메뉴 건너뛰기




Volumn 18, Issue 1, 2004, Pages 48-61

Progesterone and insulin stimulation of CPEB-dependent polyadenylation is regulated by Aurora A and glycogen synthase kinase-3

Author keywords

Aurora A; CPEB; Cytoplasmic polyadenylation; GSK 3; Insulin; Xenopus oocytes

Indexed keywords

AURORA A KINASE; CYCLIN B; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; GLYCOGEN SYNTHASE KINASE 3; INSULIN; MESSENGER RNA; MOS PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROGESTERONE; PROTEIN; PROTEIN KINASE C ZETA; SERINE; UNCLASSIFIED DRUG;

EID: 0346497760     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1136004     Document Type: Article
Times cited : (110)

References (49)
  • 1
    • 0032563091 scopus 로고    scopus 로고
    • Protein kinase B/Akt Induces resumption of meiosis in Xenopus oocytes
    • Andersen, C., Roth, R.A., and Conti, M. 1998. Protein kinase B/Akt Induces resumption of meiosis in Xenopus oocytes. J. Biol. Chem. 273: 18705-18708.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18705-18708
    • Andersen, C.1    Roth, R.A.2    Conti, M.3
  • 2
    • 0346460958 scopus 로고    scopus 로고
    • Protein kinase B/Akt is essential for the insulin- but not progesterone-stimulated resumption of meiosis in Xenopus oocytes
    • Andersen, C., Sakaue, H., Nedachi, T., Kovacina, K.S., Clayberger, C., Conti, M., and Roth, R.A. 2003. Protein kinase B/Akt is essential for the insulin- but not progesterone-stimulated resumption of meiosis in Xenopus oocytes. Biochem. J. 369: 227-238.
    • (2003) Biochem. J. , vol.369 , pp. 227-238
    • Andersen, C.1    Sakaue, H.2    Nedachi, T.3    Kovacina, K.S.4    Clayberger, C.5    Conti, M.6    Roth, R.A.7
  • 3
    • 0343917044 scopus 로고    scopus 로고
    • The kinase Eg2 is a component of the Xenopus oocyte progesterone-activated signaling pathway
    • Andresson, T. and Ruderman, J.V. 1998. The kinase Eg2 is a component of the Xenopus oocyte progesterone-activated signaling pathway. EMBO J. 17: 5627-5637.
    • (1998) EMBO J. , vol.17 , pp. 5627-5637
    • Andresson, T.1    Ruderman, J.V.2
  • 5
    • 0034677804 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3B facilitates staurosporine and heat shock induced apoptosis
    • Bijur, G.N., De Sarno, P., and Jope, R.S. 2000. Glycogen synthase kinase-3B facilitates staurosporine and heat shock induced apoptosis. J. Biol. Chem. 275: 7583-7590.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7583-7590
    • Bijur, G.N.1    De Sarno, P.2    Jope, R.S.3
  • 6
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin layer cellulose plates
    • Boyle, W.J., van der Geer, P., and Hunter, T. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin layer cellulose plates. Methods Enzymol. 201: 110-149.
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 7
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L.C. 2002. The phosphoinositide 3-kinase pathway. Science 296: 1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 8
    • 0037099704 scopus 로고    scopus 로고
    • Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation
    • Cao, Q. and Richter, J.D. 2002. Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation. EMBO J. 21: 3852-3862.
    • (2002) EMBO J. , vol.21 , pp. 3852-3862
    • Cao, Q.1    Richter, J.D.2
  • 9
    • 0027177288 scopus 로고
    • Insulin receptor substrate 1 mediates insulin and insulin-like growth factor 1-stimulated maturation of Xenopus oocytes
    • Chuang, L.M., Myers, M.G., Seidner, G.A., Birnbaum, M.J., White, M.F., and Kahn, R.C. 1993a. Insulin receptor substrate 1 mediates insulin and insulin-like growth factor 1-stimulated maturation of Xenopus oocytes. Proc. Natl. Acad. Sci. 90: 5172-5175.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 5172-5175
    • Chuang, L.M.1    Myers, M.G.2    Seidner, G.A.3    Birnbaum, M.J.4    White, M.F.5    Kahn, R.C.6
  • 10
    • 0027379041 scopus 로고
    • Insulin-stimulated oocyte maturation requires insulin receptor substrate 1 and interaction with the SH2 domains of phosphatidylinositol 3-kinase
    • Chuang, L.M., Myers, M.G., Backer, J.M., Shoelson, S.E., White, M.F., Birnbaum, M.J., and Kahn, R.C. 1993b. Insulin-stimulated oocyte maturation requires insulin receptor substrate 1 and interaction with the SH2 domains of phosphatidylinositol 3-kinase. Mol. Cell. Biol. 13: 6653-6660.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6653-6660
    • Chuang, L.M.1    Myers, M.G.2    Backer, J.M.3    Shoelson, S.E.4    White, M.F.5    Birnbaum, M.J.6    Kahn, R.C.7
  • 11
    • 0030869091 scopus 로고    scopus 로고
    • The mos pathway regulates cytoplasmic polyadenylation in Xenopus oocytes
    • de Moor, C.H. and Richter, J.D. 1997. The mos pathway regulates cytoplasmic polyadenylation in Xenopus oocytes. Mol. Cell. Biol. 17: 6419-6426.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6419-6426
    • De Moor, C.H.1    Richter, J.D.2
  • 13
    • 0037446847 scopus 로고    scopus 로고
    • A novel mechanism for activation of the protein kinase Aurora A
    • Eyers, P.A., Erikson E., Chen, L.G., and Maller, J.L. 2003. A novel mechanism for activation of the protein kinase Aurora A. Curr. Biol. 13: 691-697.
    • (2003) Curr. Biol. , vol.13 , pp. 691-697
    • Eyers, P.A.1    Erikson, E.2    Chen, L.G.3    Maller, J.L.4
  • 14
    • 0033214147 scopus 로고    scopus 로고
    • Xenopus oocyte maturation: New lessons from a good egg
    • Ferrell, J.E. 1999. Xenopus oocyte maturation: New lessons from a good egg. BioEssays 21: 833-842.
    • (1999) BioEssays , vol.21 , pp. 833-842
    • Ferrell, J.E.1
  • 15
    • 0033002114 scopus 로고    scopus 로고
    • A novel role for glycogen synthase kinase-3 in Xenopus development: Maintenance of oocyte cell cycle arrest by a β-catenin-independent mechanism
    • Fisher, D.J., Morin, N., and Doree, M. 1999. A novel role for glycogen synthase kinase-3 in Xenopus development: Maintenance of oocyte cell cycle arrest by a β-catenin-independent mechanism. Development 126: 567-576
    • (1999) Development , vol.126 , pp. 567-576
    • Fisher, D.J.1    Morin, N.2    Doree, M.3
  • 16
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes center stage more than 20 years after its discovery
    • Frame, S. and Cohen, P. 2001. GSK3 takes center stage more than 20 years after its discovery. Biochem. J. 359: 1-16.
    • (2001) Biochem. J. , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 18
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras, AC., Raught, B., and Sonenberg, N. 2001. Regulation of translation initiation by FRAP/mTOR. Genes & Dev. 15: 807-826.
    • (2001) Genes & Dev. , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 20
    • 0028029983 scopus 로고
    • CPEB is a specific factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation
    • Hake, L.E. and Richter, J.D. 1994. CPEB is a specific factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation. Cell 79: 617-628.
    • (1994) Cell , vol.79 , pp. 617-628
    • Hake, L.E.1    Richter, J.D.2
  • 21
    • 0036565678 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and αCaMKII mRNA polyadenylation at synapses
    • Huang Y.S., Jung, M.Y., Sarkissian, M., and Richter, J. 2002. N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and αCaMKII mRNA polyadenylation at synapses. EMBO J. 21: 2139-2148.
    • (2002) EMBO J. , vol.21 , pp. 2139-2148
    • Huang, Y.S.1    Jung, M.Y.2    Sarkissian, M.3    Richter, J.4
  • 22
    • 0036007421 scopus 로고    scopus 로고
    • Regulation of cell size in growth, development and human disease: PI3K, PKB and S6K
    • Kozma, S.C. and Thomas, G. 2002. Regulation of cell size in growth, development and human disease: PI3K, PKB and S6K. BioEssays 24: 65-71.
    • (2002) BioEssays , vol.24 , pp. 65-71
    • Kozma, S.C.1    Thomas, G.2
  • 24
    • 0037414701 scopus 로고    scopus 로고
    • The cytoplasmic polyadenylation element binding protein and polyadenylation of messenger RNA in Aplysia neurons
    • Liu, J. and Schwartz, J.H. 2003. The cytoplasmic polyadenylation element binding protein and polyadenylation of messenger RNA in Aplysia neurons. Brain Res. 959: 68-76.
    • (2003) Brain Res. , vol.959 , pp. 68-76
    • Liu, J.1    Schwartz, J.H.2
  • 25
    • 0029067502 scopus 로고
    • Molecular cloning of an amphibian insulin receptor substrate 1-Like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation
    • Liu, X.J., Sorisky, A., Zhu, L., and Pawson, T. 1995. Molecular cloning of an amphibian insulin receptor substrate 1-Like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation. Mol. Cell. Biol. 15: 3563-3570.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3563-3570
    • Liu, X.J.1    Sorisky, A.2    Zhu, L.3    Pawson, T.4
  • 26
    • 0037373247 scopus 로고    scopus 로고
    • Biphasic activation of Aurora-A kinase during the meiosis I- meiosis II transition in Xenopus oocytes
    • Ma, C., Cummings, C., and Liu, X.J. 2003. Biphasic activation of Aurora-A kinase during the meiosis I- meiosis II transition in Xenopus oocytes. Mol. Cell. Biol. 23: 1703-1716.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1703-1716
    • Ma, C.1    Cummings, C.2    Liu, X.J.3
  • 27
    • 0035404265 scopus 로고    scopus 로고
    • Translational control by CPEB: A means to the end
    • Mendez, R. and Richter, J.D. 2001. Translational control by CPEB: A means to the end. Nat. Rev. Mol. Cell. Biol. 2: 521-529.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 521-529
    • Mendez, R.1    Richter, J.D.2
  • 28
    • 0034673706 scopus 로고    scopus 로고
    • Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA
    • Mendez, R., Hake, L.E., Andresson, T., Littlepage, L.E., Ruderman, J.V., and Richter, J.D. 2000a. Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA. Nature 404: 302-307.
    • (2000) Nature , vol.404 , pp. 302-307
    • Mendez, R.1    Hake, L.E.2    Andresson, T.3    Littlepage, L.E.4    Ruderman, J.V.5    Richter, J.D.6
  • 29
    • 0033634850 scopus 로고    scopus 로고
    • Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex
    • Mendez, R., Murthy, K.G.K., Ryan, K., Manley, J.L., and Richter, J.D. 2000b. Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex. Mol. Cell. Biol. 6: 1253-1259.
    • (2000) Mol. Cell. Biol. , vol.6 , pp. 1253-1259
    • Mendez, R.1    Murthy, K.G.K.2    Ryan, K.3    Manley, J.L.4    Richter, J.D.5
  • 31
    • 0037007233 scopus 로고    scopus 로고
    • Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction
    • Mendez, R., Barnard, D., and Richter, J.D. 2002. Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction. EMBO J. 21: 1833-1844.
    • (2002) EMBO J. , vol.21 , pp. 1833-1844
    • Mendez, R.1    Barnard, D.2    Richter, J.D.3
  • 33
    • 0024239777 scopus 로고
    • Changes in the polyadenylation of specific stable RNA during the early development of Xenopus laevis
    • Paris, J., Osborne, H.B., Couturier, A., Le Guellac, R., and Philippe, M. 1988. Changes in the polyadenylation of specific stable RNA during the early development of Xenopus laevis. Gene 72: 169-176.
    • (1988) Gene , vol.72 , pp. 169-176
    • Paris, J.1    Osborne, H.B.2    Couturier, A.3    Le Guellac, R.4    Philippe, M.5
  • 35
    • 0028935672 scopus 로고
    • Regulation of Spemann organizer formation by the intracellular kinase Xgsk-3
    • Pierce, S.B. and Kimelman, D. 1995. Regulation of Spemann organizer formation by the intracellular kinase Xgsk-3. Development 121: 755-765.
    • (1995) Development , vol.121 , pp. 755-765
    • Pierce, S.B.1    Kimelman, D.2
  • 36
    • 0001364237 scopus 로고    scopus 로고
    • The influence of polyadenylation-induced translation on metazoan development and neuronal synaptic function
    • (eds. M.B. Matthews et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Richter, J.D. 2000. The influence of polyadenylation-induced translation on metazoan development and neuronal synaptic function. In Translational control of gene expression (eds. M.B. Matthews et al.), pp. 785-805. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 785-805
    • Richter, J.D.1
  • 37
    • 0019860035 scopus 로고
    • Progesterone inhibits adenylate cyclase in Xenopus oocytes. Action on the guanine nucleotide regulatory protein
    • Sadler, S.E. and Maller, J.L. 1981. Progesterone inhibits adenylate cyclase in Xenopus oocytes. Action on the guanine nucleotide regulatory protein. J. Biol. Chem. 256: 6368-6373.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6368-6373
    • Sadler, S.E.1    Maller, J.L.2
  • 38
    • 0024494198 scopus 로고
    • 59]Ha-ras protein
    • 59]Ha-ras protein. J. Biol. Chem. 264: 856-861.
    • (1989) J. Biol. Chem. , vol.264 , pp. 856-861
  • 39
    • 0024280269 scopus 로고
    • Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes
    • Sagata, N., Oskarsson, M., Copeland, T., Brumbaugh, J., and vande Woude, G.F. 1988. Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature 335: 519-525.
    • (1988) Nature , vol.335 , pp. 519-525
    • Sagata, N.1    Oskarsson, M.2    Copeland, T.3    Brumbaugh, J.4    Vande Woude, G.F.5
  • 40
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmelzle, T. and Hall, M.N. 2000. TOR, a central controller of cell growth. Cell 103: 253-262.
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 41
    • 0037007012 scopus 로고    scopus 로고
    • Inhibition of Xenopus oocyte meiotic maturation by catalytically inactive protein kinase A
    • Schmitt, A. and Nebreda, A.R. 2002. Inhibition of Xenopus oocyte meiotic maturation by catalytically inactive protein kinase A. Proc. Natl. Acad. Sci. 99: 4361-4366.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 4361-4366
    • Schmitt, A.1    Nebreda, A.R.2
  • 43
    • 0029998640 scopus 로고    scopus 로고
    • CPEB controls the cytoplasmic polyadenylation of cyclin, CDK2 and c-mos mRNA and is necessary for oocyte maturation in Xenopus
    • Stebbins-Boaz, B., Hake, L.E., and Richter, J.D. 1996. CPEB controls the cytoplasmic polyadenylation of cyclin, CDK2 and c-mos mRNA and is necessary for oocyte maturation in Xenopus. EMBO J. 15: 2582-2592.
    • (1996) EMBO J. , vol.15 , pp. 2582-2592
    • Stebbins-Boaz, B.1    Hake, L.E.2    Richter, J.D.3
  • 44
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with eIF-4E
    • Stebbins-Boaz, B., Cao, Q., de Moor, C.H., Mendez, R., and Richter, J.D. 1999. Maskin is a CPEB-associated factor that transiently interacts with eIF-4E. Mol. Cell 4: 1017-1027.
    • (1999) Mol. Cell , vol.4 , pp. 1017-1027
    • Stebbins-Boaz, B.1    Cao, Q.2    De Moor, C.H.3    Mendez, R.4    Richter, J.D.5
  • 46
    • 0034609753 scopus 로고    scopus 로고
    • The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation
    • Walter, A.O., Seghezzi, W., Korver W., Sheung, J., and Lees, E. 2000. The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation. Oncogene 19: 4906-4916.
    • (2000) Oncogene , vol.19 , pp. 4906-4916
    • Walter, A.O.1    Seghezzi, W.2    Korver, W.3    Sheung, J.4    Lees, E.5
  • 47
    • 0035894857 scopus 로고    scopus 로고
    • A role for the cytoplasmic polyadenylation element in NMDA receptor-regulated mRNA translation in neurons
    • Wells, D.G., Dong, X., Quinlan, E.M., Huang, Y.S., Bear, M.F., Richter, J.D., and Fallon, J.R. 2001. A role for the cytoplasmic polyadenylation element in NMDA receptor-regulated mRNA translation in neurons. J. Neurosci. 21: 9541-9548.
    • (2001) J. Neurosci. , vol.21 , pp. 9541-9548
    • Wells, D.G.1    Dong, X.2    Quinlan, E.M.3    Huang, Y.S.4    Bear, M.F.5    Richter, J.D.6    Fallon, J.R.7
  • 48
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of α-CaMKII mRNA at synapses
    • Wu, L., Wells, D., Tay, J., Mendis, D., Abbott, M., Barnitt, A., Quinlan, E., Heynen, A., Fallon, J., and Richter, J.D. 1998. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of α-CaMKII mRNA at synapses. Neuron 21: 1129-1139.
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1    Wells, D.2    Tay, J.3    Mendis, D.4    Abbott, M.5    Barnitt, A.6    Quinlan, E.7    Heynen, A.8    Fallon, J.9    Richter, J.D.10
  • 49
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
    • Wymann, M.P., Bulgarelli-Leva, G., Zvelebil, M.J., Pirola, L., Vanhaesebroeck, B., Waterfield, M.D., and Panayotou, G. 1996. Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell. Biol. 16: 1722-1733.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1722-1733
    • Wymann, M.P.1    Bulgarelli-Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesebroeck, B.5    Waterfield, M.D.6    Panayotou, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.