Cited by 106Heat shock proteins researchGenomics and Chromatin DynamicsBacterial Genetics and Biotechnology

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Genetic and Biochemical Analysis of p23 and Ansamycin Antibiotics in the Function of Hsp90-Dependent Signaling Proteins

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Bohen, Sean P.·1998·Molecular and Cellular Biology

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Abstract

The ubiquitous molecular chaperone Hsp90 acts in concert with a cohort of associated proteins to facilitate the functional maturation of a number of cellular signaling proteins, such as steroid hormone receptors and oncogene tyrosine kinases. The Hsp90-associated protein p23 is required for the assembly of functional steroid aporeceptor complexes in cell lysates, and Hsp90-binding ansamycin antibiotics disrupt the activity of Hsp90-dependent signaling proteins in cultured mammalian cells and prevent the association of p23 with Hsp90-receptor heterocomplexes; these observations have led to the hypotheses that p23 is required for the maturation of Hsp90 target proteins and that ansamycin antibiotics abrogate the activity of such proteins by disrupting the interaction of p23 with Hsp90. In this study, I demonstrate that ansamycin antibiotics disrupt the function of Hsp90 target proteins expressed in yeast cells; prevent the assembly of Sba1, a yeast p23-like protein, into steroid receptor-Hsp90 complexes; and result in the assembly of receptor-Hsp90 complexes that are defective for ligand binding. To assess the role of p23 in Hsp90 target protein function, I show that the activity of Hsp90 target proteins is unaffected by deletion of SBA1. Interestingly, steroid receptor activity in cells lacking Sba1 displays increased sensitivity to ansamycin antibiotics, and this phenotype is rescued by the expression of human p23 in yeast cells. These findings indicate that Hsp90-dependent signaling proteins can achieve a functional conformation in vivo in the absence of p23. Furthermore, while the presence of p23 decreases the sensitivity of Hsp90-dependent processes to ansamycin treatment, ansamycin antibiotics disrupt signaling through some mechanism other than altering the Hsp90-p23 interaction.

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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae.
Sikorski, R. S., & Hieter, P. (1989) · Genetics · doi:10.1093/genetics/122.1.19 · Cited by 8,590
The Steroid and Thyroid Hormone Receptor Superfamily
Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,394
Getting started with yeast
Sherman, F. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94004-v · Cited by 4,078
Improved method for high efficiency transformation of intact yeast cells.
Gietz, D., Jean, A. S., Woods, R. A., & Schiestl, R. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.6.1425 · Cited by 3,379
STEROID RECEPTOR REGULATED TRANSCRIPTION OF SPECIFIC GENES AND GENE NETWORKS
Yamamoto, K. R. (1985) · Annual Review of Genetics · doi:10.1146/annurev.ge.19.120185.001233 · Cited by 1,850
Multifunctional yeast high-copy-number shuttle vectors
Christianson, T., Sikorski, R. S., Dante, M., Shero, J. H., & Hieter, P. (1992) · Gene · doi:10.1016/0378-1119(92)90454-w · Cited by 1,660
Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent
Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370
Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone
Prodromou, C., Roe, S. M., O’Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,258
The Biology of heat shock proteins and molecular chaperones.
Morimoto, R. I., Tissieres, A., & Georgopoulos, C. P. (1994) · Cited by 1,244
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
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
The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation
Grenert, J. P., Sullivan, W. P., Fadden, P., Haystead, T., Clark, J., Mimnaugh, E. G., Krutzsch, H. C., Ochel, H.-J., Schulte, T. W., Sausville, E. A., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23843 · Cited by 568
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
The common 90‐kd protein component of non‐transformed ‘8S’ steroid receptors is a heat‐shock protein.
CATELLI, M. G., Binart, N., Jung‐Testas, I., Renoir, J., Baulieu, E. E., Feramisco, J. R., & Wj, W. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04055.x · Cited by 516
Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent
Supko, J. G., Hickman, R. L., Grever, M. R., & Malspeis, L. (1995) · Cancer Chemotherapy and Pharmacology · doi:10.1007/bf00689048 · Cited by 512
The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
Nelson, R., Ziegelhoffer, T., Nicolet, C. M., Werner‐Washburne, M., & Craig, E. A. (1992) · Cell · doi:10.1016/0092-8674(92)90269-i · Cited by 512
Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.
Sánchez, E. R., Toft, D. O., Schlesinger, M. J., & Pratt, W. B. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38886-5 · Cited by 482
Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association
Schulte, T. W., Blagosklonny, M. V., Ingui, C., & Neckers, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24585 · Cited by 457
Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement
Godowski, P. J., Rusconi, S., Miesfeld, R. L., & Yamamoto, K. R. (1987) · Nature · doi:10.1038/325365a0 · Cited by 420
Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416
Evidence That the 90-kDa Heat Shock Protein Is Necessary for the Steroid Binding Conformation of the L Cell Glucocorticoid Receptor
Bresnick, E. H., Dalman, F. C., Sánchez, E. R., & Pratt, W. B. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83689-4 · Cited by 384
The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor
Vegeto, E., Allan, G. F., Schrader, W. T., Tsai, M., McDonnell, D. P., & O’Malley, B. W. (1992) · Cell · doi:10.1016/0092-8674(92)90234-4 · Cited by 376
Complete DNA sequence of yeast chromosome XI
Dujon, B., Alexandraki, D., André, B., Ansorge, W. J., Baladrón, V., Ballesta, J. P. G., Bánrévi, A., Bolle, P. A., Bolotin‐Fukuhara, M., Bossier, P., et al. (1994) · Nature · doi:10.1038/369371a0 · Cited by 374
Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.
Blagosklonny, M. V., Toretsky, J. A., Bohen, S. P., & Neckers, L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8379 · Cited by 312
Self-citation
Mammalian Glucocorticoid Receptor Derivatives Enhance Transcription in Yeast
Schena, M., & Yamamoto, K. R. (1988) · Science · doi:10.1126/science.3043665 · Cited by 309
Dynamics of heat shock protein 90–progesterone receptor binding and the disactivation loop model for steroid receptor complexes
Smith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300
Progesterone Receptor Structure and Function Altered by Geldanamycin, an hsp90-Binding Agent
Smith, D. F., Whitesell, L. J., Nair, S. C., Chen, S., Prapapanich, V., & Rimerman, R. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.6804 · Cited by 289
Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila
Cutforth, T. (1994) · Cell · doi:10.1016/0092-8674(94)90442-1 · Cited by 287
Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery
Dittmar, K. D., Demady, D. R., Stancato, L. F., Krishna, P., & Pratt, W. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21213 · Cited by 265
Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
Whitesell, L. J., & Cook, P. (1996) · Molecular Endocrinology · doi:10.1210/mend.10.6.8776730 · Cited by 263
A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.
Aligue, R., Akhavan‐Niak, H., & Russell, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06956.x · Cited by 261
Quantitation and Intracellular Localization of the 85K Heat Shock Protein by Using Monoclonal and Polyclonal Antibodies
Lai, B.-T., Chin, N. W., Stanek, A. E., Keh, W., & Lanks, K. W. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.12.2802 · Cited by 243
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
Binding of p23 and hsp90 during assembly with the progesterone receptor.
Johnson, J. L., & Toft, D. O. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.6.8592513 · Cited by 233
A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23.
Johnson, J. L., & Toft, D. O. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31487-4 · Cited by 229
Role of the Protein Chaperone YDJ1 in Establishing Hsp90-Mediated Signal Transduction Pathways
Kimura, Y., Yahara, I., & Lindquist, S. L. (1995) · Science · doi:10.1126/science.7761857 · Cited by 228
Interaction of the Rous Sarcoma Virus Protein pp60 src with the Cellular Proteins pp50 and pp90
Brugge, J. S. (1986) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-70810-7_1 · Cited by 225
A Cyclophilin Function in Hsp90-Dependent Signal Transduction
Duina, A. A., Foreman, H.-C. C., Marsh, J. A., Lindquist, S. L., & Gaber, R. F. (1996) · Science · doi:10.1126/science.274.5293.1713 · Cited by 224
[31] Use and selectivity of herbimycin A as inhibitor of protein-tyrosine kinases
Uehara, Y., & Fukazawa, H. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)01033-x · Cited by 216
In Vivo Analysis of the Hsp90 Cochaperone Sti1 (p60)
Foreman, H.-C. C., Nathan, D. F., & Lindquist, S. L. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.318 · Cited by 214
Functional Specificity Among Hsp70 Molecular Chaperones
James, P. M., Pfund, C., & Craig, E. A. (1997) · Science · doi:10.1126/science.275.5298.387 · Cited by 202
The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein.
Wilhelmsson, A., Cuthill, S., Denis, M. G., Wikström, A., Gustafsson, J.-Å., & Poellinger, L. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08081.x · Cited by 198
Characterization of a Novel 23-Kilodalton Protein of Unactive Progesterone Receptor Complexes
Johnson, J. L., Beito, T. G., Krco, C. J., & Toft, D. O. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.3.1956 · Cited by 197
Hold 'em and Fold 'em: Chaperones and Signal Transduction
Bohen, S. P., Kralli, A., & Yamamoto, K. R. (1995) · Science · doi:10.1126/science.7761850 · Cited by 196
Self-citation
Isolation of Hsp90 mutants by screening for decreased steroid receptor function.
Bohen, S. P., & Yamamoto, K. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11424 · Cited by 195
Self-citation
Folding of the Glucocorticoid Receptor by the Reconstituted hsp90-based Chaperone Machinery
Dittmar, K. D., & Pratt, W. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13047 · Cited by 183
Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events.
Smith, D. F., Stensgard, B. A., Welch, W. J., & Toft, D. O. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48438-4 · Cited by 174
Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90.
Hutchison, K. A., Dittmar, K. D., Czar, M. J., & Pratt, W. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37651-2 · Cited by 165
The Function of Steroid Hormone Receptors Is Inhibited by the hsp90-specific Compound Geldanamycin
Segnitz, B., & Gehring, U. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18694 · Cited by 160
LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones.
Kralli, A., Bohen, S. P., & Yamamoto, K. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4701 · Cited by 160
Self-citation
Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae.
Chang, H.-C., & Lindquist, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31486-2 · Cited by 158
Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.
Murphy, S. M., Bergman, M., & Morgan, D. O. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5290 · Cited by 130
The 23-kDa Acidic Protein in Reticulocyte Lysate Is the Weakly Bound Component of the hsp Foldosome That Is Required for Assembly of the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90
Hutchison, K. A., Stancato, L. F., Owens-Grillo, J. K., Johnson, J. L., Krishna, P., Toft, D. O., & Pratt, W. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18841 · Cited by 125
An FK506-sensitive Transporter Selectively Decreases Intracellular Levels and Potency of Steroid Hormones
Kralli, A., & Yamamoto, K. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.17152 · Cited by 123
Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast.
Garabedian, M. J., & Yamamoto, K. R. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.11.1245 · Cited by 103
Retinoic acid receptor belongs to a subclass of nuclear receptors that do not form "docking" complexes with hsp90
Dalman, F. C., Sturzenbecker, L. J., Levin, A. A., Lucas, D. A., Perdew, G. H., Petkovitch, M., Chambon, P., Grippo, J. F., & Pratt, W. B. (1991) · Biochemistry · doi:10.1021/bi00236a038 · Cited by 90
Protein components of the nonactivated glucocorticoid receptor.
Rexin, M., Busch, W., & Gehring, U. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54271-x · Cited by 82
A role for Hsp90 in retinoid receptor signal transduction.
Holley, S., & Yamamoto, K. R. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.12.1833 · Cited by 82
The viral erbA oncogene protein, a constitutive repressor in animal cells, is a hormone-regulated activator in yeast
Privalsky, M. L., Sharif, M., & Yamamoto, K. R. (1990) · Cell · doi:10.1016/0092-8674(90)90423-c · Cited by 75
[Experimental study of glucocorticoid in the treatment of acute respiratory distress syndrome induced by E.coli].
Song, Z.-F., Xie, W., Shan, H.-M., Guo, X.-H., & Sun, B. (2006) · PubMed · doi:10.1101/087969427.26.313 · Cited by 66
Growth inhibition of virus transformed cells in vitro and antitumor activity in vivo of geldanamycin and its derivatives.
Sasaki, K., Yasuda, H., & Onodera, K. (1979) · The Journal of Antibiotics · doi:10.7164/antibiotics.32.849 · Cited by 65
Reconstitution of retinoid X receptor function and combinatorial regulation of other nuclear hormone receptors in the yeast Saccharomyces cerevisiae.
Hall, B. L., Smit‐McBride, Z., & Privalsky, M. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.6929 · Cited by 64
A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex
Pratt, W. B., Scherrer, L. C., Hutchison, K. A., & Dalman, F. C. (1992) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(92)90348-m · Cited by 60
Macbecins I and II, new antitumor antibiotics. I. Producing organism, fermentation and antimicrobial activities.
TANIDA, S., HASEGAWA, T., & Higashide, E. (1980) · The Journal of Antibiotics · doi:10.7164/antibiotics.33.199 · Cited by 52
A heat shock protein complex isolated from rabbit reticulocyte lysate can reconstitute a functional glucocorticoid receptor-Hsp90 complex
Scherrer, L. C., Hutchison, K. A., Sánchez, E. R., Randall, S. K., & Pratt, W. B. (1992) · Biochemistry · doi:10.1021/bi00147a017 · Cited by 49
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
Self-citation
Macbecins I and II, new antitumor antibiotics. II. Isolation and characterization.
Muroi, M., Izawa, M., KOSAI, Y., & Asai, M. (1980) · The Journal of Antibiotics · doi:10.7164/antibiotics.33.205 · Cited by 43
Heterotetrameric structure of the human progesterone receptor.
Rehberger, P. A., Rexin, M., & Gehring, U. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.17.8001 · Cited by 36
Antitumor and cytocidal activities of a newly isolated benzenoid ansamycin, macbecin I.
Ono, Y., Kozai, Y., & Ootsu, K. (1982) · PubMed · Cited by 10

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Research works printed but not linked: 4

10.1128/mcb.9.9.3919-3930.1989 · DOI · Paper page
10.1128/mcb.14.3.1956-1963.1994 · DOI
10.1128/mcb.4.12.2802-2810.1984 · DOI
10.1128/mcb.13.9.5290-5300.1993 · DOI

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Authors: Bohen, S. P.
Affiliations: National Institutes of Health (US)
Corresponding author: Bohen, Sean P.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1998-06
Volume: 18
Issue: 6
Pages: 3330-3339
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.18.6.3330
PMC: PMC108914
OpenAlex: W1827557434
Cited by: 106
References: 70
Citations by year: 2024: 1 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 3
FWCI: 3.72
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute for Health and Care Research
National Institutes of Health
National Cancer Institute
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: HSP90, p23, ansamycin antibiotics, steroid hormone receptors, molecular chaperones, ligand binding, protein maturation
MeSH terms: Amino Acid Sequence, Anti-Bacterial Agents, Antibiotics, Antineoplastic, DNA-Binding Proteins, Humans, Molecular Sequence Data, Phenotype, Protein-Tyrosine Kinases, Quinones, Receptors, Steroid, Saccharomyces cerevisiae, Signal Transduction, Oncogene Protein pp60(v-src), Benzoquinones, Sequence Alignment, HSP90 Heat-Shock Proteins, Lactams, Macrocyclic

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Genetic and Biochemical Analysis of p23 and Ansamycin Antibiotics in the Function of Hsp90-Dependent Signaling Proteins

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