The glucocorticoid responses are shaped by molecular chaperones

[1]  M. Cohn,et al.  Essential Role for Co-chaperone Fkbp52 but Not Fkbp51 in Androgen Receptor-mediated Signaling and Physiology* , 2007, Journal of Biological Chemistry.

[2]  W. Wurst,et al.  The Hsp90 Cochaperone p23 Is Essential for Perinatal Survival , 2006, Molecular and Cellular Biology.

[3]  D. Picard.  Chaperoning steroid hormone action , 2006, Trends in Endocrinology & Metabolism.

[4]  L. Pearl,et al.  Structure and mechanism of the Hsp90 molecular chaperone machinery. , 2006, Annual review of biochemistry.

[5]  J. Buchner,et al.  The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90 , 2006, The EMBO journal.

[6]  D. Picard.  Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90. , 2006, Experimental cell research.

[7]  W. Pratt,et al.  Chaperoning of glucocorticoid receptors. , 2006, Handbook of experimental pharmacology.

[8]  Michael Sendtner,et al.  Bag1 is essential for differentiation and survival of hematopoietic and neuronal cells , 2005, Nature Neuroscience.

[9]  Joyce Cheung-Flynn,et al.  Physiological role for the cochaperone FKBP52 in androgen receptor signaling. , 2005, Molecular endocrinology.

[10]  Minoru Yoshida,et al.  HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. , 2005, Molecular cell.

[11]  W. Obermann,et al.  Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. , 2005, The Biochemical journal.

[12]  F. Holsboer,et al.  FK506-binding Proteins 51 and 52 Differentially Regulate Dynein Interaction and Nuclear Translocation of the Glucocorticoid Receptor in Mammalian Cells* , 2005, Journal of Biological Chemistry.

[13]  M. Mayer,et al.  Hsp70 chaperones: Cellular functions and molecular mechanism , 2005, Cellular and Molecular Life Sciences.

[14]  Jennifer M Harrell,et al.  Evidence for Glucocorticoid Receptor Transport on Microtubules by Dynein* , 2004, Journal of Biological Chemistry.

[15]  G. Blatch,et al.  Hop: more than an Hsp70/Hsp90 adaptor protein , 2004, BioEssays : news and reviews in molecular, cellular and developmental biology.

[16]  D. DeFranco,et al.  Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement. , 2004, Cellular signalling.

[17]  P. Roberts,et al.  The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor. , 2004, Molecular endocrinology.

[18]  M. Ljungman,et al.  Hsp90-binding Immunophilins Link p53 to Dynein During p53 Transport to the Nucleus* , 2004, Journal of Biological Chemistry.

[19]  S. Hooper,et al.  Altered epithelial cell proportions in the fetal lung of glucocorticoid receptor null mice. , 2004, American journal of respiratory cell and molecular biology.

[20]  K. Yamamoto,et al.  Importin 7 and Importin / Importin Are Nuclear Import Receptors for the Glucocorticoid Receptor , 2003 .

[21]  Jennifer M Harrell,et al.  Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation. , 2004, Brain research. Molecular brain research.

[22]  James G. McNally,et al.  Rapid Glucocorticoid Receptor Exchange at a Promoter Is Coupled to Transcription and Regulated by Chaperones and Proteasomes , 2004, Molecular and Cellular Biology.

[23]  Cem Elbi,et al.  Molecular chaperones function as steroid receptor nuclear mobility factors. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[24]  Jason C. Young,et al.  Inhibition of GR‐mediated transcription by p23 requires interaction with Hsp90 , 2004, FEBS letters.

[25]  K. Takano,et al.  Regulation of nuclear retention of glucocorticoid receptor by nuclear Hsp90 , 2004, Molecular and Cellular Endocrinology.

[26]  David F. Smith.  Tetratricopeptide repeat cochaperones in steroid receptor complexes , 2004, Cell stress & chaperones.

[27]  Heike Brand,et al.  Estrogen Receptor-α Directs Ordered, Cyclical, and Combinatorial Recruitment of Cofactors on a Natural Target Promoter , 2003, Cell.

[28]  R. Sunahara,et al.  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* , 2003, Journal of Biological Chemistry.

[29]  M. Morimoto,et al.  Yellow fluorescent protein-tagged and cyan fluorescent protein-tagged imaging analysis of glucocorticoid receptor and importins in single living cells. , 2003, Endocrinology.

[30]  R. Minchin,et al.  Immunophilin chaperones in steroid receptor signalling. , 2003, Current topics in medicinal chemistry.

[31]  D. Picard,et al.  The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo , 2003, The EMBO journal.

[32]  Holly McDonough,et al.  CHIP: a link between the chaperone and proteasome systems , 2003, Cell stress & chaperones.

[33]  Mingjie Zhang,et al.  Binding of hsp90-associated immunophilins to cytoplasmic dynein: direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain. , 2002, Biochemistry.

[34]  D. Picard,et al.  Heat-shock protein 90, a chaperone for folding and regulation , 2002, Cellular and Molecular Life Sciences CMLS.

[35]  L. Neckers,et al.  Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[36]  K. Yamamoto,et al.  Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones , 2002, Science.

[37]  D. Toft,et al.  HSP40 Binding Is the First Step in the HSP90 Chaperoning Pathway for the Progesterone Receptor* , 2002, The Journal of Biological Chemistry.

[38]  L. Neckers,et al.  Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. , 2002, Journal of the National Cancer Institute.

[39]  E. R. Sánchez,et al.  A New First Step in Activation of Steroid Receptors , 2002, The Journal of Biological Chemistry.

[40]  D. Moskophidis,et al.  Insights into Regulation and Function of the Major Stress-Induced hsp70 Molecular Chaperone In Vivo: Analysis of Mice with Targeted Gene Disruption of the hsp70.1 orhsp70.3 Gene , 2001, Molecular and Cellular Biology.

[41]  Keiji Tanaka,et al.  CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein , 2001, EMBO reports.

[42]  D. Cyr,et al.  CHIP Is a U-box-dependent E3 Ubiquitin Ligase , 2001, The Journal of Biological Chemistry.

[43]  C. Patterson,et al.  Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling , 2001, Current Biology.

[44]  D. Cyr,et al.  From the cradle to the grave: molecular chaperones that may choose between folding and degradation , 2001, EMBO reports.

[45]  B. Wasylyk,et al.  Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2. , 2001, Genes & development.

[46]  C. Young,et al.  Silymarin inhibits function of the androgen receptor by reducing nuclear localization of the receptor in the human prostate cancer cell line LNCaP. , 2001, Carcinogenesis.

[47]  R. Minchin,et al.  Estradiol-regulated expression of the immunophilins cyclophilin 40 and FKBP52 in MCF-7 breast cancer cells. , 2001, Biochemical and biophysical research communications.

[48]  M. Galigniana,et al.  Evidence That the Peptidylprolyl Isomerase Domain of the hsp90-binding Immunophilin FKBP52 Is Involved in Both Dynein Interaction and Glucocorticoid Receptor Movement to the Nucleus* , 2001, The Journal of Biological Chemistry.

[49]  Lars Packschies,et al.  Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange , 2001, Nature Structural Biology.

[50]  John Calvin Reed,et al.  hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1. , 2000, Biochemistry.

[51]  S. Kimmins,et al.  Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteins , 2000, Cell stress & chaperones (Print).

[52]  J. Schneikert,et al.  BAG-1M: a potential specificity determinant of corticosteroid receptor action. , 2000, Kidney international.

[53]  Luis Moroder,et al.  Structure of TPR Domain–Peptide Complexes Critical Elements in the Assembly of the Hsp70–Hsp90 Multichaperone Machine , 2000, Cell.

[54]  J. McNally,et al.  The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. , 2000, Science.

[55]  J. Höhfeld,et al.  The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the Proteasome* , 2000, The Journal of Biological Chemistry.

[56]  K. Yamamoto,et al.  The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. , 2000, Genes & development.

[57]  P. Gruss,et al.  Mice lacking HSP90beta fail to develop a placental labyrinth. , 2000, Development.

[58]  D. Picard.  Posttranslational regulation of proteins by fusions to steroid-binding domains. , 2000, Methods in enzymology.

[59]  P. Connell,et al.  The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins , 2000, Nature Cell Biology.

[60]  M. Galigniana,et al.  Different Regions of the Immunophilin FKBP52 Determine Its Association with the Glucocorticoid Receptor, hsp90, and Cytoplasmic Dynein* , 1999, The Journal of Biological Chemistry.

[61]  C. Hsiao,et al.  Specific Interaction of the 70-kDa Heat Shock Cognate Protein with the Tetratricopeptide Repeats* , 1999, The Journal of Biological Chemistry.

[62]  J. Schneikert,et al.  A Nuclear Action of the Eukaryotic Cochaperone Rap46 in Downregulation of Glucocorticoid Receptor Activity , 1999, The Journal of cell biology.

[63]  Y. Niyaz,et al.  The hsp70-associating protein Hap46 binds to DNA and stimulates transcription. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[64]  D. Toft,et al.  The Importance of ATP Binding and Hydrolysis by Hsp90 in Formation and Function of Protein Heterocomplexes* , 1999, The Journal of Biological Chemistry.

[65]  P. Connell,et al.  Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions , 1999, Molecular and Cellular Biology.

[66]  J. Reinstein,et al.  Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[67]  R. McMacken,et al.  DnaJ dramatically stimulates ATP hydrolysis by DnaK: insight into targeting of Hsp70 proteins to polypeptide substrates. , 1999, Biochemistry.

[68]  D. DeFranco,et al.  Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90. , 1999, Molecular endocrinology.

[69]  E. Baulieu,et al.  The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[70]  D. F. Smith,et al.  Glucocorticoid resistance in the squirrel monkey is associated with overexpression of the immunophilin FKBP51. , 1999, The Journal of clinical endocrinology and metabolism.

[71]  L. Muglia,et al.  Proliferation and differentiation defects during lung development in corticotropin-releasing hormone-deficient mice. , 1999, American journal of respiratory cell and molecular biology.

[72]  Chrisostomos Prodromou,et al.  Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)‐domain co‐chaperones , 1999, The EMBO journal.

[73]  David F. Smith,et al.  Hop as an Adaptor in the Heat Shock Protein 70 (Hsp70) and Hsp90 Chaperone Machinery* , 1998, The Journal of Biological Chemistry.

[74]  J. Song,et al.  BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release , 1998, The EMBO journal.

[75]  U. Gehring,et al.  Interference between Proteins Hap46 and Hop/p60, Which Bind to Different Domains of the Molecular Chaperone hsp70/hsc70 , 1998, Molecular and Cellular Biology.

[76]  W. Pratt,et al.  Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor–hsp90 Heterocomplex Assembly , 1998, Trends in Endocrinology & Metabolism.

[77]  S. Heck,et al.  RAP46 Is a Negative Regulator of Glucocorticoid Receptor Action and Hormone-induced Apoptosis* , 1998, The Journal of Biological Chemistry.

[78]  M. Galigniana,et al.  The Role of DnaJ-like Proteins in Glucocorticoid Receptor·hsp90 Heterocomplex Assembly by the Reconstituted hsp90·p60·hsp70 Foldosome Complex* , 1998, The Journal of Biological Chemistry.

[79]  U. Gehring,et al.  Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity , 1997, FEBS letters.

[80]  W. Pratt,et al.  Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery , 1997, The Journal of Biological Chemistry.

[81]  B. van der Burg,et al.  Novel Progesterone Target Genes Identified by an Improved Differential Display Technique Suggest That Progestin-induced Growth Inhibition of Breast Cancer Cells Coincides with Enhancement of Differentiation* , 1997, Journal of Biological Chemistry.

[82]  D. DeFranco,et al.  Subnuclear Trafficking of Glucocorticoid Receptors In Vitro: Chromatin Recycling and Nuclear Export , 1997, The Journal of cell biology.

[83]  M. Martin,et al.  Tissue distribution and abundance of human FKBP51, and FK506-binding protein that can mediate calcineurin inhibition. , 1997, Biochemical and biophysical research communications.

[84]  L. Whitesell,et al.  Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. , 1996, Molecular endocrinology.

[85]  D. Dix,et al.  Targeted gene disruption of Hsp70-2 results in failed meiosis, germ cell apoptosis, and male infertility. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[86]  D. DeFranco,et al.  Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking. , 1996, Molecular endocrinology.

[87]  K. Umesono,et al.  The nuclear receptor superfamily: The second decade , 1995, Cell.

[88]  F. Hartl,et al.  Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle , 1995, Cell.

[89]  M. Welsh,et al.  Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus. , 1995, Molecular endocrinology.

[90]  S. Lindquist,et al.  Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. , 1995, Science.

[91]  M. Welsh,et al.  The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor. , 1994, Molecular endocrinology.

[92]  E. Baulieu,et al.  In vivo functional protein-protein interaction: nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[93]  D. DeFranco,et al.  Bidirectional transport of glucocorticoid receptors across the nuclear envelope. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[94]  D. Toft,et al.  Steroid receptors and their associated proteins. , 1993, Molecular endocrinology.

[95]  A. Reik,et al.  Glucocorticoids are required for establishment and maintenance of an alteration in chromatin structure: induction leads to a reversible disruption of nucleosomes over an enhancer. , 1991, The EMBO journal.

[96]  R. Evans,et al.  Heat shock protein 90 as a critical factor in maintaining glucocorticosteroid receptor in a nonfunctional state. , 1991, The Journal of biological chemistry.

[97]  S. Meshinchi,et al.  Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex. , 1990, The Journal of biological chemistry.

[98]  J. Gustafsson,et al.  The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptor. , 1990, Biochemistry.

[99]  J. Funder,et al.  Mineralocorticoid action: target tissue specificity is enzyme, not receptor, mediated. , 1988, Science.

[100]  J. Gustafsson,et al.  Interaction of the glucocorticoid receptor with the Mr approximately 90,000 heat shock protein. , 1988, Biochemical Society transactions.

[101]  K. Yamamoto,et al.  A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor , 1988, Cell.

[102]  A. Munck,et al.  Kinetics of glucocorticoid-receptor complexes in rat thymus cells. , 1976, Journal of steroid biochemistry.