The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
Open accessAbstract
Multiple molecular chaperones, including Hsp90 and p23, interact with members of the intracellular receptor (IR) family. To investigate p23 function, we compared the effects of three p23 proteins on IR activities, yeast p23 (sba1p) and the two human p23 homologs, p23 and tsp23. We found that Sba1p was indistinguishable from human p23 in assays of seven IR activities in both animal cells and in yeast; in contrast, certain effects of tsp23 were specific to that homolog. Transcriptional activation by two IRs was increased by expression of any of the p23 species, whereas activation by five other IRs was decreased by Sba1p or p23, and unaffected by tsp23. p23 was expressed in all tissues examined except striated and cardiac muscle, whereas tsp23 accumulated in a complementary pattern; hence, p23 proteins might contribute to tissue-specific differences in IR activities. Unlike Hsp90, which acts on IR aporeceptors to stimulate ligand potency (i.e., hormone-binding affinity), p23 proteins acted on IR holoreceptors to alter ligand efficiencies (i.e., transcriptional activation activity). Moreover, the p23 effects developed slowly, requiring prolonged exposure to hormone. In vitro, p23 interacted preferentially with hormone–receptor–response element ternary complexes, and stimulated receptor–DNA dissociation. The dissociation was reversed by addition of a fragment of the GRIP1 coactivator, suggesting that the two reactions may be in competition in vivo. Our findings suggest that p23 functions at one or more late steps in IR-mediated signal transduction, perhaps including receptor recycling and/or reversal of the response.
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Expression of p23 significantly enhanced GR activity relative to Sba1, consistent with a previous report.
“expression of p23 significantly enhanced GR activity relative to Sba1, consistent with a previous report32.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [32]
In “Effects of the yeast p23 homolog on IR activities” (page unavailable), the paper says p23 and Sba1p were “indistinguishable in their effects on receptors.” Its mammalian-cell results report that both increased GR activity two- to threefold, rather than p23 enhancing it significantly more than Sba1p. (LLM, conf=0.88)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredp23 can substitute for Sba1 in yeast GR transactivation assays.
“given that p23 can substitute for Sba1 in yeast GR transactivation assays32,33.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [32]
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HSP90AB1: Helping the good and the bad
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“HSP90 converts to a closed conformation after binding of ATP and binding of p23 (Johnson et al. 1994; Johnson & Toft 1995; Freeman et al. 2000; McLaughlin et al. 2006; Forafonov et al. 2008), releasing Hop and HSC70 from the complex, leaving space for another PPIase molecule.”
BackgroundDynamic 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
The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins
McLaughlin, S. H., Sobott, F., Yao, Z.-P., Zhang, W., Nielsen, P. R., Grossmann, J. G., Laue, E. D., Robinson, C. V., & Jackson, S. E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.085 · Cited by 196 · see citing works
“Opposing a role in assisting the assembly process, p23 may alter the transcriptional activity of nuclear receptors by affecting the dissociation rate of the receptor–DNA response element complex.(28) The molecular mechanism by which p23 acts as a co-chaperone for Hsp90 is unknown.”
BackgroundFries, G. R., Gassen, N. C., & Rein, T. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122614 · Cited by 167 · see citing works
Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism
Noddings, C. M., Wang, R. Y.-R., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04236-1 · Cited by 165 · see citing works
Richter, K., Walter, S., & Buchner, J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.064 · Cited by 159 · see citing works
Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein
Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.003 · Cited by 151 · see citing works
“Finally, p23, which operates during late steps in receptor action, stabilizes the Hsp90-SHR-interaction (Freeman et al., 2000).”
BackgroundMixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle
Li, J., Richter, K., & Buchner, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1965 · Cited by 155 · see citing works
Chadli, A., Bouhouche, I., Sullivan, W. J., Stensgard, B., McMahon, N., Catelli, M., & Toft, D. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.220430297 · Cited by 159 · see citing works
Self-citationFungal heat-shock proteins in human disease
Burnie, J., Carter, T. L., Hodgetts, S. J., & Matthews, R. (2005) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2005.00001.x · Cited by 158 · see citing works
Han, R., Tsui, S., & Smith, T. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111246200 · Cited by 152 · 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
Chell, S. D., Кади, А., Williams, A. C., & Paraskeva, C. (2006) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.05.002 · Cited by 144 · see citing works
AIP and its interacting partners
Trivellin, G., & Korbonits, M. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0054 · Cited by 144 · see citing works
“These functions are in line with the modulating role that p23 has been shown to exert in different steroid hormone receptors (Smith et al. 1995, Dittmar et al. 1997, Freeman et al. 2000).”
BackgroundIntegration of the accelerator Aha1 in the Hsp90 co-chaperone cycle
Li, J., Richter, K., Reinstein, J., & Büchner, J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2502 · Cited by 132 · see citing works
Unexpected Virilization in Male Mice Lacking Steroid 5 -Reductase Enzymes
Mahendroo, M., Cala, K. M., Hess, D. L., & Russell, D. W. (2001) · Endocrinology · doi:10.1210/endo.142.11.8510 · Cited by 133 · see citing works
“The requirement for a stronger signal may arise in a tissue due to poor vascularization and hence diminished access to hormone, to the presence of high levels of catabolic enzymes that specifically degrade one or the other androgen (47), or to the expression of receptor-binding proteins that destabilize a particular l…”
p23, a simple protein with complex activities
Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116 · see citing works
Self-citationEstrogen Receptor-α Hinge-Region Lysines 302 and 303 Regulate Receptor Degradation by the Proteasome
Berry, N. B., Fan, M., & Nephew, K. P. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0449 · Cited by 112 · see citing works
The Influence of ATP and p23 on the Conformation of hsp90
Sullivan, W. P., Owen, B. A. L., & Toft, D. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207754200 · Cited by 111 · see citing works
Self-citationCardozo, C. P., Michaud, C., Ost, M. C., Fliss, A., Yang, E., Patterson, C., Hall, S. J., & Caplan, A. J. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00680-x · Cited by 106 · see citing works
Molecular chaperones throughout the life cycle of the androgen receptor
Prescott, J., & Coetzee, G. A. (2005) · Cancer Letters · doi:10.1016/j.canlet.2004.12.037 · Cited by 103 · see citing works
Dancing with the Diva: Hsp90–Client Interactions
Radli, M., & Rüdiger, S. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.026 · Cited by 101 · see citing works
“The client binds to Hsp90 and the complex is stabilized by an ATPase inhibitor co-chaperone, such as p23 for GR-LBD and Cdc37 for Cdk4 [28,40,103,104].”
BackgroundNovobiocin Induces a Distinct Conformation of Hsp90 and Alters Hsp90−Cochaperone−Client Interactions
Yun, B.-G., Huang, W., Leach, N., Hartson, S. D., & Matts, R. L. (2004) · Biochemistry · doi:10.1021/bi0497998 · Cited by 101 · see citing works
Chaperoning steroidal physiology: Lessons from mouse genetic models of Hsp90 and its cochaperones
Sánchez, E. R. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.006 · Cited by 96 · see citing works
“Cell-based studies, however, paint a more complicated picture with p23 being either stimulatory [33] or inhibitory [34] of GR activity, stimulatory of ER [35], and inhibitory of TR, AR and MR [33].”
BackgroundFurness, S. G. B., Lees, M. J., & Whitelaw, M. L. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.011 · Cited by 95 · see citing works
“p23 is expressed highly in the majority of murine tissues [63], however p23 and a related protein (transcript similar p23)”
BackgroundInfluentialThe Hsp90 Cochaperone p23 Is Essential for Perinatal Survival
Grad, I., McKee, T., Ludwig, S. M., Hoyle, G. W., Ruíz, P., Wurst, W., Floß, T., Miller, C. A., & Picard, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00734-06 · Cited by 91 · see citing works
“This result argues very strongly that p23 has an essential function that, at least for perinatal survival, cannot be compensated for by the two relatively distant homologs tsp23 and B-ind1 (13, 16). p23 is required for final fetal lung and skin maturation.”
BackgroundInfluentialHsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast
Abbas‐Terki, T., Donzé, O., Briand, P.-A., & Picard, D. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.22.7569-7575.2001 · Cited by 94 · see citing works
“wt and 704, strains HH1a-p2HG/Hsp82 and HH1a-p2HG/Hsp82(1-704), with wild-type Hsp82 and mutant Hsp82 lacking amino acids 705 to 709, respectively.”
BackgroundInfluentialHsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules
Röhl, A., Wengler, D., Madl, T., Lagleder, S., Tippel, F., Herrmann, M., Hendrix, J., Richter, K., Hack, G., Schmid, A. B., et al. (2015) · Nature Communications · doi:10.1038/ncomms7655 · Cited by 88 · see citing works
Modulation of the Maladaptive Stress Response to Manage Diseases of Protein Folding
Roth, D., Hutt, D. M., Tong, J., Bouchecareilh, M., Wang, N., Seeley, T., Dekkers, J. F., Beekman, J. M., Garza, D., Drew, L., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001998 · Cited by 89 · see citing works
“down-regulates the transcription of the glucocorticoid and thyroid hormone receptors [54,55], we did not observe any changes in WT- or F508del-CFTR mRNA levels (Figure 3D).”
BackgroundDahiya, V., Agam, G. N., Lawatscheck, J., Rutz, D. A., Lamb, D. C., & Büchner, J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.026 · Cited by 92 · see citing works
Quintá, H., Maschi, D., Gomez-Sanchez, C., Piwien-Pilipuk, G., & Galigniana, M. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06970.x · Cited by 86 · see citing works
p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
Forafonov, F., Toogun, O. A., Grad, I., Suslova, E., Freeman, B. C., & Picard, D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02246-07 · Cited by 84 · see citing works
Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling
Cox, M., & Miller, C. A. (2004) · Cell stress & chaperones (Print) · doi:10.1379/1466-1268(2004)009 · Cited by 90 · see citing works
Continuous recycling: a mechanism for modulatory signal transduction.
Freeman, B. C., & Yamamoto, K. R. (2001) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(01)01834-5 · Cited by 81 · see citing works
Self-citationShatkina, L., Mink, S., Rogatsch, H., Klocker, H., Langer, G., Nestl, A., & Cato, A. C. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7189-7197.2003 · Cited by 78 · see citing works
“For example, the molecular chaperone p23 has been shown to act at a late step in nuclear receptor action, promoting disassembly of the transcriptional regulatory complex (14, 16).”
BackgroundRegulation of cytosolic prostaglandin E synthase by phosphorylation.
Kobayashi, T., Nakatani, Y., Tanioka, T., Tsujimoto, M., Nakajo, S., Nakaya, K., Murakami, M., & Kudo, I. (2004) · Biochemical Journal · doi:10.1042/bj20040118 · Cited by 84 · see citing works
Modifying chromatin to permit steroid hormone receptor-dependent transcription
Kinyamu, H. K., & Archer, T. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.09.015 · Cited by 78 · see citing works
Proteolytic turnover of the Gal4 transcription factor is not required for function in vivo
Nalley, K., Johnston, S. A., & Kodadek, T. (2006) · Nature · doi:10.1038/nature05067 · Cited by 82 · see citing works
Glucocorticoid receptor dynamics and gene regulation
Biddie, S. C., & Hager, G. L. (2008) · Stress · doi:10.1080/10253890802506409 · Cited by 73 · see citing works
“Introducing a cognate peptide of the TR interaction surface of the GRIP1 coactivator in vitro at TR-thyroid response element (TRE) complexes resulted in competitive stabilization against p23-mediated dissociation of the complex (Freeman et al. 2000).”
BackgroundBhattacharya, K., & Picard, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03962-z · Cited by 73 · see citing works
Protein dynamics in the nuclear compartment
Hager, G. L., Elbi, C., & Becker, M. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00278-2 · Cited by 72 · see citing works
Toxicology mechanism of the persistent organic pollutants (POPs) in fish through AhR pathway
Zhou, H., Wu, H., Liao, C., Diao, X., Jiping, Z., Chen, L., & Xue, Q. (2010) · Toxicology Mechanisms and Methods · doi:10.3109/15376516.2010.485227 · Cited by 71 · see citing works
“The phosphoprotein p23 is a small, acidic protein that is ubiquitously expressed in virtually all tissues highly conserved protein from yeast to humans, (Freeman et al. 2000).”
BackgroundMini-review: Foldosome regulation of androgen receptor action in prostate cancer
Cano, L. Q., Lavery, D. N., & Bevan, C. L. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.01.023 · Cited by 70 · see citing works
Structure and Function of the Glucocorticoid Receptor Ligand Binding Domain
Bledsoe, R. K., Stewart, E. L., & Pearce, K. H. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)68002-2 · Cited by 68 · see citing works
Morales, J. L., & Perdew, G. H. (2006) · Biochemistry · doi:10.1021/bi062165b · Cited by 64 · 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
“However, (b) the p23Δ94 mutant (1-122) reveals significant changes of the chemical shifts.”
BackgroundMolecular Cochaperones: Tumor Growth and Cancer Treatment
Calderwood, S. K. (2013) · Scientifica · doi:10.1155/2013/217513 · Cited by 63 · see citing works
“The mechanisms which underlie the elevated expression of molecular chaperones of the HSPA and HSPD families in cancer are currently unclear but may involve the dysregulation of transcription factor HSF1 first shown to couple stress to HSP transcription [8, 26].”
BackgroundInfluentialSimpson, N., Lambert, W. M., Watkins, R. A., Giashuddin, S., Huang, S., Oxelmark, E., Arju, R., Hochman, T., Goldberg, J. D., Schneider, R. J., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1590 · Cited by 11 · see citing works
“p23 acts as a cochaperone, stabilizing the ATP-bound form of Hsp90, thereby stabilizing Hsp90 interactions with steroid receptors (SR) (3) and assisting Hsp90 in increasing the hormone binding affinities of many SRs (4-6).”
Fang, L., Ricketson, D., Getubig, L., & Darimont, B. D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609163103 · Cited by 61 · see citing works
Rao, J., Lee, P., Benzeno, S., Cardozo, C., Albertus, J. A., Robins, D. M., & Caplan, A. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007385200 · Cited by 60 · see citing works
BAG-1 family of cochaperones in the modulation of nuclear receptor action
Cato, A. C. B., & Mink, S. (2001) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(01)00114-5 · Cited by 60 · see citing works
Schmidt, 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
The Ligand Binding Domain Controls Glucocorticoid Receptor Dynamics Independent of Ligand Release
Meijsing, S. H., Elbi, C., Luecke, H. F., Hager, G. L., & Yamamoto, K. R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01570-06 · Cited by 58 · see citing works
“Furthermore, studies in vitro and in vivo have shown that the destabilizing effect of p23 can be countered by receptor binding to GRIP (12, 13), a transcriptional coregulatory factor that interacts with the GR LBD.”
BackgroundResultInfluentialSelf-citationHollingshead, B. D., Petrulis, J. R., & Perdew, G. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407840200 · Cited by 55 · see citing works
Walther, R. F., Lamprecht, C., Ridsdale, A., Groulx, I., Lee, S., Lefebvre, Y. A., & Haché, R. J. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306356200 · Cited by 55 · see citing works
Reebye, V., Querol Cano, L., Lavery, D. N., Brooke, G. N., Powell, S. M., Chotai, D., Walker, M. M., Whitaker, H. C., Wait, R., Hurst, H. C., et al. (2012) · Molecular Endocrinology · doi:10.1210/me.2012-1056 · Cited by 47 · see citing works
“(15) reported it as inhibiting AR activity, whereas Fang et al.”
BackgroundInfluentialAllosteric Effects of Dexamethasone and RU486 on Glucocorticoid Receptor-DNA Interactions
Pandit, S., Geissler, W. M., Harris, G., & Sitlani, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105438200 · Cited by 49 · see citing works
NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems
Biebl, M. M., Delhommel, F., Faust, O., Żak, K. M., Agam, G. N., Guo, X., Mühlhofer, M., Dahiya, V., Hillebrand, D., Popowicz, G. M., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.12.031 · Cited by 48 · see citing works
The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically
Abbas‐Terki, T., Briand, P.-A., Donzé, O., & Picard, D. (2002) · Biological Chemistry · doi:10.1515/bc.2002.152 · Cited by 47 · see citing works
“…at least in some cases, to the stability and/or specificity of Hsp90-substrate complexes through direct contacts with the Hsp90 substrates (Hu et al., 1997; Silverstein et al., 1998; Grammatikakis et al., 1999; Freeman et al., 2000; Hartson et al., 2000; Donzé et al., 2001; Shao et al., 2001).”
BackgroundWang, Y., Thuillier, R., & Culty, M. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.104.030205 · Cited by 47 · see citing works
Zelin, E., Zhang, Y., Toogun, O. A., Zhong, S., & Freeman, B. C. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.026 · Cited by 46 · see citing works
“Molecular chaperones have been shown to promote the assembly and disassembly of diverse protein DNA complexes, including transcription and telomere structures (Freeman et al., 2000; Freeman and Yamamoto, 2002; Toogun et al., 2007, 2008; DeZwaan et al., 2009; DeZwaan and Freeman, 2010).”
Self-citationCo-chaperone p23 Regulates C. elegans Lifespan in Response to Temperature
Horikawa, M., Sural, S., Hsu, A., & Antebi, A. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005023 · Cited by 44 · see citing works
“The p23-HSP90 complex also regulates type II nuclear receptors, such as the thyroid receptor [20], which constitutively reside in the nucleus, a situation more resembling that of DAF-12.”
Inhibition of GR‐mediated transcription by p23 requires interaction with Hsp90
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
The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system
Cox, M. B., & Miller, C. A. (2002) · Toxicology Letters · doi:10.1016/s0378-4274(01)00465-9 · Cited by 43 · see citing works
“Steroid hormone receptor signaling pathways constructed in yeast are affected by the absence of Sba1, the yeast homolog of p23 (Freeman et al., 2000; Knoblauch and Garabedian, 1999).”
BackgroundResultGold, B. G., & Zhong, Y. (2004) · Neurosignals · doi:10.1159/000076565 · Cited by 43 · see citing works
Taguwa, S., Kambara, H., Omori, H., Tani, H., Abe, T., Mori, Y., Suzuki, T., Yoshimori, T., Moriishi, K., & Matsuura, Y. (2009) · Journal of Virology · doi:10.1128/jvi.01035-09 · Cited by 41 · see citing works
Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90.
Picard, D. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.10.009 · Cited by 38 · see citing works
Weeks, S. A., & Miller, D. J. (2007) · Journal of Virology · doi:10.1128/jvi.02017-07 · Cited by 40 · see citing works
“Wild-type (wt) BY4743 and diploid strains with homozygous deletions of SBA1, STI1, or YDJ1 were purchased from the American Type Culture Collection (Manassas, VA).”
BackgroundInfluentialIdentification 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 · see citing works
Hsp70–RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor
Schneikert, J., Hübner, S., Langer, G., Petri, T., Jäättelä, M., Reed, J., & Cato, A. C. B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.23.6508 · Cited by 40 · see citing works
Regulation of Androgen Receptor-Mediated Transcription by RPB5 Binding Protein URI/RMP
Mita, P., Savas, J. N., Djouder, N., Yates, J. R., Ha, S., Ruoff, R., Schafler, E. D., Nwachukwu, J. C., Tanese, N., Cowan, N. J., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05429-11 · Cited by 39 · see citing works
“The p23/hsp90 complex (R2TP complex) regulates the estrogen receptor (ER), and in particular, the small chaperone p23 was reported to affect the binding of ER to chromatin (10, 19).”
BackgroundDahiya, V., Rutz, D. A., Moessmer, P., Mühlhofer, M., Lawatscheck, J., Rief, M., & Büchner, J. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.01.016 · Cited by 39 · see citing works
Echeverría, P. C., Briand, P.-A., & Picard, D. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.01099-15 · Cited by 39 · see citing works
“An altered efficacy can be an indication for a mechanism that 292 affects post-maturation events such as the dynamic and Hsp90-independent 293 recycling of GR transactivation complexes by p23 at the chromatin (28).”
BackgroundInfluentialOxelmark, 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
- Authors
- Freeman, B. C., Felts, S. J., Toft, D. O., & Yamamoto, K. R.
- Affiliations
- Mayo Clinic (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-02-15
- Volume
- 14
- Issue
- 4
- Pages
- 422-434
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC316379
- OpenAlex
- W2156437614
- Cited by
- 168
- References
- 65
- Citations by year
- 2025: 3 · 2023: 3 · 2022: 4 · 2021: 3 · 2020: 1 · 2019: 4 · 2018: 4 · 2017: 5 · 2016: 4 · 2015: 5 · 2014: 6 · 2013: 5 · 2012: 7
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Leukemia Research Foundation
- National Institutes of Health (Hsp70)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- p23, molecular chaperones, intracellular receptors, HSP90, ligand efficacy, transcriptional activation, receptor recycling, signal transduction, tissue-specific gene expression
- MeSH terms
- Prostaglandin-E Synthases, Amino Acid Sequence, Animals, DNA, Fungal Proteins, HeLa Cells, Hormones, Humans, Intracellular Fluid, Ligands, Molecular Sequence Data, Organ Specificity, Phosphoproteins, Protein Binding, Receptors, Steroid, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Transfection, Tretinoin, Receptors, Retinoic Acid, Molecular Chaperones, HSP90 Heat-Shock Proteins, Intramolecular Oxidoreductases, Protein Isoforms, Saccharomyces cerevisiae Proteins, Mice, Rats
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