The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex
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A variety of signaling proteins form heterocomplexes with and are regulated by the heat shock protein chaperone hsp90. These complexes are formed by a multiprotein machinery, including hsp90 and hsp70 as essential and abundant components and Hop, hsp40, and p23 as non-essential cochaperones that are present in much lower abundance in cells. Overexpression of signaling proteins can overwhelm the capacity of this machinery to properly assemble heterocomplexes with hsp90. Here, we show that the limiting component of this assembly machinery in vitro in reticulocyte lysate and in vivo in Sf9 cells is p23. Only a fraction of glucocorticoid receptors (GR) overexpressed in Sf9 cells are in heterocomplex with hsp90 and have steroid binding activity, with the majority of the receptors present as both insoluble and cytosolic GR aggregates. Coexpression of p23 with the GR increases the proportion of cytosolic receptors that are in stable GR.hsp90 heterocomplexes with steroid binding activity, a strictly hsp90-dependent activity for the GR. Coexpression of p23 eliminates the insoluble GR aggregates and shifts the cytosolic receptor from very large aggregates without steroid binding activity to approximately 600-kDa heterocomplexes with steroid binding activity. These data lead us to conclude that p23 acts in vivo to stabilize hsp90 binding to client protein.
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p23 marks steroid receptors in the apo state that are poised to bind hormone.
“In this context, p23 is known to mark steroid receptors in the apo state that are poised to bind hormone (15).”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [15]
The Coexpression of p23 section (page unavailable) says p23 binds and stabilizes glucocorticoid receptor–hsp90 complexes that can subsequently bind steroid. This supports a hormone-binding-ready state for that receptor, but the paper does not establish p23 as a marker of apo steroid receptors generally. (LLM, conf=0.82)
Experimental — accuracy not yet measuredp23 acts as a limiting component for assembly of the multicomponent Hsp90 superchaperone complex that stabilizes the LBD in a hormone-binding competent conformation.
“p23 function is critical for steroid hormone receptors, as it has been shown to act as a limiting component for assembly of the multicomponent Hsp90 'superchaperone' complex that stabilizes the LBD in a conformation that is competent for hormone binding (15).”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [15]
The Abstract and Coexpression of p23 section report that p23 limits formation of stable GR–Hsp90 complexes with steroid-binding activity. The experiments concern glucocorticoid receptors in Sf9 cells, rather than steroid hormone receptors generally; the paper also says p23 is not required to open the steroid-binding cleft, but stabilizes the resulting complex. (LLM, conf=0.84)
Experimental — accuracy not yet measuredp23 binds directly to the ATP form of Hsp90, and this stabilizes Hsp90-client protein interactions.
“because the cochaperone p23 binds directly to the ATP form of Hsp90, and this stabilizes Hsp90-client protein interactions (1, 14, 15).”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [15]
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Cites
Pratt, W., & Toft, D. (2003) · Experimental biology and medicine · doi:10.1177/153537020322800201 · Cited by 1,539 · see citing works
Self-citationActivation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1
Panaretou, B., Siligardi, G., Meyer, P., Maloney, A., Sullivan, J. K., Singh, S., Millson, S. H., Clarke, P. A., Naaby‐Hansen, S., Stein, R. C., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00785-2 · Cited by 544 · see citing works
Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones
Freeman, B. C., & Yamamoto, K. R. (2002) · Science · doi:10.1126/science.1073051 · Cited by 400 · see citing works
Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370 · see citing works
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
Höhfeld, J., Cyr, D., & Patterson, C. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve206 · Cited by 338 · see citing works
Smith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300 · see citing works
Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery
Dittmar, K. D., Demady, D. R., Stancato, L., Krishna, P., & Pratt, W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21213 · Cited by 288 · see citing works
Self-citationSánchez, E. R., Meshinchi, S., Tienrungroj, W., Schlesinger, M. J., Toft, D. O., & Pratt, W. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48191-4 · Cited by 263 · see citing works
Self-citationThe Assembly of Progesterone Receptor-hsp90 Complexes Using Purified Proteins*
Kosano, H., Stensgard, B., Charlesworth, M., McMahon, N., & Toft, D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32973 · Cited by 251 · see citing works
Grenert, J. P., Johnson, B. D., & Toft, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17525 · Cited by 238 · see citing works
Nucleotides and Two Functional States of hsp90
Sullivan, W., Stensgard, B. A., Caucutt, G., Bartha, B. B., McMahon, N., Alnemri, E. S., Litwack, G., & Toft, D. O. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.8007 · Cited by 235 · see citing works
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co‐chaperone p23
Young, J. C., & Hartl, F. U. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5930 · Cited by 230 · see citing works
Johnson, J. L., & Toft, D. O. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31487-4 · Cited by 229 · see citing works
Caplan, A. J., Tsai, J., Casey, P. J., & Douglas, M. G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37044-9 · Cited by 187 · see citing works
Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex.
Scherrer, L. C., Dalman, F. C., Massa, E., Meshinchi, S., & Pratt, W. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45746-8 · Cited by 186 · see citing works
Self-citationDynamic Remodeling of Transcription Complexes by Molecular Chaperones
Morimoto, R. I. (2002) · Cell · doi:10.1016/s0092-8674(02)00860-7 · Cited by 177 · see citing works
Morishima, Y., Murphy, P. J. M., Li, D.-P., Sanchez, E. R., & Pratt, W. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000434200 · Cited by 166 · see citing works
Self-citationDittmar, K. D., Banach, M., Galigniana, M. D., & Pratt, W. B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7358 · Cited by 163 · see citing works
Self-citationHonoré, B., Leffers, H. C. B., Madsen, P., Rasmussen, H. H., Vandekerckhove, J. S., & Celis, J. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42471-4 · Cited by 159 · see citing works
Dittmar, K. D., Hutchison, K. A., Owens-Grillo, J. K., & Pratt, W. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12833 · Cited by 158 · see citing works
Self-citationSBA1 Encodes a Yeast Hsp90 Cochaperone That Is Homologous to Vertebrate p23 Proteins
Fang, Y., Fliss, A., Rao, J., & Caplan, A. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3727 · Cited by 154 · see citing works
Reconstitution of Progesterone Receptor with Heat Shock Proteins
Smith, D. F., Schowalter, D. B., Kost, S. L., & Toft, D. O. (1990) · Molecular Endocrinology · doi:10.1210/mend-4-11-1704 · Cited by 144 · see citing works
Bohen, S. P. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3330 · Cited by 106 · see citing works
Morishima, Y., Kanelakis, K. C., Silverstein, A. M., Dittmar, K. D., Estrada, L., & Pratt, W. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.6894 · Cited by 106 · see citing works
Self-citationLiu, J., & DeFranco, D. B. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.3.0258 · Cited by 96 · see citing works
Kanelakis, K. C., Morishima, Y., Dittmar, K. D., Galigniana, M. D., Takayama, S.-I. J., Reed, J. C., & Pratt, W. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34134 · Cited by 92 · see citing works
Self-citationGee, A. C., & Katzenellenbogen, J. A. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.3.0602 · Cited by 65 · see citing works
Kanelakis, K. C., Murphy, P. J. M., Galigniana, M. D., Morishima, Y., Takayama, S.-I. J., Reed, J. C., Toft, D. O., & Pratt, W. B. (2000) · Biochemistry · doi:10.1021/bi001671c · Cited by 65 · see citing works
Self-citationSchmidt, U., Wochnik, G. M., Rosenhagen, M. C., Young, J. C., Hartl, F. U., Holsboer, F., & Rein, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212000200 · Cited by 58 · see citing works
Murphy, P. J. M., Morishima, Y., Chen, H., Galigniana, M. D., Mansfield, J. F., Simons, S. S., & Pratt, W. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304469200 · Cited by 53 · see citing works
Self-citationAlnemri, E. S., & Litwack, G. (1993) · Biochemistry · doi:10.1021/bi00071a014 · Cited by 48 · see citing works
Oxelmark, E., Knoblauch, R. E., Arnal, S. M., Su, L. F., Schapira, M., & Garabedian, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305960200 · Cited by 38 · see citing works
Srinivasan, G., Post, J. F. M., & Thompson, E. B. (1997) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(96)00182-3 · Cited by 33 · see citing works
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HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works
Self-citationA General Introduction to Glucocorticoid Biology
Timmermans, S., Souffriau, J., & Libert, C. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01545 · Cited by 619 · see citing works
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498 · see citing works
The glucocorticoid responses are shaped by molecular chaperones
Grad, I., & Picard, D. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.018 · Cited by 423 · see citing works
Gymnastics of Molecular Chaperones
Mayer, M. P. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.012 · Cited by 364 · see citing works
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
Pratt, W. B., Galigniana, M. D., Harrell, J. M., & DeFranco, D. B. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.02.004 · Cited by 285 · see citing works
Self-citationGene regulation by the glucocorticoid receptor: structure:function relationship
Kumar, R., & Thompson, E. B. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2004.12.046 · Cited by 261 · see citing works
The Stress of Protein Misfolding: From Single Cells to Multicellular OrganismsPreprint
Gidalevitz, T., Prahlad, V., & Morimoto, R. I. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009704 · Cited by 254 · see citing works
Chaperoning of Glucocorticoid Receptors
Pratt, W. B., Morishima, Y., Murphy, M. N., & Harrell, M. (2005) · Springer eBooks · doi:10.1007/3-540-29717-0_5 · Cited by 247 · see citing works
Self-citationMolecular chaperones, essential partners of steroid hormone receptors for activity and mobility
Echeverría, P. C., & Picard, D. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.11.012 · Cited by 225 · see citing works
Role of Acetylation and Extracellular Location of Heat Shock Protein 90α in Tumor Cell Invasion
Yang, Y., Rao, R., Shen, J., Tang, Y., Fiskus, W. C., Nechtman, J., Atadja, P. W., & Bhalla, K. N. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0644 · Cited by 221 · see citing works
On the Trail of the Glucocorticoid Receptor: Into the Nucleus and Back
Vandevyver, S., Dejager, L., & Libert, C. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01288.x · Cited by 222 · see citing works
Han, L., Wang, B., Wang, R., Gong, S., Chen, G., & Xu, W. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1498-0 · Cited by 172 · see citing works
Murphy, P. J. M., Morishima, Y., Kovacs, J. J., Yao, T.-P., & Pratt, W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506997200 · Cited by 167 · see citing works
Self-citationNi, L., Yang, C.-S., Gioeli, D., Frierson, H., Toft, D. O., & Paschal, B. M. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01891-08 · Cited by 155 · see citing works
The Hsp90 Chaperone Machinery Regulates Signaling by Modulating Ligand Binding Clefts
Pratt, W. B., Morishima, Y., & Osawa, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800023200 · Cited by 151 · see citing works
Self-citationChaperone Functions of the E3 Ubiquitin Ligase CHIP
Rosser, M. F. N., Washburn, E. K., Muchowski, P. J., Patterson, C., & Cyr, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700513200 · Cited by 144 · see citing works
The Plasticity of the Hsp90 Co-chaperone System
Sahasrabudhe, P., Rohrberg, J., Biebl, M. M., Rutz, D. A., & Buchner, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.004 · Cited by 136 · see citing works
The Middle Domain of Hsp90 Acts as a Discriminator between Different Types of Client Proteins
Hawle, P., Siepmann, M., Harst, A., Siderius, M., Reusch, H. P., & Obermann, W. M. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02188-05 · Cited by 127 · see citing works
Harst, A., Lin, H.-Y., & Obermann, W. (2005) · Biochemical Journal · doi:10.1042/bj20041283 · Cited by 121 · see citing works
Galigniana, M. D., Echeverría, P. C., Erlejman, A. G., & Piwien-Pilipuk, G. (2010) · Nucleus · doi:10.4161/nucl.1.4.11743 · Cited by 114 · see citing works
Plasmodial heat shock proteins: targets for chemotherapy
Shonhai, A. (2009) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2009.00639.x · Cited by 113 · see citing works
Sinclair, D., Fillman, S. G., Webster, M. J., & Weickert, C. S. (2013) · Scientific Reports · doi:10.1038/srep03539 · Cited by 102 · see citing works
Thomas, M., Harrell, J. M., Morishima, Y., Peng, H., Pratt, W. B., & Lieberman, A. P. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl110 · Cited by 95 · see citing works
Self-citationMultiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.
Bhangoo, M. K., Tzankov, S., Fan, A., Dejgaard, K., Thomas, D. Y., & Young, J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0088 · Cited by 98 · see citing works
Dammer, E. B., Lee, A. K., Duong, D. M., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2014) · PROTEOMICS · doi:10.1002/pmic.201400189 · Cited by 80 · see citing works
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Gathercole, L., & Stewart, P. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.03.060 · Cited by 82 · see citing works
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French, J. B., Zhao, H., An, S., Niessen, S., Deng, Y., Cravatt, B. F., & Benkovic, S. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300173110 · Cited by 82 · see citing works
Review: HPA‐axis activity in alcoholism: examples for a gene–environment interaction
Clarke, T., Treutlein, J., Zimmermann, U. S., Kiefer, F., Skowronek, M. H., Rietschel, M., Mann, K., & Schumann, G. (2008) · Addiction Biology · doi:10.1111/j.1369-1600.2007.00084.x · Cited by 80 · see citing works
Baker, J. D., McMillan, I. O., Ospina, S. R., Gulick, D., & Blair, L. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010079 · Cited by 73 · see citing works
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Cintron, N. S., & Toft, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605417200 · Cited by 77 · see citing works
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Donato, M. D., & Geisler, M. M. (2019) · FEBS Letters · doi:10.1002/1873-3468.13499 · Cited by 66 · see citing works
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Lopez, A., Dahiya, V., Delhommel, F., Freiburger, L., Stehle, R., Asami, S., Rutz, D., Blair, L., Buchner, J., & Sattler, M. (2021) · Science Advances · doi:10.1126/sciadv.abl7295 · Cited by 59 · see citing works
Biebl, M. M., Lopez, A., Rehn, A., Freiburger, L., Lawatscheck, J., Blank, B., Sattler, M., & Buchner, J. (2021) · Nature Communications · doi:10.1038/s41467-021-21063-0 · Cited by 58 · see citing works
Braga‐Basaria, M., Hardy, E., Gottfried, R., Burman, K. D., Saji, M., & Ringel, M. D. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031767 · Cited by 56 · see citing works
Rose’Meyer, R. B. (2013) · Molecular Autism · doi:10.1186/2040-2392-4-37 · Cited by 56 · see citing works
Functions of the Hsp90 chaperone system: lifting client proteins to new heights.
Eckl, J. M., & Richter, K. (2013) · Europe PMC (PubMed Central) · Cited by 53 · see citing works
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Younes, A., & Georgakis, G. V. (2005) · Future Oncology · doi:10.1517/14796694.1.2.273 · Cited by 51 · see citing works
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Wochnik, G. M., Young, J. C., Schmidt, U., Holsboer, F., Hartl, F. U., & Rein, T. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00066-3 · Cited by 46 · see citing works
Yang, P., Sampson, H. M., & Krause, H. M. (2006) · PROTEOMICS · doi:10.1002/pmic.200500230 · Cited by 43 · see citing works
NudC-like protein 2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90
Yang, Y., Yan, X., Cai, Y., Lü, Y., Si, J., & Zhou, T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914307107 · Cited by 41 · see citing works
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Graf, C., Lee, C., Meier-Andrejszki, L. E., Nguyễn, M. T., & Mayer, M. P. (2014) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2014.00004 · Cited by 40 · see citing works
Peng, H., Morishima, Y., Clapp, K. M., Lau, M., Pratt, W. B., & Osawa, Y. (2009) · Biochemistry · doi:10.1021/bi901058g · Cited by 40 · see citing works
Self-citationPare, J. M., LaPointe, P., & Hobman, T. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-12-0892 · Cited by 40 · see citing works
Zhu, X.-J., Liu, X., Jin, Q., Cai, Y., Yang, Y., & Zhou, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105494 · Cited by 39 · see citing works
Schumacher, J. A., Crockett, D. K., Elenitoba‐Johnson, K. S. J., & Lim, M. S. (2007) · PROTEOMICS · doi:10.1002/pmic.200700108 · Cited by 39 · see citing works
Blacklock, K. M., & Verkhivker, G. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071936 · Cited by 38 · see citing works
Echeverría, P. C., Figueras, M. J., Vogler, M., Kriehuber, T., de Miguel, N., Deng, B., Dalmasso, M. C., Matthews, D. E., Matrajt, M., Haslbeck, M., et al. (2010) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2010.04.004 · Cited by 36 · see citing works
General Structural and Functional Features of Molecular Chaperones
Edkins, A. L., & Boshoff, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-78397-6_2 · Cited by 36 · see citing works
Kumar, P. (2008) · Biologics · doi:10.2147/btt.s3820 · Cited by 34 · see citing works
Generalized and tissue specific glucocorticoid resistance
Martins, C. S., & de Castro, M. (2021) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2021.111277 · Cited by 30 · see citing works
Rehn, A., & Büchner, J. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-11731-7_6 · Cited by 30 · see citing works
Chapter 13 Xenobiotic impact on corticosteroid signaling
Vijayan, M. M., Prunet, P., & Boone, A. N. (2005) · Biochemistry and molecular biology of fishes · doi:10.1016/s1873-0140(05)80016-5 · Cited by 29 · see citing works
The helix 1–3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones
Cluning, C., Ward, B. K., Rea, S. L., Arulpragasam, A., Fuller, P. J., & Ratajczak, T. (2013) · Molecular Endocrinology · doi:10.1210/me.2012-1023 · Cited by 26 · see citing works
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Gu, X., Xue, W., Yin, Y.-J., Liu, H.-W., Li, S.-J., & Sun, X.-Y. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01571 · Cited by 26 · see citing works
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Molecular mechanisms of glucocorticoid resistance in systemic lupus erythematosus: A review
Gao, H., Wang, Q., Yu, X., Liu, J., Bai, S., Feng, J. C., & Wu, B. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.08.038 · Cited by 25 · see citing works
The co‐chaperone p23 is degraded by caspases and the proteasome during apoptosis
Mollerup, J., & Berchtold, M. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.06.045 · Cited by 25 · see citing works
The role of the FKBP51–Hsp90 complex in Alzheimer’s disease: An emerging new drug target
Jeanne, X., Török, Z., Vı́gh, L., & Prodromou, C. (2024) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2024.11.006 · Cited by 21 · see citing works
Recombinant expression of aryl hydrocarbon receptor for quantitative ligand-binding analysis
Fan, M. Q., Bell, A. R., Bell, D., Clode, S. A., Fernandes, A., Foster, P. M. D., Fry, J. R., Jiang, T., Loizou, G. D., MacNicoll, A. D., et al. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.10.003 · Cited by 20 · see citing works
Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein
Cha, J., Ermawati, N., Jung, M., Su’udi, M., Kim, K.-Y., Kim, J.-Y., Han, C.-D., Lee, K.-H., & Son, D. (2009) · Cell stress & chaperones (Print) · doi:10.1007/s12192-008-0077-6 · Cited by 18 · see citing works
Oasa, S., Sasaki, A., Yamamoto, J., Mikuni, S., & Kinjo, M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.07.003 · Cited by 17 · see citing works
Munezero, D., Aliff, H. L., Salido, E. M., Saravanan, T., Sanzhaeva, U., Guan, T., & Ramamurthy, V. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104809 · Cited by 15 · see citing works
Liu, Y., Jang, S., Wang, S., Chen, C.-H., & Li, F. (2015) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2015.1074113 · Cited by 13 · see citing works
Clapp, K. M., Peng, H., Morishima, Y., Lau, M., Walker, V. J., Pratt, W. B., & Osawa, Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159178 · Cited by 13 · see citing works
Self-citationHsp90 Co-chaperones as Drug Targets in Cancer: Current Perspectives
Edkins, A. L. (2016) · Topics in medicinal chemistry · doi:10.1007/7355_2015_99 · Cited by 13 · see citing works
Bishop, Ö. T., Edkins, A. L., & Blatch, G. L. (2013) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.22541 · Cited by 11 · see citing works
Eckl, J. M., Drazic, A., Rutz, D. A., & Richter, K. (2014) · Biochemistry · doi:10.1021/bi5000542 · Cited by 11 · see citing works
Proteomics in myocardial diseases
Bukowska, A., Lendeckel, U., Kähne, T., & Goette, A. (2004) · Pathology - Research and Practice · doi:10.1016/j.prp.2004.02.004 · Cited by 11 · see citing works
Interplay of p23 with FKBP51 and their chaperone complex in regulating tau aggregation
Chakraborty, P., & Zweckstetter, M. (2025) · Nature Communications · doi:10.1038/s41467-025-56028-0 · Cited by 10 · see citing works
p23 and Aha1: Distinct Functions Promote Client Maturation
Biebl, M. M., & Büchner, J. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-14740-1_6 · Cited by 9 · see citing works
Genomic and non-genomic effects of glucocorticoids in respiratory diseases
Lee, Z.-Y., & Tran, T. (2023) · Advances in pharmacology · doi:10.1016/bs.apha.2023.04.006 · Cited by 9 · see citing works
Chaperones and the maturation of steroid hormone receptor complexes
Tao, Y. J., & Zheng, W. (2011) · Oncotarget · doi:10.18632/oncotarget.238 · Cited by 8 · see citing works
Bernadotte, A., Kumar, R., Winblad, B. G., & Pavlov, P. F. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12521 · Cited by 7 · see citing works
head-bent resistant Hsc70 variants show reduced Hsp40 affinity and altered protein folding activity
Papsdorf, K., Sima, S., Schmauder, L., Peter, S., Renner, L., Hoffelner, P., & Richter, K. (2019) · Scientific Reports · doi:10.1038/s41598-019-48109-0 · Cited by 7 · see citing works
SUMO conjugation as regulator of the glucocorticoid receptor-FKBP51 cellular response to stress
Liberman, A. C., Budziñski, M. L., Sokn, C., Gobbini, R. P., Ugo, M. B., & ARZT, E. S. (2019) · Steroids · doi:10.1016/j.steroids.2019.108520 · Cited by 7 · see citing works
Tang, P., Chen, Y., Chen, D., Zhu, H., Dai, S., Zhou, J., Huang, X., Huang, X., Ouyang, P., Geng, Y., et al. (2025) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2025.110262 · Cited by 5 · see citing works
Defining the Differential Corticosteroid Response Basis from Multiple Omics Approaches
Ramirez-Falcon, M., Suarez-Pajes, E., & Flores, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252413611 · Cited by 3 · see citing works
The Hsp90 Chaperone Machinery: An Important Hub in Protein Interaction Networks
Radons, J. (2016) · Journal of Advances in Medicine and Medical Research · doi:10.9734/bjmmr/2016/24631 · Cited by 3 · see citing works
Role of Heat Shock Proteins in Immune Modulation in Malaria
Böttger, E., & Multhoff, G. (2013) · Springer eBooks · doi:10.1007/978-94-007-7438-4_7 · Cited by 3 · see citing works
Role of Heat Shock Proteins in Immune Modulation in Malaria
Zininga, T., Böttger, E., & Multhoff, G. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-78397-6_7 · Cited by 3 · see citing works
Mechanisms of Glucocorticoid Actions and Resistance in Multiple Myeloma
Gandhi, V. V., & Sánchez-Vega, B. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-035-5_23 · Cited by 2 · see citing works
p23-FKBP51 chaperone complex regulates tau aggregationPreprint
Chakraborty, P., & Zweckstetter, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.27.573415 · Cited by 2 · see citing works
Emergence and Characterization of the p23 Molecular Chaperone
Echtenkamp, F., & Freeman, B. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_9 · Cited by 1 · see citing works
General Structural and Functional Features of Molecular Chaperones.
Edkins, A., & Boshoff, A. (2021) · Advances in Experimental Medicine and Biology · doi:10.1007/978-94-007-7438-4_2 · Cited by 32 · see citing works
Pratt, W. B., Morishima, Y., & Osawa, Y. (2007) · Springer eBooks · doi:10.1007/978-1-4020-6401-2_1 · Cited by 1 · see citing works
Self-citationModulation of allergic airway inflammation by glucocorticoids
Karabinskaya, A. (2014) · doi:10.53846/goediss-4399
Schafer, E. A. (2005) · D-Scholarship@Pitt (University of Pittsburgh)
Hsp90 molecular chaperone: structure, functions and participation in the cardio-vascular pathologies
Kroupskaya, I. V. (2009) · Biopolymers and Cell · doi:10.7124/bc.0007ef
Kovacs, J. J. (2005) · Defense Technical Information Center (DTIC) · doi:10.21236/ada435267
40 – Nuclear Mechanisms of Glucocorticoid Action
Hager, G. L., Stavreva, D., & Voss, T. (2009) · Elsevier eBooks · doi:10.1016/b978-008088783-8.00040-1
Banasavadi‐Siddegowda, Y. (2011) · OhioLink ETD Center (Ohio Library and Information Network)
Sahebari, M., Rezaieyazdi, Z., Khodashahi, M., Rafatpanah, H., Mehrad‐Majd, H., Saadati, N., & Salari, M. (2023) · PubMed Central · doi:10.22088/cjim.14.3.470
WITHAFERIN A: A NOVEL THERAPEUTIC APPROACH FOR MALIGANT BRAIN TUMORS
Grogan, P. T. (2014) · KU ScholarWorks (The University of Kansas)
- Authors
- Morishima, Y., Kanelakis, K. C., Murphy, P. J. M., Lowe, E. R., Jenkins, G. J., Osawa, Y., Sunahara, R. K., & Pratt, W. B.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Pratt, William B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-12
- Volume
- 278
- Issue
- 49
- Pages
- 48754-48763
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2074527824
- Cited by
- 97
- References
- 33
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 5 · 2022: 3 · 2021: 5 · 2019: 5 · 2018: 4 · 2017: 1 · 2016: 3 · 2015: 2 · 2014: 7 · 2013: 10
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (CA28010, DK31573)
- National Cancer Institute (R01CA028010, CA 28010)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK31573)
- National Institute of Environmental Health Sciences (ES 08365, R01ES008365)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- p23, Hsp90 co-chaperone, HSP70, Hsp90 client proteins, glucocorticoid receptor, protein aggregation, Humulus lupulus, Hsp40, Sf9 cells, reticulocyte lysate
- MeSH terms
- Prostaglandin-E Synthases, Animals, Cell Line, Humans, Phosphoproteins, Protein Binding, Receptors, Glucocorticoid, Recombinant Proteins, Molecular Chaperones, HSP70 Heat-Shock Proteins, In Vitro Techniques
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