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Volumn 24, Issue 9, 2004, Pages 4038-4048

Negative Regulation of Prolactin Receptor Stability and Signaling Mediated by SCFβ-TrCP E3 Ubiquitin Ligase

Author keywords

[No Author keywords available]

Indexed keywords

F BOX PROTEIN; HORMONE RECEPTOR; MUTANT PROTEIN; PROLACTIN; PROLACTIN RECEPTOR; PROTEIN BETA TRCP2; PROTEIN SUBUNIT; SCF BETA TRCP E3 UBIQUITIN LIGASE; SERINE; STAT5 PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 1942453784     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.9.4038-4048.2004     Document Type: Article
Times cited : (76)

References (55)
  • 2
    • 0032460226 scopus 로고    scopus 로고
    • Prolactin (PRL) and its receptor: Actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice
    • Bole-Feysot, C., V. Goffin, M. Edery, N. Binart, and P. A. Kelly. 1998. Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice. Endocr. Rev. 19:225-268.
    • (1998) Endocr. Rev. , vol.19 , pp. 225-268
    • Bole-Feysot, C.1    Goffin, V.2    Edery, M.3    Binart, N.4    Kelly, P.A.5
  • 5
    • 0031809982 scopus 로고    scopus 로고
    • Prolactin receptor signal transduction in cells of the immune system
    • Clevenger, C. V., D. O. Freier, and J. B. Kline. 1998. Prolactin receptor signal transduction in cells of the immune system. J. Endocrinol. 157:187-197.
    • (1998) J. Endocrinol. , vol.157 , pp. 187-197
    • Clevenger, C.V.1    Freier, D.O.2    Kline, J.B.3
  • 7
    • 0034757830 scopus 로고    scopus 로고
    • Prolactin receptor signal transduction
    • Clevenger, C. V., and J. B. Kline. 2001. Prolactin receptor signal transduction. Lupus 10:706-718.
    • (2001) Lupus , vol.10 , pp. 706-718
    • Clevenger, C.V.1    Kline, J.B.2
  • 8
    • 0030621563 scopus 로고    scopus 로고
    • Prolactin as an autocrine/paracrine factor in breast tissue
    • Clevenger, C. V., and T. L. Plank. 1997. Prolactin as an autocrine/paracrine factor in breast tissue. J. Mammary Gland Biol. Neoplasia 2:59-68.
    • (1997) J. Mammary Gland Biol. Neoplasia , vol.2 , pp. 59-68
    • Clevenger, C.V.1    Plank, T.L.2
  • 10
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies, R. J. 1999. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15:435-467.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 11
    • 0018600137 scopus 로고
    • Rapid down-regulation of prolactin receptors in mammary gland and liver
    • Djiane, J., H. Clauser, and P. A. Kelly. 1979. Rapid down-regulation of prolactin receptors in mammary gland and liver. Biochem. Biophys. Res. Commun. 90:1371-1378.
    • (1979) Biochem. Biophys. Res. Commun. , vol.90 , pp. 1371-1378
    • Djiane, J.1    Clauser, H.2    Kelly, P.A.3
  • 12
    • 0020057517 scopus 로고
    • Prolactin receptor turnover in explants of pseudopregnant rabbit mammary gland
    • Djiane, J., C. Delouis, and P. A. Kelly. 1982. Prolactin receptor turnover in explants of pseudopregnant rabbit mammary gland. Mol. Cell. Endocrinol. 25:163-170.
    • (1982) Mol. Cell. Endocrinol. , vol.25 , pp. 163-170
    • Djiane, J.1    Delouis, C.2    Kelly, P.A.3
  • 13
    • 0019772911 scopus 로고
    • Down-regulation of prolactin receptors in rabbit mammary gland: Differential subcellular localization
    • Djiane, J., L. M. Houdebine, and P. A. Kelly. 1981. Down-regulation of prolactin receptors in rabbit mammary gland: differential subcellular localization. Proc. Soc. Exp. Biol. Med. 168:378-381.
    • (1981) Proc. Soc. Exp. Biol. Med. , vol.168 , pp. 378-381
    • Djiane, J.1    Houdebine, L.M.2    Kelly, P.A.3
  • 14
    • 0018850008 scopus 로고
    • Effects of lysosomotropic agents, cytochalasin B and colchicine on the "down-regulation" of prolactin receptors in mammary gland explants
    • Djiane, J., P. A. Kelly, and L. M. Houdebine. 1980. Effects of lysosomotropic agents, cytochalasin B and colchicine on the " down-regulation" of prolactin receptors in mammary gland explants. Mol. Cell. Endocrinol. 18:87-98.
    • (1980) Mol. Cell. Endocrinol. , vol.18 , pp. 87-98
    • Djiane, J.1    Kelly, P.A.2    Houdebine, L.M.3
  • 15
    • 0033771336 scopus 로고    scopus 로고
    • Prolactin: Structure, function, and regulation of secretion
    • Freeman, M. E., B. Kanyicska, A. Lerant, and G. Nagy. 2000. Prolactin: structure, function, and regulation of secretion. Physiol. Rev. 80:1523-1631.
    • (2000) Physiol. Rev. , vol.80 , pp. 1523-1631
    • Freeman, M.E.1    Kanyicska, B.2    Lerant, A.3    Nagy, G.4
  • 16
    • 0033602475 scopus 로고    scopus 로고
    • HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IκB and beta-catenin
    • Fuchs, S. Y., A. Chen, Y. Xiong, Z. Q. Pan, and Z. Ronai. 1999. HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IκB and beta-catenin. Oncogene 18:2039-2046.
    • (1999) Oncogene , vol.18 , pp. 2039-2046
    • Fuchs, S.Y.1    Chen, A.2    Xiong, Y.3    Pan, Z.Q.4    Ronai, Z.5
  • 17
    • 0028221574 scopus 로고
    • Endocytosis and degradation of prolactin and its receptor in Chinese hamster ovary cells stably transfected with prolactin receptor cDNA
    • Genty, N., J. Paly, M. Edery, P. A. Kelly, J. Djiane, and R. Salesse. 1994. Endocytosis and degradation of prolactin and its receptor in Chinese hamster ovary cells stably transfected with prolactin receptor cDNA. Mol. Cell. Endocrinol. 99:221-228.
    • (1994) Mol. Cell. Endocrinol. , vol.99 , pp. 221-228
    • Genty, N.1    Paly, J.2    Edery, M.3    Kelly, P.A.4    Djiane, J.5    Salesse, R.6
  • 19
    • 1242298802 scopus 로고    scopus 로고
    • Expression by transgenesis of a constitutively active mutant form of the prolactin receptor induces premature abnormal development of the mouse mammary gland and lactation failure
    • Gourdou, I., J. Paly, C. Hue-Beauvais, L. Pessemesse, J. Clark, and J. Djiane. 2004. Expression by transgenesis of a constitutively active mutant form of the prolactin receptor induces premature abnormal development of the mouse mammary gland and lactation failure. Biol. Reprod. 70:718-728.
    • (2004) Biol. Reprod. , vol.70 , pp. 718-728
    • Gourdou, I.1    Paly, J.2    Hue-Beauvais, C.3    Pessemesse, L.4    Clark, J.5    Djiane, J.6
  • 20
    • 0032568841 scopus 로고    scopus 로고
    • Dileucine-mediated internalization of ligand by a truncated growth hormone receptor is independent of the ubiquitin conjugation system
    • Govers, R., P. van Kerkhof, A. L. Schwartz, and G. J. Strous. 1998. Dileucine-mediated internalization of ligand by a truncated growth hormone receptor is independent of the ubiquitin conjugation system. J. Biol. Chem. 273:16426-16433.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16426-16433
    • Govers, R.1    Van Kerkhof, P.2    Schwartz, A.L.3    Strous, G.J.4
  • 24
    • 0026751717 scopus 로고
    • The p70 tumor necrosis factor receptor mediates cytotoxicity
    • Heller, R. A., K. Song, N. Fan, and D. J. Chang. 1992. The p70 tumor necrosis factor receptor mediates cytotoxicity. Cell 70:47-56.
    • (1992) Cell , vol.70 , pp. 47-56
    • Heller, R.A.1    Song, K.2    Fan, N.3    Chang, D.J.4
  • 25
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke, L. 1999. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol. 9:107-112.
    • (1999) Trends Cell Biol. , vol.9 , pp. 107-112
    • Hicke, L.1
  • 26
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. 2001. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2:195-201.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 27
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke, L., and R. Dunn. 2003. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19:141-172.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 30
    • 0033544961 scopus 로고    scopus 로고
    • Functional characterization of the intermediate isoform of the human prolactin receptor
    • Kline, J. B., H. Roehrs, and C. V. Clevenger. 1999. Functional characterization of the intermediate isoform of the human prolactin receptor. J. Biol. Chem. 274:35461-35468.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35461-35468
    • Kline, J.B.1    Roehrs, H.2    Clevenger, C.V.3
  • 31
    • 0036794307 scopus 로고    scopus 로고
    • Characterization of a novel and functional human prolactin receptor isoform (deltaS1PRLr) containing only one extracellular fibronectin-like domain
    • Kline, J. B., M. A. Rycyzyn, and C. V. Clevenger. 2002. Characterization of a novel and functional human prolactin receptor isoform (deltaS1PRLr) containing only one extracellular fibronectin-like domain. Mol. Endocrinol. 16:2310-2322.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2310-2322
    • Kline, J.B.1    Rycyzyn, M.A.2    Clevenger, C.V.3
  • 32
    • 0142105396 scopus 로고    scopus 로고
    • SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor
    • Kumar, K. G., W. Tang, A. K. Ravindranath, W. A. Clark, E. Croze, and S. Y. Fuchs. 2003. SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor. EMBO J. 22:5480-5490.
    • (2003) EMBO J. , vol.22 , pp. 5480-5490
    • Kumar, K.G.1    Tang, W.2    Ravindranath, A.K.3    Clark, W.A.4    Croze, E.5    Fuchs, S.Y.6
  • 34
    • 0033611567 scopus 로고    scopus 로고
    • The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin
    • Latres, E., D. S. Chiaur, and M. Pagano. 1999. The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin. Oncogene 18:849-854.
    • (1999) Oncogene , vol.18 , pp. 849-854
    • Latres, E.1    Chiaur, D.S.2    Pagano, M.3
  • 35
    • 0033537939 scopus 로고    scopus 로고
    • Constitutive activation of the prolactin receptor results in the induction of growth factor-independent proliferation and constitutive activation of signaling molecules
    • Lee, R. C., J. A. Walters, M. E. Reyland, and S. M. Anderson. 1999. Constitutive activation of the prolactin receptor results in the induction of growth factor-independent proliferation and constitutive activation of signaling molecules. J. Biol. Chem. 274:10024-10034.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10024-10034
    • Lee, R.C.1    Walters, J.A.2    Reyland, M.E.3    Anderson, S.M.4
  • 37
    • 0036843906 scopus 로고    scopus 로고
    • Multiple internalization motifs differentially used by prolactin receptor isoforms mediate similar endocytic pathways
    • Lu, J. C., P. Scott, G. J. Strous, and L. A. Schuler. 2002. Multiple internalization motifs differentially used by prolactin receptor isoforms mediate similar endocytic pathways. Mol. Endocrinol. 16:2515-2527.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2515-2527
    • Lu, J.C.1    Scott, P.2    Strous, G.J.3    Schuler, L.A.4
  • 38
    • 0142149094 scopus 로고    scopus 로고
    • Regulation of the discs large tumor suppressor by a phosphorylation-dependent interaction with the β-TrCP ubiquitin ligase receptor
    • Mantovani, F., and L. Banks. 2003. Regulation of the discs large tumor suppressor by a phosphorylation-dependent interaction with the β-TrCP ubiquitin ligase receptor. J. Biol. Chem. 278:42477-42486.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42477-42486
    • Mantovani, F.1    Banks, L.2
  • 39
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin, F., S. P. Bour, H. Durand, L. Selig, S. Benichou, V. Richard, D. Thomas, K. Strebel, and R. Benarous. 1998. A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell 1:565-574.
    • (1998) Mol. Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 41
    • 0017248186 scopus 로고
    • Growth hormone and prolactin in the fetus
    • Root, A. W. 1976. Growth hormone and prolactin in the fetus. Prog. Clin. Biol. Res. 10:107-126.
    • (1976) Prog. Clin. Biol. Res. , vol.10 , pp. 107-126
    • Root, A.W.1
  • 42
    • 0031044017 scopus 로고    scopus 로고
    • A short isoform of the human growth hormone receptor functions as a dominant negative inhibitor of the full-length receptor and generates large amounts of binding protein
    • Ross, R. J., N. Esposito, X. Y. Shen, S. Von Laue, S. L. Chew, P. R. Dobson, M. C. Postel-Vinay, and J. Finidori. 1997. A short isoform of the human growth hormone receptor functions as a dominant negative inhibitor of the full-length receptor and generates large amounts of binding protein. Mol. Endocrinol. 11:265-273.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 265-273
    • Ross, R.J.1    Esposito, N.2    Shen, X.Y.3    Von Laue, S.4    Chew, S.L.5    Dobson, P.R.6    Postel-Vinay, M.C.7    Finidori, J.8
  • 44
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP
    • Spencer, E., J. Jiang, and Z. J. Chen. 1999. Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP. Genes Dev. 13:284-294.
    • (1999) Genes Dev. , vol.13 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 45
    • 85047697637 scopus 로고    scopus 로고
    • Inhibition of HOS expression and activities by Wnt pathway
    • Spiegelman, V. S., W. Tang, M. Katoh, T. J. Slaga, and S. Y. Fuchs. 2002. Inhibition of HOS expression and activities by Wnt pathway. Oncogene 21:856-860.
    • (2002) Oncogene , vol.21 , pp. 856-860
    • Spiegelman, V.S.1    Tang, W.2    Katoh, M.3    Slaga, T.J.4    Fuchs, S.Y.5
  • 46
    • 0037010119 scopus 로고    scopus 로고
    • Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function
    • Strous, G. J., and J. Gent. 2002. Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function. FEBS Lett. 529:102-109.
    • (2002) FEBS Lett. , vol.529 , pp. 102-109
    • Strous, G.J.1    Gent, J.2
  • 47
    • 0037195510 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability
    • Strous, G. J., and P. van Kerkhof. 2002. The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability. Mol. Cell. Endocrinol. 197:143-151.
    • (2002) Mol. Cell. Endocrinol. , vol.197 , pp. 143-151
    • Strous, G.J.1    Van Kerkhof, P.2
  • 49
    • 0033120593 scopus 로고    scopus 로고
    • Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IκBα
    • Tan, P., S. Y. Fuchs, A. Chen, K. Wu, C. Gomez, Z. Ronai, and Z. Q. Pan. 1999. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IκBα. Mol. Cell 3:527-533.
    • (1999) Mol. Cell , vol.3 , pp. 527-533
    • Tan, P.1    Fuchs, S.Y.2    Chen, A.3    Wu, K.4    Gomez, C.5    Ronai, Z.6    Pan, Z.Q.7
  • 50
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier, M., L. M. Staszewski, and D. Bohmann. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78:787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 51
    • 0030989801 scopus 로고    scopus 로고
    • Identification of cytoplasmic motifs required for short prolactin receptor internalization
    • Vincent, V., V. Goffin, M. Rozakis-Adcock, J. P. Mornon, and P. A. Kelly. 1997. Identification of cytoplasmic motifs required for short prolactin receptor internalization. J. Biol. Chem. 272:7062-7068.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7062-7068
    • Vincent, V.1    Goffin, V.2    Rozakis-Adcock, M.3    Mornon, J.P.4    Kelly, P.A.5
  • 52
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman, A. M. 2001. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2:169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 54
    • 0033068154 scopus 로고    scopus 로고
    • β-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • β-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro. Genes Dev. 13:270-283.
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6


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