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Volumn 74, Issue 7, 2009, Pages 568-572

Scaffolding actions of membrane-associated progesterone receptors

Author keywords

c Src; CD domain; MEK1; Progesterone receptor; Rapid kinase activation; Scaffold

Indexed keywords

ESTROGEN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; PROGESTERONE; PROGESTERONE RECEPTOR; PROGESTERONE RECEPTOR A; PROGESTERONE RECEPTOR B; PROGESTERONE RECEPTOR C; PROTEIN KINASE; SCAFFOLD PROTEIN; STEROID RECEPTOR; UNCLASSIFIED DRUG;

EID: 63749084159     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2008.12.004     Document Type: Review
Times cited : (32)

References (37)
  • 1
    • 0025239785 scopus 로고
    • Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B
    • Kastner P., Krust A., Turcotte B., Stropp U., Tora L., Gronemeyer H., et al. Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B. EMBO J 9 (1990) 1603-1614
    • (1990) EMBO J , vol.9 , pp. 1603-1614
    • Kastner, P.1    Krust, A.2    Turcotte, B.3    Stropp, U.4    Tora, L.5    Gronemeyer, H.6
  • 2
    • 0030816914 scopus 로고    scopus 로고
    • An N-terminally truncated third progesterone receptor protein, PR(C), forms heterodimers with PR(B) but interferes in PR(B)-DNA binding
    • Wei L.L., Norris B.M., and Baker C.J. An N-terminally truncated third progesterone receptor protein, PR(C), forms heterodimers with PR(B) but interferes in PR(B)-DNA binding. J Steroid Biochem Mol Biol 62 4 (1997) 287-297
    • (1997) J Steroid Biochem Mol Biol , vol.62 , Issue.4 , pp. 287-297
    • Wei, L.L.1    Norris, B.M.2    Baker, C.J.3
  • 3
    • 33645406947 scopus 로고    scopus 로고
    • Up-regulation of the progesterone receptor (PR)-C isoform in laboring myometrium by activation of nuclear factor-kappaB may contribute to the onset of labor through inhibition of PR function
    • Condon J.C., Hardy D.B., Kovaric K., and Mendelson C.R. Up-regulation of the progesterone receptor (PR)-C isoform in laboring myometrium by activation of nuclear factor-kappaB may contribute to the onset of labor through inhibition of PR function. Mol Endocrinol 20 4 (2006) 764-775
    • (2006) Mol Endocrinol , vol.20 , Issue.4 , pp. 764-775
    • Condon, J.C.1    Hardy, D.B.2    Kovaric, K.3    Mendelson, C.R.4
  • 4
    • 0035919191 scopus 로고    scopus 로고
    • Reproductive functions of the progesterone receptor isoforms: lessons from knock-out mice
    • Conneely O.M., Mulac-Jericevic B., Lydon J.P., De F.J., and Mayo. Reproductive functions of the progesterone receptor isoforms: lessons from knock-out mice. Mol Cell Endocrinol 179 1/2 (2001) 97-103
    • (2001) Mol Cell Endocrinol , vol.179 , Issue.1-2 , pp. 97-103
    • Conneely, O.M.1    Mulac-Jericevic, B.2    Lydon, J.P.3    De Mayo, F.J.4
  • 5
    • 0029115517 scopus 로고
    • Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities
    • Lydon J.P., DeMayo F.J., Funk C.R., Mani S.K., Hughes A.R., Montgomery C.A., et al. Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities. Genes Dev 9 (1995) 2266-2278
    • (1995) Genes Dev , vol.9 , pp. 2266-2278
    • Lydon, J.P.1    DeMayo, F.J.2    Funk, C.R.3    Mani, S.K.4    Hughes, A.R.5    Montgomery, C.A.6
  • 6
    • 0042693019 scopus 로고    scopus 로고
    • Defective mammary gland morphogenesis in mice lacking the progesterone receptor B isoform
    • Mulac-Jericevic B., Lydon J.P., DeMayo F.J., and Conneely O.M. Defective mammary gland morphogenesis in mice lacking the progesterone receptor B isoform. Proc Natl Acad Sci USA 100 17 (2003) 9744-9749
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.17 , pp. 9744-9749
    • Mulac-Jericevic, B.1    Lydon, J.P.2    DeMayo, F.J.3    Conneely, O.M.4
  • 7
    • 0031906819 scopus 로고    scopus 로고
    • Transgenic mice carrying an imbalance in the native ratio of A to B forms of progesterone receptor exhibit developmental abnormalities in mammary glands
    • Shyamala G., Yang X., Silberstein G., Barcellos-Hoff M.H., and Dale E. Transgenic mice carrying an imbalance in the native ratio of A to B forms of progesterone receptor exhibit developmental abnormalities in mammary glands. Proc Natl Acad Sci USA 95 2 (1998) 696-701
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.2 , pp. 696-701
    • Shyamala, G.1    Yang, X.2    Silberstein, G.3    Barcellos-Hoff, M.H.4    Dale, E.5
  • 8
    • 0037085303 scopus 로고    scopus 로고
    • Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells
    • Richer J.K., Jacobsen B.M., Manning N.G., Abel M.G., Wolf D.M., and Horwitz K.B. Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells. J Biol Chem 277 7 (2002) 5209-5218
    • (2002) J Biol Chem , vol.277 , Issue.7 , pp. 5209-5218
    • Richer, J.K.1    Jacobsen, B.M.2    Manning, N.G.3    Abel, M.G.4    Wolf, D.M.5    Horwitz, K.B.6
  • 9
    • 36849096094 scopus 로고    scopus 로고
    • Phosphorylation-dependent antagonism of sumoylation de-represses progesterone receptor action in breast cancer cells
    • Daniel A.R., Faivre E.J., and Lange C.A. Phosphorylation-dependent antagonism of sumoylation de-represses progesterone receptor action in breast cancer cells. Mol Endocrinol (2007)
    • (2007) Mol Endocrinol
    • Daniel, A.R.1    Faivre, E.J.2    Lange, C.A.3
  • 10
    • 0033967491 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome
    • Lange C.A., Shen T., and Horwitz K.B. Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc Natl Acad Sci USA 97 3 (2000) 1032-1037
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.3 , pp. 1032-1037
    • Lange, C.A.1    Shen, T.2    Horwitz, K.B.3
  • 11
    • 0023640540 scopus 로고
    • Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases
    • Rao K.V., Peralta W.D., Greene G.L., and Fox C.F. Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases. Biochem Biophys Res Commun 146 3 (1987) 1357-1365
    • (1987) Biochem Biophys Res Commun , vol.146 , Issue.3 , pp. 1357-1365
    • Rao, K.V.1    Peralta, W.D.2    Greene, G.L.3    Fox, C.F.4
  • 12
    • 0035896651 scopus 로고    scopus 로고
    • Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites
    • Knotts T.A., Orkiszewski R.S., Cook R.G., Edwards D.P., and Weigel N.L. Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites. J Biol Chem 276 11 (2001) 8475-8483
    • (2001) J Biol Chem , vol.276 , Issue.11 , pp. 8475-8483
    • Knotts, T.A.1    Orkiszewski, R.S.2    Cook, R.G.3    Edwards, D.P.4    Weigel, N.L.5
  • 13
    • 0029976989 scopus 로고    scopus 로고
    • Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptors
    • Takimoto G.S., Hovland A.R., Tasset D.M., Melville M.Y., Tung L., and Horwitz K.B. Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptors. J Biol Chem 271 23 (1996) 13308-13316
    • (1996) J Biol Chem , vol.271 , Issue.23 , pp. 13308-13316
    • Takimoto, G.S.1    Hovland, A.R.2    Tasset, D.M.3    Melville, M.Y.4    Tung, L.5    Horwitz, K.B.6
  • 14
    • 0029855010 scopus 로고    scopus 로고
    • Steroid hormone receptors and their regulation by phosphorylation
    • Weigel N.L. Steroid hormone receptors and their regulation by phosphorylation. Biochem J 319 Pt 3 (1996) 657-667
    • (1996) Biochem J , vol.319 , Issue.PART 3 , pp. 657-667
    • Weigel, N.L.1
  • 15
    • 0030923066 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo
    • Zhang Y., Beck C.A., Poletti A., Clement JPt, Prendergast P., Yip T.T., et al. Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo. Mol Endocrinol 11 6 (1997) 823-832
    • (1997) Mol Endocrinol , vol.11 , Issue.6 , pp. 823-832
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Clement JPt4    Prendergast, P.5    Yip, T.T.6
  • 16
    • 0027988153 scopus 로고
    • Identification of phosphorylation sites unique to the B form of human progesterone receptor. In vitro phosphorylation by casein kinase II
    • Zhang Y., Beck C.A., Poletti A., Edwards D.P., and Weigel N.L. Identification of phosphorylation sites unique to the B form of human progesterone receptor. In vitro phosphorylation by casein kinase II. J Biol Chem 269 49 (1994) 31034-31040
    • (1994) J Biol Chem , vol.269 , Issue.49 , pp. 31034-31040
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Edwards, D.P.4    Weigel, N.L.5
  • 17
    • 0029168036 scopus 로고
    • Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor
    • Zhang Y., Beck C.A., Poletti A., Edwards D.P., and Weigel N.L. Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor. Mol Endocrinol 9 8 (1995) 1029-1040
    • (1995) Mol Endocrinol , vol.9 , Issue.8 , pp. 1029-1040
    • Zhang, Y.1    Beck, C.A.2    Poletti, A.3    Edwards, D.P.4    Weigel, N.L.5
  • 18
    • 0037385535 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors
    • Qiu M., Olsen A., Faivre E., Horwitz K.B., and Lange C.A. Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors. Mol Endocrinol 17 4 (2003) 628-642
    • (2003) Mol Endocrinol , vol.17 , Issue.4 , pp. 628-642
    • Qiu, M.1    Olsen, A.2    Faivre, E.3    Horwitz, K.B.4    Lange, C.A.5
  • 19
    • 10044257416 scopus 로고    scopus 로고
    • Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase2
    • Pierson-Mullany L.K., and Lange C.A. Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase2. Mol Cell Biol 24 24 (2004)
    • (2004) Mol Cell Biol , vol.24 , Issue.24
    • Pierson-Mullany, L.K.1    Lange, C.A.2
  • 20
    • 0035726623 scopus 로고    scopus 로고
    • Transcriptional hyperactivity of human progesterone receptors is coupled to their ligand-dependent down-regulation by mitogen-activated protein kinase-dependent phosphorylation of serine 294
    • Shen T., Horwitz K.B., and Lange C.A. Transcriptional hyperactivity of human progesterone receptors is coupled to their ligand-dependent down-regulation by mitogen-activated protein kinase-dependent phosphorylation of serine 294. Mol Cell Biol 21 18 (2001) 6122-6131
    • (2001) Mol Cell Biol , vol.21 , Issue.18 , pp. 6122-6131
    • Shen, T.1    Horwitz, K.B.2    Lange, C.A.3
  • 21
    • 11144274562 scopus 로고    scopus 로고
    • Cyclin-dependent kinase activity is required for progesterone receptor function: novel role for cyclin A/Cdk2 as a progesterone receptor coactivator
    • Narayanan R., Adigun A.A., Edwards D.P., and Weigel N.L. Cyclin-dependent kinase activity is required for progesterone receptor function: novel role for cyclin A/Cdk2 as a progesterone receptor coactivator. Mol Cell Biol 25 1 (2005) 264-277
    • (2005) Mol Cell Biol , vol.25 , Issue.1 , pp. 264-277
    • Narayanan, R.1    Adigun, A.A.2    Edwards, D.P.3    Weigel, N.L.4
  • 23
    • 0034852802 scopus 로고    scopus 로고
    • Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases
    • Boonyaratanakornkit V., Scott M.P., Ribon V., Sherman L., Anderson S.M., Maller J.L., et al. Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases. Mol Cell 8 2 (2001) 269-280
    • (2001) Mol Cell , vol.8 , Issue.2 , pp. 269-280
    • Boonyaratanakornkit, V.1    Scott, M.P.2    Ribon, V.3    Sherman, L.4    Anderson, S.M.5    Maller, J.L.6
  • 24
    • 0032036584 scopus 로고    scopus 로고
    • Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-talk with estrogen receptor
    • Migliaccio A., Piccolo D., Castoria G., Di Domenico M., Bilancio A., Lombardi M., et al. Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-talk with estrogen receptor. EMBO J 17 7 (1998) 2008-2018
    • (1998) EMBO J , vol.17 , Issue.7 , pp. 2008-2018
    • Migliaccio, A.1    Piccolo, D.2    Castoria, G.3    Di Domenico, M.4    Bilancio, A.5    Lombardi, M.6
  • 25
    • 0037371863 scopus 로고    scopus 로고
    • Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Erk pathway in mammalian cells
    • Ballare C., Uhrig M., Bechtold T., Sancho E., Di Domenico M., Migliaccio A., et al. Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Erk pathway in mammalian cells. Mol Cell Biol 23 6 (2003) 1994-2008
    • (2003) Mol Cell Biol , vol.23 , Issue.6 , pp. 1994-2008
    • Ballare, C.1    Uhrig, M.2    Bechtold, T.3    Sancho, E.4    Di Domenico, M.5    Migliaccio, A.6
  • 26
    • 33846581488 scopus 로고    scopus 로고
    • The role of extranuclear signaling actions of progesterone receptor in mediating progesterone regulation of gene expression and the cell cycle
    • Boonyaratanakornkit V., McGowan E., Sherman L., Mancini M.A., Cheskis B.J., and Edwards D.P. The role of extranuclear signaling actions of progesterone receptor in mediating progesterone regulation of gene expression and the cell cycle. Mol Endocrinol 21 2 (2007) 359-375
    • (2007) Mol Endocrinol , vol.21 , Issue.2 , pp. 359-375
    • Boonyaratanakornkit, V.1    McGowan, E.2    Sherman, L.3    Mancini, M.A.4    Cheskis, B.J.5    Edwards, D.P.6
  • 28
    • 0345732643 scopus 로고    scopus 로고
    • A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration
    • Murphy L.O., MacKeigan J.P., and Blenis J. A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration. Mol Cell Biol 24 1 (2004) 144-153
    • (2004) Mol Cell Biol , vol.24 , Issue.1 , pp. 144-153
    • Murphy, L.O.1    MacKeigan, J.P.2    Blenis, J.3
  • 29
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy L.O., Smith S., Chen R.H., Fingar D.C., and Blenis J. Molecular interpretation of ERK signal duration by immediate early gene products. Nat Cell Biol 4 8 (2002) 556-564
    • (2002) Nat Cell Biol , vol.4 , Issue.8 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 30
    • 0032749494 scopus 로고    scopus 로고
    • Identification of a cytoplasmic-retention sequence in ERK2
    • Rubinfeld H., Hanoch T., and Seger R. Identification of a cytoplasmic-retention sequence in ERK2. J Biol Chem 274 43 (1999) 30349-30352
    • (1999) J Biol Chem , vol.274 , Issue.43 , pp. 30349-30352
    • Rubinfeld, H.1    Hanoch, T.2    Seger, R.3
  • 31
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates, activators and regulators
    • Tanoue T., Adachi M., Moriguchi T., and Nishida E. A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat Cell Biol 2 2 (2000) 110-116
    • (2000) Nat Cell Biol , vol.2 , Issue.2 , pp. 110-116
    • Tanoue, T.1    Adachi, M.2    Moriguchi, T.3    Nishida, E.4
  • 33
    • 33846590071 scopus 로고    scopus 로고
    • Interaction with MEK causes nuclear export and downregulation of peroxisome proliferator-activated receptor gamma
    • Burgermeister E., Chuderland D., Hanoch T., Meyer M., Liscovitch M., and Seger R. Interaction with MEK causes nuclear export and downregulation of peroxisome proliferator-activated receptor gamma. Mol Cell Biol 27 3 (2007) 803-817
    • (2007) Mol Cell Biol , vol.27 , Issue.3 , pp. 803-817
    • Burgermeister, E.1    Chuderland, D.2    Hanoch, T.3    Meyer, M.4    Liscovitch, M.5    Seger, R.6
  • 34
    • 41649119043 scopus 로고    scopus 로고
    • Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors
    • Faivre E.J., Daniel A.R., Hillard C.J., and Lange C.A. Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors. Mol Endocrinol 22 4 (2008) 823-837
    • (2008) Mol Endocrinol , vol.22 , Issue.4 , pp. 823-837
    • Faivre, E.J.1    Daniel, A.R.2    Hillard, C.J.3    Lange, C.A.4
  • 35
    • 0035990913 scopus 로고    scopus 로고
    • Docking interactions in the mitogen-activated protein kinase cascades
    • Tanoue T., and Nishida E. Docking interactions in the mitogen-activated protein kinase cascades. Pharmacol Ther 93 2/3 (2002) 193-202
    • (2002) Pharmacol Ther , vol.93 , Issue.2-3 , pp. 193-202
    • Tanoue, T.1    Nishida, E.2
  • 36
    • 0028833473 scopus 로고
    • Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro
    • Arnold S.F., Obourn J.D., Jaffe H., and Notides A.C. Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro. Mol Endocrinol 9 1 (1995) 24-33
    • (1995) Mol Endocrinol , vol.9 , Issue.1 , pp. 24-33
    • Arnold, S.F.1    Obourn, J.D.2    Jaffe, H.3    Notides, A.C.4
  • 37
    • 0029563173 scopus 로고
    • Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element
    • Arnold S.F., Vorojeikina D.P., and Notides A.C. Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element. J Biol Chem 270 50 (1995) 30205-30212
    • (1995) J Biol Chem , vol.270 , Issue.50 , pp. 30205-30212
    • Arnold, S.F.1    Vorojeikina, D.P.2    Notides, A.C.3


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