메뉴 건너뛰기




Volumn 21, Issue 4, 2011, Pages 452-457

Cytoplasmic polyadenylation and translational control

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; MESSENGER RNA;

EID: 79960930856     PISSN: 0959437X     EISSN: 18790380     Source Type: Journal    
DOI: 10.1016/j.gde.2011.04.006     Document Type: Review
Times cited : (95)

References (45)
  • 1
    • 41549097210 scopus 로고    scopus 로고
    • Translational control by cytoplasmic polyadenylation in Xenopus oocytes
    • Radford H.E., Meijer H.A., de Moor C.H. Translational control by cytoplasmic polyadenylation in Xenopus oocytes. Biochim Biophys Acta 2008, 1779:217-229.
    • (2008) Biochim Biophys Acta , vol.1779 , pp. 217-229
    • Radford, H.E.1    Meijer, H.A.2    de Moor, C.H.3
  • 2
    • 49349093646 scopus 로고    scopus 로고
    • Sequential waves of polyadenylation and deadenylation define a translation circuit that drives meiotic progression
    • Belloc E., Pique M., Mendez R. Sequential waves of polyadenylation and deadenylation define a translation circuit that drives meiotic progression. Biochem Soc Trans 2008, 36:665-670.
    • (2008) Biochem Soc Trans , vol.36 , pp. 665-670
    • Belloc, E.1    Pique, M.2    Mendez, R.3
  • 3
    • 34249908103 scopus 로고    scopus 로고
    • CPEB: a life in translation
    • Richter J.D. CPEB: a life in translation. Trends Biochem Sci 2007, 32:279-285.
    • (2007) Trends Biochem Sci , vol.32 , pp. 279-285
    • Richter, J.D.1
  • 4
    • 40449092963 scopus 로고    scopus 로고
    • Trading translation with RNA-binding proteins
    • Abaza I., Gebauer F. Trading translation with RNA-binding proteins. RNA 2008, 14:404-409.
    • (2008) RNA , vol.14 , pp. 404-409
    • Abaza, I.1    Gebauer, F.2
  • 5
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson R.J., Hellen C.U., Pestova T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 2010, 11:113-127.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 6
    • 8844274816 scopus 로고    scopus 로고
    • Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation
    • Barnard D.C., Ryan K., Manley J.L., Richter J.D. Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation. Cell 2004, 119:641-651.
    • (2004) Cell , vol.119 , pp. 641-651
    • Barnard, D.C.1    Ryan, K.2    Manley, J.L.3    Richter, J.D.4
  • 7
    • 33749662940 scopus 로고    scopus 로고
    • Opposing polymerase-deadenylase activities regulate cytoplasmic polyadenylation
    • Kim J.H., Richter J.D. Opposing polymerase-deadenylase activities regulate cytoplasmic polyadenylation. Mol Cell 2006, 24:173-183.
    • (2006) Mol Cell , vol.24 , pp. 173-183
    • Kim, J.H.1    Richter, J.D.2
  • 8
    • 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., Ryan K., Manley J.L., Richter J.D. Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex. Mol Cell 2000, 6:1253-1259.
    • (2000) Mol Cell , vol.6 , pp. 1253-1259
    • Mendez, R.1    Murthy, K.G.2    Ryan, K.3    Manley, J.L.4    Richter, J.D.5
  • 9
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with elF-4E
    • Stebbins-Boaz B., Cao Q., de Moor C.H., Mendez R., Richter J.D. Maskin is a CPEB-associated factor that transiently interacts with elF-4E. Mol Cell 1999, 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
  • 11
    • 38049134877 scopus 로고    scopus 로고
    • CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes
    • Minshall N., Reiter M.H., Weil D., Standart N. CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes. J Biol Chem 2007, 282:37389-37401.
    • (2007) J Biol Chem , vol.282 , pp. 37389-37401
    • Minshall, N.1    Reiter, M.H.2    Weil, D.3    Standart, N.4
  • 12
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • Cho P.F., Poulin F., Cho-Park Y.A., Cho-Park I.B., Chicoine J.D., Lasko P., Sonenberg N. A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP. Cell 2005, 121:411-423.
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Chicoine, J.D.5    Lasko, P.6    Sonenberg, N.7
  • 14
    • 78951490357 scopus 로고    scopus 로고
    • Biochemical characterization of Pumilio1 and Pumilio2 in Xenopus oocytes
    • Ota R., Kotani T., Yamashita M. Biochemical characterization of Pumilio1 and Pumilio2 in Xenopus oocytes. J Biol Chem 2011, 286:2853-2863.
    • (2011) J Biol Chem , vol.286 , pp. 2853-2863
    • Ota, R.1    Kotani, T.2    Yamashita, M.3
  • 15
    • 79960922805 scopus 로고    scopus 로고
    • Roles of Puf proteins in mRNA degradation and translation
    • doi:10.1002/wrna.69
    • Melanie A., Miller W.M.O. Roles of Puf proteins in mRNA degradation and translation. WIREs RNA 2010, doi:10.1002/wrna.69.
    • (2010) WIREs RNA
    • Melanie, A.1    Miller, W.M.O.2
  • 16
    • 0042261934 scopus 로고    scopus 로고
    • Involvement of Xenopus Pumilio in the translational regulation that is specific to cyclin B1 mRNA during oocyte maturation
    • Nakahata S., Kotani T., Mita K., Kawasaki T., Katsu Y., Nagahama Y., Yamashita M. Involvement of Xenopus Pumilio in the translational regulation that is specific to cyclin B1 mRNA during oocyte maturation. Mech Dev 2003, 120:865-880.
    • (2003) Mech Dev , vol.120 , pp. 865-880
    • Nakahata, S.1    Kotani, T.2    Mita, K.3    Kawasaki, T.4    Katsu, Y.5    Nagahama, Y.6    Yamashita, M.7
  • 17
    • 38849190013 scopus 로고    scopus 로고
    • A combinatorial code for CPE-mediated translational control
    • Pique M., Lopez J.M., Foissac S., Guigo R., Mendez R. A combinatorial code for CPE-mediated translational control. Cell 2008, 132:434-448.
    • (2008) Cell , vol.132 , pp. 434-448
    • Pique, M.1    Lopez, J.M.2    Foissac, S.3    Guigo, R.4    Mendez, R.5
  • 18
    • 33745545011 scopus 로고    scopus 로고
    • Musashi regulates the temporal order of mRNA translation during Xenopus oocyte maturation
    • Charlesworth A., Wilczynska A., Thampi P., Cox L.L., Macnicol A.M. Musashi regulates the temporal order of mRNA translation during Xenopus oocyte maturation. EMBO J 2006, 25:2792-2801.
    • (2006) EMBO J , vol.25 , pp. 2792-2801
    • Charlesworth, A.1    Wilczynska, A.2    Thampi, P.3    Cox, L.L.4    Macnicol, A.M.5
  • 19
    • 75049083859 scopus 로고    scopus 로고
    • Enforcing temporal control of maternal mRNA translation during oocyte cell-cycle progression
    • Arumugam K., Wang Y., Hardy L.L., Macnicol M.C., Macnicol A.M. Enforcing temporal control of maternal mRNA translation during oocyte cell-cycle progression. EMBO J 2010, 29:387-397.
    • (2010) EMBO J , vol.29 , pp. 387-397
    • Arumugam, K.1    Wang, Y.2    Hardy, L.L.3    Macnicol, M.C.4    Macnicol, A.M.5
  • 20
    • 2342437314 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation element (CPE)- and CPE-binding protein (CPEB)-independent mechanisms regulate early class maternal mRNA translational activation in Xenopus oocytes
    • Charlesworth A., Cox L.L., Macnicol A.M. Cytoplasmic polyadenylation element (CPE)- and CPE-binding protein (CPEB)-independent mechanisms regulate early class maternal mRNA translational activation in Xenopus oocytes. J Biol Chem 2004, 279:17650-17659.
    • (2004) J Biol Chem , vol.279 , pp. 17650-17659
    • Charlesworth, A.1    Cox, L.L.2    Macnicol, A.M.3
  • 21
    • 75149162081 scopus 로고    scopus 로고
    • A novel, noncanonical mechanism of cytoplasmic polyadenylation operates in Drosophila embryogenesis
    • Coll O., Villalba A., Bussotti G., Notredame C., Gebauer F. A novel, noncanonical mechanism of cytoplasmic polyadenylation operates in Drosophila embryogenesis. Genes Dev 2010, 24:129-134.
    • (2010) Genes Dev , vol.24 , pp. 129-134
    • Coll, O.1    Villalba, A.2    Bussotti, G.3    Notredame, C.4    Gebauer, F.5
  • 22
    • 0037136552 scopus 로고    scopus 로고
    • A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans
    • Wang L., Eckmann C.R., Kadyk L.C., Wickens M., Kimble J. A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans. Nature 2002, 419:312-316.
    • (2002) Nature , vol.419 , pp. 312-316
    • Wang, L.1    Eckmann, C.R.2    Kadyk, L.C.3    Wickens, M.4    Kimble, J.5
  • 24
  • 25
    • 64349118428 scopus 로고    scopus 로고
    • Two conserved regulatory cytoplasmic poly(A) polymerases, GLD-4 and GLD-2, regulate meiotic progression in C. elegans
    • Schmid M., Kuchler B., Eckmann C.R. Two conserved regulatory cytoplasmic poly(A) polymerases, GLD-4 and GLD-2, regulate meiotic progression in C. elegans. Genes Dev 2009, 23:824-836.
    • (2009) Genes Dev , vol.23 , pp. 824-836
    • Schmid, M.1    Kuchler, B.2    Eckmann, C.R.3
  • 26
    • 46749084324 scopus 로고    scopus 로고
    • PAP- and GLD-2-type poly(A) polymerases are required sequentially in cytoplasmic polyadenylation and oogenesis in Drosophila
    • Benoit P., Papin C., Kwak J.E., Wickens M., Simonelig M. PAP- and GLD-2-type poly(A) polymerases are required sequentially in cytoplasmic polyadenylation and oogenesis in Drosophila. Development 2008, 135:1969-1979.
    • (2008) Development , vol.135 , pp. 1969-1979
    • Benoit, P.1    Papin, C.2    Kwak, J.E.3    Wickens, M.4    Simonelig, M.5
  • 27
    • 77956115326 scopus 로고    scopus 로고
    • Developmental timing of mRNA translation-integration of distinct regulatory elements
    • Macnicol M.C., Macnicol A.M. Developmental timing of mRNA translation-integration of distinct regulatory elements. Mol Reprod Dev 2010, 77:662-669.
    • (2010) Mol Reprod Dev , vol.77 , pp. 662-669
    • Macnicol, M.C.1    Macnicol, A.M.2
  • 28
    • 77954955355 scopus 로고    scopus 로고
    • Meiosis requires a translational positive loop where CPEB1 ensues its replacement by CPEB4
    • Igea A., Mendez R. Meiosis requires a translational positive loop where CPEB1 ensues its replacement by CPEB4. EMBO J 2010, 29:2182-2193.
    • (2010) EMBO J , vol.29 , pp. 2182-2193
    • Igea, A.1    Mendez, R.2
  • 29
    • 42549107372 scopus 로고    scopus 로고
    • A deadenylation negative feedback mechanism governs meiotic metaphase arrest
    • Belloc E., Mendez R. A deadenylation negative feedback mechanism governs meiotic metaphase arrest. Nature 2008, 452:1017-1021.
    • (2008) Nature , vol.452 , pp. 1017-1021
    • Belloc, E.1    Mendez, R.2
  • 30
    • 0346186101 scopus 로고    scopus 로고
    • A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia
    • Si K., Giustetto M., Etkin A., Hsu R., Janisiewicz A.M., Miniaci M.C., Kim J.H., Zhu H., Kandel E.R. A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia. Cell 2003, 115:893-904.
    • (2003) Cell , vol.115 , pp. 893-904
    • Si, K.1    Giustetto, M.2    Etkin, A.3    Hsu, R.4    Janisiewicz, A.M.5    Miniaci, M.C.6    Kim, J.H.7    Zhu, H.8    Kandel, E.R.9
  • 31
    • 52249104915 scopus 로고    scopus 로고
    • Sustained CPEB-dependent local protein synthesis is required to stabilize synaptic growth for persistence of long-term facilitation in Aplysia
    • Miniaci M.C., Kim J.H., Puthanveettil S.V., Si K., Zhu H., Kandel E.R., Bailey C.H. Sustained CPEB-dependent local protein synthesis is required to stabilize synaptic growth for persistence of long-term facilitation in Aplysia. Neuron 2008, 59:1024-1036.
    • (2008) Neuron , vol.59 , pp. 1024-1036
    • Miniaci, M.C.1    Kim, J.H.2    Puthanveettil, S.V.3    Si, K.4    Zhu, H.5    Kandel, E.R.6    Bailey, C.H.7
  • 32
    • 36448958766 scopus 로고    scopus 로고
    • Function of the Drosophila CPEB protein Orb2 in long-term courtship memory
    • Keleman K., Kruttner S., Alenius M., Dickson B.J. Function of the Drosophila CPEB protein Orb2 in long-term courtship memory. Nat Neurosci 2007, 10:1587-1593.
    • (2007) Nat Neurosci , vol.10 , pp. 1587-1593
    • Keleman, K.1    Kruttner, S.2    Alenius, M.3    Dickson, B.J.4
  • 34
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses
    • Wu L., Wells D., Tay J., Mendis D., Abbott M.A., Barnitt A., Quinlan E., Heynen A., Fallon J.R., Richter J.D. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses. Neuron 1998, 21:1129-1139.
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1    Wells, D.2    Tay, J.3    Mendis, D.4    Abbott, M.A.5    Barnitt, A.6    Quinlan, E.7    Heynen, A.8    Fallon, J.R.9    Richter, J.D.10
  • 35
    • 0036565678 scopus 로고    scopus 로고
    • N-methyl-d-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and alpha CaMKII mRNA polyadenylation at synapses
    • Huang Y.S., Jung M.Y., Sarkissian M., Richter J.D. N-methyl-d-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and alpha CaMKII mRNA polyadenylation at synapses. EMBO J 2002, 21:2139-2148.
    • (2002) EMBO J , vol.21 , pp. 2139-2148
    • Huang, Y.S.1    Jung, M.Y.2    Sarkissian, M.3    Richter, J.D.4
  • 37
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • Si K., Lindquist S., Kandel E.R. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003, 115:879-891.
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 38
    • 79952578947 scopus 로고    scopus 로고
    • Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB)
    • Heinrich S.U., Lindquist S. Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB). Proc Natl Acad Sci U S A 2011, 108:2999-3004.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2999-3004
    • Heinrich, S.U.1    Lindquist, S.2
  • 39
    • 75749134925 scopus 로고    scopus 로고
    • Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation
    • Si K., Choi Y.B., White-Grindley E., Majumdar A., Kandel E.R. Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation. Cell 2010, 140:421-435.
    • (2010) Cell , vol.140 , pp. 421-435
    • Si, K.1    Choi, Y.B.2    White-Grindley, E.3    Majumdar, A.4    Kandel, E.R.5
  • 41
    • 33845351450 scopus 로고    scopus 로고
    • CDK1 and calcineurin regulate Maskin association with eIF4E and translational control of cell cycle progression
    • Cao Q., Kim J.H., Richter J.D. CDK1 and calcineurin regulate Maskin association with eIF4E and translational control of cell cycle progression. Nat Struct Mol Biol 2006, 13:1128-1134.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 1128-1134
    • Cao, Q.1    Kim, J.H.2    Richter, J.D.3
  • 42
    • 77951978351 scopus 로고    scopus 로고
    • Mitotic cell-cycle progression is regulated by CPEB1 and CPEB4-dependent translational control
    • Novoa I., Gallego J., Ferreira P.G., Mendez R. Mitotic cell-cycle progression is regulated by CPEB1 and CPEB4-dependent translational control. Nat Cell Biol 2010, 12:447-456.
    • (2010) Nat Cell Biol , vol.12 , pp. 447-456
    • Novoa, I.1    Gallego, J.2    Ferreira, P.G.3    Mendez, R.4
  • 43
    • 46449139041 scopus 로고    scopus 로고
    • Spindle-localized CPE-mediated translation controls meiotic chromosome segregation
    • Eliscovich C., Peset I., Vernos I., Mendez R. Spindle-localized CPE-mediated translation controls meiotic chromosome segregation. Nat Cell Biol 2008, 10:858-865.
    • (2008) Nat Cell Biol , vol.10 , pp. 858-865
    • Eliscovich, C.1    Peset, I.2    Vernos, I.3    Mendez, R.4
  • 44
    • 58049213723 scopus 로고    scopus 로고
    • CPEB regulation of human cellular senescence, energy metabolism, and p53 mRNA translation
    • Burns D.M., Richter J.D. CPEB regulation of human cellular senescence, energy metabolism, and p53 mRNA translation. Genes Dev 2008, 22:3449-3460.
    • (2008) Genes Dev , vol.22 , pp. 3449-3460
    • Burns, D.M.1    Richter, J.D.2
  • 45
    • 75149173478 scopus 로고    scopus 로고
    • The nuclear experience of CPEB: implications for RNA processing and translational control
    • Lin C.L., Evans V., Shen S., Xing Y., Richter J.D. The nuclear experience of CPEB: implications for RNA processing and translational control. RNA 2010, 16:338-348.
    • (2010) RNA , vol.16 , pp. 338-348
    • Lin, C.L.1    Evans, V.2    Shen, S.3    Xing, Y.4    Richter, J.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.