA upon protein kinase activity and signal transduction molecules are probably due to the inhibition of Hsp90 and result in destabilization and degradation of client proteins (Xu and Lindquist, 1993; Whitesell et al., 1994; Chavany et al., 1996; Hsu et al., 2001).”
Background
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
The Hsp90 Chaperone Family
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
University Licensing: Harnessing or Tarnishing Faculty Research?
Thursby, J. G., & Thursby, M. (2010) · Innovation Policy and the Economy · doi:10.1086/605856 · Cited by 24
“From the early 1980s Lindquist’s work focused on protein function, and in 1993 she published a number of influential papers examining the role of heat shock proteins and thermotolerance in yeast cells (Parsell et al. 1993; Parsell and Lindquist 1993; Xu and Lindquist 1993).”
Background
A Mutation in the Catalytic Loop of Hsp90 Specifically Impairs ATPase Stimulation by Aha1p, But Not Hch1p
Horvat, 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
Effect of HSP70 and 90 in Modulation of JNK, ERK Expression in Preeclamptic Placental Endothelial Cell
Padmini, E., Uthra, V., & Lavanya, S. (2012) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-012-9371-0 · Cited by 24
Mining of Biomarker Genes from Expressed Sequence Tags and Differential Display Reverse Transcriptase-Polymerase Chain Reaction in the Self-fertilizing Fish, Kryptolebias marmoratus and Their Expression Patterns in Response to Exposure to an Endocrine-disrupting Alkylphenol, Bisphenol A
Lee, Y., Rhee, J., Hwang, D., Kim, I., Raisuddin, S., & Lee, J. (2007) · Molecules and Cells · doi:10.1016/s1016-8478(23)10719-9 · Cited by 24
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).”
Background
Pharmacological and Genetic Analysis of 90-kDa Heat Shock Isoprotein-Aryl Hydrocarbon Receptor Complexes
Cox, M. B., & Miller, C. A. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.6.1549 · Cited by 22
The molecular chaperone Hsp90 maintains Golgi organization and vesicular trafficking by regulating microtubule stability
Wu, Y., Ding, Y., Zheng, X., & Liao, K. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz093 · Cited by 21
Down-regulation of Hsp90 could change cell cycle distribution and increase drug sensitivity of tumor cells
Liu, X. (1999) · World Journal of Gastroenterology · doi:10.3748/wjg.v5.i3.199 · Cited by 21
Exogenous Expression of Heat Shock Protein 90kDa Retards the Cell Cycle and Impairs the Heat Shock Response
Zhao, C., Hashiguchi, A., Kondoh, K., Du, W., Hata, J.-I., & Yamada, T. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5501 · Cited by 21
“For example, numerous molecules involved in cell proliferation, such as v-Src [6], Raf [7, 8], Akt [9], MyoD [10], SV40 [11], and HSF1 [12], combine directly with HSP90.”
Background
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
Involvement of the TRAP-1 homologue, Dd-TRAP1, in spore differentiation during Dictyostelium development
Morita, T., Yamaguchi, H., Amagai, A., & Maeda, Y. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.10.010 · Cited by 20
RETRACTED: A novel class of specific Hsp90 small molecule inhibitors demonstrate in vitro and in vivo anti-tumor activity in human melanoma cells
Mehta, P. P., Kung, P., Yamazaki, S., Walls, M., Shen, A., Nguyen, L., Gehring, M. R., Los, G., Smeal, T., & Yin, M.-J. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.09.002 · Cited by 20
Retracted
Heat Shock Protein 90 Recognized as an Iron-Binding Protein Associated with the Plasma Membrane of HeLa Cells
Kovár̆, J., Stýbrová, H., Novák, P., Ehrlichová, M., Truksa, J., Koc, M., Kriegerbecková, K., Scheiber‐Mojdehkar, B., & Goldenberg, H. (2004) · Cellular Physiology and Biochemistry · doi:10.1159/000076925 · 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
Biochemical Basis for the Requirement of Kinase Activity for Cbl-dependent Ubiquitinylation and Degradation of a Target Tyrosine Kinase
Ghosh, A. K., Reddi, A. L., Rao, N. L., Duan, L., Band, V., & Band, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404189200 · Cited by 20
Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain
Xu, B., & Miller, W. T. (1996) · Molecular and Cellular Biochemistry · doi:10.1007/bf00225883 · Cited by 20
ORGANIZATION OF EXTRACELLULAR MATRIX COMPONENTS DURING DIFFERENTIATION OF ADIPOCYTES IN LONG-TERM CULTURE
Yasuaki, K. U. B. O., Kaidzu, S., Nakajima, I., Takenouchi, K., & NAKAMURA, F. (2000) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1290/1071-2690(2000)036 · Cited by 133
The evolution of heat shock genes and expression patterns of heat shock proteins in the species from temperature contrasting habitats
Garbuz, D. G., & Evgen’ev, M. B. (2017) · Russian Journal of Genetics · doi:10.1134/s1022795417010069 · Cited by 19
Evidence of an interaction between Mos and Hsp70: a role of the Mos residue serine 3 in mediating Hsp70 association
Liu, H., Vuyyuru, V. B., Pham, C. D., Yang, Y., & Singh, B. (1999) · Oncogene · doi:10.1038/sj.onc.1202699 · Cited by 19
“This association is analogous to the association between another molecular chaperone, Hsp90 and some labile protein kinases including Src, Raf, Cdk4 and Wee1 (Stancato et al., 1993; Xu and Lindquist, 1993; Aligue et al., 1994; Schulte et al., 1995; Stepanova et al., 1996).”
Background
The universe of Hsp90
Stankiewicz, M., & Mayer, M. P. (2011) · BioMolecular Concepts · doi:10.1515/bmc.2011.054 · Cited by 19
Hsp90 Regulates the Phosphorylation and Activity of Serum- and Glucocorticoid-regulated Kinase-1
Belova, L., Brickley, D. R., Ky, B., Sharma, S. K., & Conzen, S. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803289200 · Cited by 17
Peroxin Puzzles and Folded Freight: Peroxisomal Protein Import in Review
Crookes‐Goodson, W. J., & Olsen, L. J. (1999) · Die Naturwissenschaften · doi:10.1007/s001140050572 · Cited by 17
“Hsp90s function in a “super-chaperone” complex with Hsp70s to prime mammalian steroid receptors for ligand binding (Jakob and Buchner 1994; Pratt 1993; Xu and Lindquist 1993).”
Background

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
DOI: 10.1073/pnas.90.15.7074
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Heat-shock protein hsp90 governs the activity of pp60v-src kinase.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks