메뉴 건너뛰기




Volumn 4, Issue 8, 2003, Pages 626-637

The power of the 3′ UTR: Translational control and development

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; MESSENGER RNA; MICRORNA; OXYGEN; UNCLASSIFIED DRUG; RNA;

EID: 0042968976     PISSN: 14710056     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrg1125     Document Type: Review
Times cited : (446)

References (124)
  • 1
    • 0002068909 scopus 로고    scopus 로고
    • (eds. Sonenberg, N., Hershey, J. & Mathews, M. B.) (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Wickens, M., Goodwin, E. B., Kimble, J., Strickland, S. & Hentze, M. W. in Translational Control of Gene Expression (eds. Sonenberg, N., Hershey, J. & Mathews, M. B.) 295-370 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2000).
    • (2000) Translational Control of Gene Expression , pp. 295-370
    • Wickens, M.1    Goodwin, E.B.2    Kimble, J.3    Strickland, S.4    Hentze, M.W.5
  • 2
    • 0035674402 scopus 로고    scopus 로고
    • Translational regulation and RNA localization in Drosophila oocytes and embryos
    • Johnstone, O. & Lasko, R Translational regulation and RNA localization in Drosophila oocytes and embryos. Annu. Rev. Genet. 35, 365-406 (2001).
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 365-406
    • Johnstone, O.1    Lasko, R.2
  • 3
  • 4
    • 0031452082 scopus 로고    scopus 로고
    • A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germline
    • Zhang, B. et al. A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germline. Nature 390, 477-484 (1997).
    • (1997) Nature , vol.390 , pp. 477-484
    • Zhang, B.1
  • 5
    • 0025748167 scopus 로고
    • RNA regulatory elements mediate control of Drosophila body pattern by the posterior morphogen nanos
    • Wharton, R. P. & Struhl, G. RNA regulatory elements mediate control of Drosophila body pattern by the posterior morphogen nanos. Cell 67, 955-967 (1991).
    • (1991) Cell , vol.67 , pp. 955-967
    • Wharton, R.P.1    Struhl, G.2
  • 6
    • 0028987223 scopus 로고
    • Binding of Pumilio to maternal hunchback mRNA is required for posterior patterning in Drosophila embryos
    • Murata, Y. & Wharton, R. P. Binding of Pumilio to maternal hunchback mRNA is required for posterior patterning in Drosophila embryos. Cell 80, 747-756 (1995).
    • (1995) Cell , vol.80 , pp. 747-756
    • Murata, Y.1    Wharton, R.P.2
  • 7
    • 0033569404 scopus 로고    scopus 로고
    • Recruitment of Nanos to hunchback mRNA by Pumilio
    • Sonoda, J. & Wharton, R. P. Recruitment of Nanos to hunchback mRNA by Pumilio. Genes Dev. 13, 2704-2712 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2704-2712
    • Sonoda, J.1    Wharton, R.P.2
  • 8
    • 0035868645 scopus 로고    scopus 로고
    • Drosophila brain tumor is a translational repressor
    • Sonoda, J. & Wharton, R. P. Drosophila Brain Tumor is a translational repressor. Genes Dev. 15, 762-773 (2001). This work shows that a complex of factors, including Nanos and Brain tumor, are recruited to the hunchback 3′ UTR by Pumilio, and that this complex is necessary for translational repression,
    • (2001) Genes Dev. , vol.15 , pp. 762-773
    • Sonoda, J.1    Wharton, R.P.2
  • 9
    • 0033046510 scopus 로고    scopus 로고
    • Role for mRNA localization in translational activation but not spatial restriction of nanos RNA
    • Bergsten, S. E. & Gavis, E. R. Role for mRNA localization in translational activation but not spatial restriction of nanos RNA. Development 126, 659-669 (1999).
    • (1999) Development , vol.126 , pp. 659-669
    • Bergsten, S.E.1    Gavis, E.R.2
  • 10
    • 0025826161 scopus 로고
    • Oskar organizes the germ plasm and directs localization of the posterior determinant nanos
    • Ephrussi, A., Dickinson, L. K. & Lehmann, R. Oskar organizes the germ plasm and directs localization of the posterior determinant nanos. Cell 66, 37-50 (1991).
    • (1991) Cell , vol.66 , pp. 37-50
    • Ephrussi, A.1    Dickinson, L.K.2    Lehmann, R.3
  • 11
    • 0026755984 scopus 로고
    • Localization of nanos RNA controls embryonic polarity
    • Gavis, E. R. & Lehmann, R. Localization of nanos RNA controls embryonic polarity. Cell 71, 301-313 (1992).
    • (1992) Cell , vol.71 , pp. 301-313
    • Gavis, E.R.1    Lehmann, R.2
  • 12
    • 0026778963 scopus 로고
    • Overexpression of Oskar directs ectopic activation of Nanos and presumptive pole cell formation in Drosophila embryos
    • Smith, J. L., Wilson, J. E. & Macdonald, P. M. Overexpression of Oskar directs ectopic activation of Nanos and presumptive pole cell formation in Drosophila embryos. Cell 70, 849-859 (1992).
    • (1992) Cell , vol.70 , pp. 849-859
    • Smith, J.L.1    Wilson, J.E.2    Macdonald, P.M.3
  • 13
    • 0033180476 scopus 로고    scopus 로고
    • Smaug, a novel RNA-binding protein that operates a translational switch in Drosophila
    • Dahanukar, A., Walker, J. A. & Wharton, R. P. Smaug, a novel RNA-binding protein that operates a translational switch in Drosophila. Mol. Cell 4, 209-218 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 209-218
    • Dahanukar, A.1    Walker, J.A.2    Wharton, R.P.3
  • 14
    • 0032786907 scopus 로고    scopus 로고
    • Smaug, a novel and conserved protein, contributes to repression of nanos MRNA translation in vitro
    • Smibert, C. A., Lie, Y. S., Shillinglaw, W., Henzel, W. J. & Macdonald, P. M. Smaug, a novel and conserved protein, contributes to repression of nanos MRNA translation in vitro. RNA 5, 1535-1547 (1999).
    • (1999) RNA , vol.5 , pp. 1535-1547
    • Smibert, C.A.1    Lie, Y.S.2    Shillinglaw, W.3    Henzel, W.J.4    Macdonald, P.M.5
  • 15
    • 0029958353 scopus 로고    scopus 로고
    • Smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo
    • Smibert, G. A., Wilson, J. E., Kerr, K. & Macdonald, P. M. Smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo. Genes Dev. 10, 2600-2609 (1996). Evidence that Smaug is important for establishing the Nanos protein gradient by repressing the translation of unlocalized nanos mRNA.
    • (1996) Genes Dev. , vol.10 , pp. 2600-2609
    • Smibert, G.A.1    Wilson, J.E.2    Kerr, K.3    Macdonald, P.M.4
  • 16
    • 0029028583 scopus 로고
    • Translational regulation of oskar mRNA by Bruno, an ovarian RNA-binding protein, is essential
    • Kim-Ha, J., Kerr, K. & Macdonald, P. M. Translational regulation of oskar mRNA by Bruno, an ovarian RNA-binding protein, is essential. Cell 81, 403-412 (1995). This study shows that Bruno is a trans-acting factor that regulates the translation of oskar mRNA.
    • (1995) Cell , vol.81 , pp. 403-412
    • Kim-Ha, J.1    Kerr, K.2    Macdonald, P.M.3
  • 17
    • 0029085434 scopus 로고
    • Localization of oskar RNA regulates oskar translation and requires Oskar protein
    • Rongo, C., Gavis, E. R. & Lehmann, R. Localization of oskar RNA regulates oskar translation and requires Oskar protein. Development 121, 2737-2746 (1995).
    • (1995) Development , vol.121 , pp. 2737-2746
    • Rongo, C.1    Gavis, E.R.2    Lehmann, R.3
  • 18
    • 0028863317 scopus 로고
    • Translational control of oskar generates short OSK, the isoform that induces pole plasma assembly
    • Markussen, F. H., Michon, A. M., Breitwieser, W. & Ephrussi, A. Translational control of oskar generates short OSK, the isoform that induces pole plasma assembly. Development 121, 3723-3732 (1995).
    • (1995) Development , vol.121 , pp. 3723-3732
    • Markussen, F.H.1    Michon, A.M.2    Breitwieser, W.3    Ephrussi, A.4
  • 19
    • 0030808440 scopus 로고    scopus 로고
    • Translational repressor Bruno plays multiple roles in development and is widely conserved
    • Webster, P. J., Liang, L., Berg, C. A., Lasko, P. & Macdonald, P. M. Translational repressor Bruno plays multiple roles in development and is widely conserved. Genes Dev. 11, 2510-2521 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 2510-2521
    • Webster, P.J.1    Liang, L.2    Berg, C.A.3    Lasko, P.4    Macdonald, P.M.5
  • 20
    • 0032938811 scopus 로고    scopus 로고
    • Apontic binds the translational repressor Bruno and is implicated in regulation of oskar mRNA translation
    • Lie, Y. S. & Macdonald, P. M. Apontic binds the translational repressor Bruno and is implicated in regulation of oskar mRNA translation. Development 126, 1129-1138 (1999).
    • (1999) Development , vol.126 , pp. 1129-1138
    • Lie, Y.S.1    Macdonald, P.M.2
  • 21
    • 2642633741 scopus 로고    scopus 로고
    • Localization-dependent translation requires a functional interaction between the 5′ and 3′ ends of oskar mRNA
    • Gunkel, N., Yano, T., Markussen, F. H., Olsen, L. C. & Ephrussi, A. Localization-dependent translation requires a functional interaction between the 5′ and 3′ ends of oskar mRNA. Genes Dev. 12, 1652-1664 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 1652-1664
    • Gunkel, N.1    Yano, T.2    Markussen, F.H.3    Olsen, L.C.4    Ephrussi, A.5
  • 22
    • 0033452314 scopus 로고    scopus 로고
    • Translational regulation of oskar mRNA occurs independent of the cap and poly(A) tail in Drosophila ovarian extracts
    • Lie, Y. S. & Macdonald, P. M. Translational regulation of oskar mRNA occurs independent of the cap and poly(A) tail in Drosophila ovarian extracts. Development 126, 4989-4996 (1999).
    • (1999) Development , vol.126 , pp. 4989-4996
    • Lie, Y.S.1    Macdonald, P.M.2
  • 23
    • 0031462473 scopus 로고    scopus 로고
    • Efficient translation and phosphorylation of Oskar require Oskar protein and the RNA helicase Vasa
    • Markussen, F. H., Breitwieser, W. & Ephrussi, A. Efficient translation and phosphorylation of Oskar require Oskar protein and the RNA helicase Vasa. Cold Spring Harb. Symp. Quant. Biol. 62, 13-17 (1997).
    • (1997) Cold Spring Harb. Symp. Quant. Biol. , vol.62 , pp. 13-17
    • Markussen, F.H.1    Breitwieser, W.2    Ephrussi, A.3
  • 24
    • 0033231210 scopus 로고    scopus 로고
    • The Drosophila CPEB homolog, Orb, is required for Oskar protein expression in oocytes
    • Chang, J. S., Tan, L. & Schedl, P. The Drosophila CPEB homolog, Orb, is required for Oskar protein expression in oocytes. Dev. Biol. 215, 91-106 (1999).
    • (1999) Dev. Biol. , vol.215 , pp. 91-106
    • Chang, J.S.1    Tan, L.2    Schedl, P.3
  • 25
    • 0037350432 scopus 로고    scopus 로고
    • Orb and along poly(A) tail are required for efficient oskar translation at the posterior pole of the Drosophila oocyte
    • Castagnetti, S. & Ephrussi, A. Orb and along poly(A) tail are required for efficient oskar translation at the posterior pole of the Drosophila oocyte. Development 130, 835-843 (2003).
    • (2003) Development , vol.130 , pp. 835-843
    • Castagnetti, S.1    Ephrussi, A.2
  • 26
    • 0034653570 scopus 로고    scopus 로고
    • Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation
    • Micklem, D. R., Adams, J., Grunert, S. & St. Johnston, D. Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation. EMBO J. 19, 1366-1377 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1366-1377
    • Micklem, D.R.1    Adams, J.2    Grunert, S.3    St. Johnston, D.4
  • 27
    • 0029980987 scopus 로고    scopus 로고
    • Aubergine enhances oskar translation in the Drosophila ovary
    • Wilson, J. E., Connell, J. E. & Macdonald, P. M. Aubergine enhances oskar translation in the Drosophila ovary. Development 122, 1631-1639 (1996).
    • (1996) Development , vol.122 , pp. 1631-1639
    • Wilson, J.E.1    Connell, J.E.2    Macdonald, P.M.3
  • 28
    • 0034925616 scopus 로고    scopus 로고
    • Aubergine encodes a Drosophila polar granule component required for pole cell formation and related to elF2C
    • Harris, A. N. & Macdonald, P. M. Aubergine encodes a Drosophila polar granule component required for pole cell formation and related to elF2C. Development 128, 2823-2832 (2001).
    • (2001) Development , vol.128 , pp. 2823-2832
    • Harris, A.N.1    Macdonald, P.M.2
  • 29
    • 0036682990 scopus 로고    scopus 로고
    • RNAi is activated during Drosophila oocyte maturation in a manner dependent on aubergine and spindle-E
    • Kennerdell, J. R., Yamaguchi, S. & Carthew, R. W. RNAi is activated during Drosophila oocyte maturation in a manner dependent on aubergine and spindle-E. Genes Dev 16, 1884-1889 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 1884-1889
    • Kennerdell, J.R.1    Yamaguchi, S.2    Carthew, R.W.3
  • 30
    • 0036337502 scopus 로고    scopus 로고
    • An anterior function for the Drosophila posterior determinant Pumilio
    • Gamberi, C., Peterson, D. S., He, L. & Gottlieb, E. An anterior function for the Drosophila posterior determinant Pumilio. Development 129, 2699-2710 (2002).
    • (2002) Development , vol.129 , pp. 2699-2710
    • Gamberi, C.1    Peterson, D.S.2    He, L.3    Gottlieb, E.4
  • 31
    • 0031603007 scopus 로고    scopus 로고
    • Maternal control of pattern formation in early Caenorhabditis elegans embryos
    • Bowerman, B. Maternal control of pattern formation in early Caenorhabditis elegans embryos. Curr. Top. Dev. Biol. 39, 73-117 (1998).
    • (1998) Curr. Top. Dev. Biol. , vol.39 , pp. 73-117
    • Bowerman, B.1
  • 32
    • 0025015282 scopus 로고
    • Selective silencing of cell communication influences anteroposterior pattern formation in C. elegans
    • Waring, D. A. & Kenyon, C. Selective silencing of cell communication influences anteroposterior pattern formation in C. elegans. Cell 60, 123-131 (1990).
    • (1990) Cell , vol.60 , pp. 123-131
    • Waring, D.A.1    Kenyon, C.2
  • 33
    • 0030592556 scopus 로고    scopus 로고
    • Spatial and temporal controls target pal-1 blastomere-specification activity to a single blastomere lineage in C. elegans embryos
    • Hunter, C. P. & Kenyon, C. Spatial and temporal controls target pal-1 blastomere-specification activity to a single blastomere lineage in C. elegans embryos. Cell 87, 217-226 (1996).
    • (1996) Cell , vol.87 , pp. 217-226
    • Hunter, C.P.1    Kenyon, C.2
  • 34
    • 0030592578 scopus 로고    scopus 로고
    • MEX-3 is a KH domain protein that regulates blastomere identity in early C. elegans embryos
    • Draper, B. W., Mello, C. C., Bowerman, B., Hardin, J. & Priess, J. R. MEX-3 is a KH domain protein that regulates blastomere identity in early C. elegans embryos. Cell 87, 205-216 (1996).
    • (1996) Cell , vol.87 , pp. 205-216
    • Draper, B.W.1    Mello, C.C.2    Bowerman, B.3    Hardin, J.4    Priess, J.R.5
  • 35
    • 0036339909 scopus 로고    scopus 로고
    • MEX-3 interacting proteins link cell polarity to asymmetric gene expression in Caenorhabditis elegans
    • Huang, N. N., Mootz, D. E., Walhout, A. J., Vidal, M. & Hunter, C. P. MEX-3 interacting proteins link cell polarity to asymmetric gene expression in Caenorhabditis elegans. Development 129, 747-759 (2002). Reference 35 shows that MEX-5, MEX-6 and SPN-4, which function downstream of PAR-1, a protein central to the establishment of embryonic polarity, link cell polarity with asymmetric gene expression by regulating the activity of MEX-3, a translational repressor of pal-1.
    • (2002) Development , vol.129 , pp. 747-759
    • Huang, N.N.1    Mootz, D.E.2    Walhout, A.J.3    Vidal, M.4    Hunter, C.P.5
  • 36
    • 0033634970 scopus 로고    scopus 로고
    • MEX-5 and MEX-6 function to establish soma/germline asymmetry in early C. elegans embryos
    • Schubert, C. M., Lin, R., de Vries, C. J., Plasterk, R. H. & Priess, J. R. MEX-5 and MEX-6 function to establish soma/germline asymmetry in early C. elegans embryos. Mol. Cell 5, 671-682 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 671-682
    • Schubert, C.M.1    Lin, R.2    De Vries, C.J.3    Plasterk, R.H.4    Priess, J.R.5
  • 37
    • 0037032795 scopus 로고    scopus 로고
    • Anterior-posterior polarity in C. elegans and Drosophila - PARallels and differences
    • Pellettieri, J. & Seydoux, G. Anterior-posterior polarity in C. elegans and Drosophila - PARallels and differences. Science 298, 1946-1950 (2002).
    • (2002) Science , vol.298 , pp. 1946-1950
    • Pellettieri, J.1    Seydoux, G.2
  • 38
    • 0035160113 scopus 로고    scopus 로고
    • The maternal gene spn-4 encodes a predicted RRM protein required for mitotic spindle orientation and cell fate patterning in early C. elegans embryos
    • Gomes, J. E. et al. The maternal gene spn-4 encodes a predicted RRM protein required for mitotic spindle orientation and cell fate patterning in early C. elegans embryos. Development 128, 4301-4314 (2001).
    • (2001) Development , vol.128 , pp. 4301-4314
    • Gomes, J.E.1
  • 39
    • 0028217190 scopus 로고
    • Translational control of maternal glp-1 MRNA establishes an asymmetry in the C. elegans embryo
    • Evans, T. C., Crittenden, S. L., Kodoyianni, V. & Kimble, J. Translational control of maternal glp-1 MRNA establishes an asymmetry in the C. elegans embryo. Cell 77, 183-194 (1994).
    • (1994) Cell , vol.77 , pp. 183-194
    • Evans, T.C.1    Crittenden, S.L.2    Kodoyianni, V.3    Kimble, J.4
  • 40
    • 0028283996 scopus 로고
    • The maternal genes apx-1 and qlp-1 and establishment of dorsal-ventral polarity in the early C. elegans embryo
    • Mello, C. C., Draper, B. W. & Priess, J. R. The maternal genes apx-1 and qlp-1 and establishment of dorsal-ventral polarity in the early C. elegans embryo. Cell 77, 95-106 (1994).
    • (1994) Cell , vol.77 , pp. 95-106
    • Mello, C.C.1    Draper, B.W.2    Priess, J.R.3
  • 41
    • 0023667756 scopus 로고
    • Cellular interactions in early C. elegans embryos
    • Priess, J. R. & Thomson, J. N. Cellular interactions in early C. elegans embryos. Cell 48, 241-250 (1987).
    • (1987) Cell , vol.48 , pp. 241-250
    • Priess, J.R.1    Thomson, J.N.2
  • 42
    • 0035107906 scopus 로고    scopus 로고
    • Conservation of glp-1 regulation and function in nematodes
    • Rudel, D. & Kimble, J. Conservation of glp-1 regulation and function in nematodes. Genetics 157, 639-654 (2001).
    • (2001) Genetics , vol.157 , pp. 639-654
    • Rudel, D.1    Kimble, J.2
  • 43
    • 0042330209 scopus 로고    scopus 로고
    • Translational repression of a C. elegans Notch mRNA by the STAR/KH domain protein GLD-1
    • in the press
    • Marin, V. A. & Evans, T. C. Translational repression of a C. elegans Notch mRNA by the STAR/KH domain protein GLD-1. Development (in the press). Work showing that GLD-1, a STAR family RNA-binding protein, helps to regulate the decision between mitosis and meiosis in the germline by controlling the translation of the glp-1 mRNA.
    • Development
    • Marin, V.A.1    Evans, T.C.2
  • 44
    • 0038010231 scopus 로고    scopus 로고
    • Translational control of maternal glp-1 mRNA by POS-1 and its interacting protein SPN-4 in Caenorhabditis elegans
    • Ogura, K., Kishimoto, N., Mitani, S., Gengyo-Ando, K. & Kohara, Y. Translational control of maternal glp-1 mRNA by POS-1 and its interacting protein SPN-4 in Caenorhabditis elegans. Development 130, 2495-2503 (2003).
    • (2003) Development , vol.130 , pp. 2495-2503
    • Ogura, K.1    Kishimoto, N.2    Mitani, S.3    Gengyo-Ando, K.4    Kohara, Y.5
  • 45
    • 0028796703 scopus 로고
    • gld-1, a tumor suppressor gene required for oocyte development in Caenorhabditis elegans
    • Francis, R., Barton, M. K., Kimble, J. & Schedl, T. gld-1, a tumor suppressor gene required for oocyte development in Caenorhabditis elegans. Genetics 139, 579-606 (1995).
    • (1995) Genetics , vol.139 , pp. 579-606
    • Francis, R.1    Barton, M.K.2    Kimble, J.3    Schedl, T.4
  • 46
    • 0031451912 scopus 로고    scopus 로고
    • STAR, a gene family involved in signal transduction and activation of RNA
    • Vernet, C. & Artzt, K. STAR, a gene family involved in signal transduction and activation of RNA. Trends Genet. 13, 479-484 (1997).
    • (1997) Trends Genet. , vol.13 , pp. 479-484
    • Vernet, C.1    Artzt, K.2
  • 47
    • 0028873015 scopus 로고
    • Analysis of the multiple roles of gld-1 in germline development: Interactions with the sex determination cascade and the glp-1 signaling pathway
    • Francis, R., Maine, E. & Schedl, T. Analysis of the multiple roles of gld-1 in germline development: interactions with the sex determination cascade and the glp-1 signaling pathway. Genetics 139, 607-630 (1995).
    • (1995) Genetics , vol.139 , pp. 607-630
    • Francis, R.1    Maine, E.2    Schedl, T.3
  • 48
    • 0032922940 scopus 로고    scopus 로고
    • pos-1 encodes a cytoplasmic zinc-finger protein essential for germline specification in C. elegans
    • Tabara, H., Hill, R. J., Mello, C. C., Priess, J. R. & Kohara, Y. pos-1 encodes a cytoplasmic zinc-finger protein essential for germline specification in C. elegans. Development 126, 1-11 (1999).
    • (1999) Development , vol.126 , pp. 1-11
    • Tabara, H.1    Hill, R.J.2    Mello, C.C.3    Priess, J.R.4    Kohara, Y.5
  • 49
    • 0031451172 scopus 로고    scopus 로고
    • The LIN-12/Notch signaling pathway and its regulation
    • Kimble, J. & Simpson, P. The LIN-12/Notch signaling pathway and its regulation. Annu. Rev. Cell Dev. Biol. 13, 333-361 (1997).
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 333-361
    • Kimble, J.1    Simpson, P.2
  • 50
    • 0035883742 scopus 로고    scopus 로고
    • Identification of in vivo mRNA targets of GLD-1, a maxi-KH motif containing protein required for C. elegans germ cell development
    • Lee, M. H. & Schedl, T. Identification of in vivo mRNA targets of GLD-1, a maxi-KH motif containing protein required for C. elegans germ cell development. Genes Dev. 15, 2408-2420 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2408-2420
    • Lee, M.H.1    Schedl, T.2
  • 51
    • 0035674968 scopus 로고    scopus 로고
    • Caenorhabditis elegans MES-3 is a target of GLD-1 and functions epigenetically in germline development
    • Xu, L., Paulsen, J., Yoo, Y., Goodwin, E. B. & Strome, S. Caenorhabditis elegans MES-3 is a target of GLD-1 and functions epigenetically in germline development. Genetics 159, 1007-1017 (2001).
    • (2001) Genetics , vol.159 , pp. 1007-1017
    • Xu, L.1    Paulsen, J.2    Yoo, Y.3    Goodwin, E.B.4    Strome, S.5
  • 52
    • 0033521534 scopus 로고    scopus 로고
    • The STAR protein, GLD-1, is a translational regulator of sexual identity in Caenorhabditis elegans
    • Jan, E., Motzny, C. K., Graves, L. E. & Goodwin, E. B. The STAR protein, GLD-1, is a translational regulator of sexual identity in Caenorhabditis elegans. EMBO J. 18, 258-269 (1999).
    • (1999) EMBO J. , vol.18 , pp. 258-269
    • Jan, E.1    Motzny, C.K.2    Graves, L.E.3    Goodwin, E.B.4
  • 53
    • 0031452082 scopus 로고    scopus 로고
    • A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germline
    • Zhang, B. et al. A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germline. Nature 390, 477-484 (1997).
    • (1997) Nature , vol.390 , pp. 477-484
    • Zhang, B.1
  • 54
    • 0037030730 scopus 로고    scopus 로고
    • A conserved RNA-binding protein controls germline stem cells in Caenorhabditis elegans
    • Crittenden, S. L. et al. A conserved RNA-binding protein controls germline stem cells in Caenorhabditis elegans. Nature 417, 660-603 (2002). Reference 54 shows that the conserved FBF proteins, members of the PUF family, in part regulate the mitosis/meiosis decision in C. elegans by regulating the activity of the gld-1 mRNA.
    • (2002) Nature , vol.417 , pp. 660-603
    • Crittenden, S.L.1
  • 55
    • 0031778453 scopus 로고    scopus 로고
    • Genetic regulation of entry into meiosis in Caenorhabditis elegans
    • Kadyk, L. C. & Kimble, J. Genetic regulation of entry into meiosis in Caenorhabditis elegans. Development 125, 1803-1813 (1998).
    • (1998) Development , vol.125 , pp. 1803-1813
    • Kadyk, L.C.1    Kimble, J.2
  • 56
    • 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 419, 312-316 (2002). Evidence that GLD-2 is a new form of poly(A) polymerase that functions with GLD-3, a KH-binding protein, to regulate germline cell-fate decisions in C. elegans.
    • (2002) Nature , vol.419 , pp. 312-316
    • Wang, L.1    Eckmann, C.R.2    Kadyk, L.C.3    Wickens, M.4    Kimble, J.5
  • 57
    • 0036848046 scopus 로고    scopus 로고
    • GLD-3, a bicaudal-C homolog that inhibits FBF to control germline sex determination in C. elegans
    • Eckmann, C. R., Kraemer, B., Wickens, M. & Kimble, J. GLD-3, a bicaudal-C homolog that inhibits FBF to control germline sex determination in C. elegans. Dev. Cell 3, 697-710 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 697-710
    • Eckmann, C.R.1    Kraemer, B.2    Wickens, M.3    Kimble, J.4
  • 58
    • 0030755562 scopus 로고    scopus 로고
    • A novel group of pumilio mutations affects the asymmetric division of germline stem cells in the Drosophila ovary
    • Lin, H. & Spradling, A. C. A novel group of pumilio mutations affects the asymmetric division of germline stem cells in the Drosophila ovary. Development 124, 2463-2476 (1997).
    • (1997) Development , vol.124 , pp. 2463-2476
    • Lin, H.1    Spradling, A.C.2
  • 59
    • 0031885720 scopus 로고    scopus 로고
    • Nanos and Pumilio have critical roles in the development and function of Drosophila germline stem cells
    • Forbes, A. & Lehmann, R. Nanos and Pumilio have critical roles in the development and function of Drosophila germline stem cells. Development 125, 679-690 (1998).
    • (1998) Development , vol.125 , pp. 679-690
    • Forbes, A.1    Lehmann, R.2
  • 60
    • 0032767435 scopus 로고    scopus 로고
    • Starvation promotes Dictyostelium development by relieving PufA inhibition of PKA translation through the YakA kinase pathway
    • Souza, G. M., da Silva, A. M. & Kuspa, A, Starvation promotes Dictyostelium development by relieving PufA inhibition of PKA translation through the YakA kinase pathway. Development 126, 3263-3274 (1999).
    • (1999) Development , vol.126 , pp. 3263-3274
    • Souza, G.M.1    Da Silva, A.M.2    Kuspa, A.3
  • 61
    • 0030916153 scopus 로고    scopus 로고
    • Redistribution of silencing proteins from telomeres to the nucleolus is associated with extension of life span in S. cerevisiae
    • Kennedy, B. K. et al. Redistribution of silencing proteins from telomeres to the nucleolus is associated with extension of life span in S. cerevisiae. Cell 89, 381-391 (1997).
    • (1997) Cell , vol.89 , pp. 381-391
    • Kennedy, B.K.1
  • 62
    • 0037022244 scopus 로고    scopus 로고
    • Turning clustering loops: Sex determination in Caenorhabditis elegans
    • Goodwin, E, B. & Ellis, R. E. Turning clustering loops: sex determination in Caenorhabditis elegans. Curr. Biol. 12, R111-R120 (2002).
    • (2002) Curr. Biol. , vol.12
    • Goodwin, E.B.1    Ellis, R.E.2
  • 63
    • 0027507891 scopus 로고
    • Translational regulation of tra-2 by its 3′ untranslated region controls sexual identity in C. elegans
    • Goodwin, E. B., Okkema, P. G., Evans, T. C. & Kimble, J. Translational regulation of tra-2 by its 3′ untranslated region controls sexual identity in C. elegans. Cell 75, 329-339 (1993).
    • (1993) Cell , vol.75 , pp. 329-339
    • Goodwin, E.B.1    Okkema, P.G.2    Evans, T.C.3    Kimble, J.4
  • 65
    • 0034519641 scopus 로고    scopus 로고
    • FOG-2, a novel F-box containing protein, associates with the GLD-1 RNA binding protein and directs male sex determination in the C. elegans hermaphrodite germline
    • Clifford, R. et al. FOG-2, a novel F-box containing protein, associates with the GLD-1 RNA binding protein and directs male sex determination in the C. elegans hermaphrodite germline. Development 127, 5265-5276 (2000).
    • (2000) Development , vol.127 , pp. 5265-5276
    • Clifford, R.1
  • 66
    • 0030663764 scopus 로고    scopus 로고
    • Conservation of the C. elegans tra-2 3′-UTR translational control
    • Jan, E., Yoon, J., Watterhouse, D., Iannaccone, P. & Goodwin, E. Conservation of the C. elegans tra-2 3′-UTR translational control. EMBO J. 16, 6301-6313 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6301-6313
    • Jan, E.1    Yoon, J.2    Watterhouse, D.3    Iannaccone, P.4    Goodwin, E.5
  • 67
    • 0033598198 scopus 로고    scopus 로고
    • NANOS-3 and FBF proteins physically interact to control the sperm-oocyte switch in Caenorhabditis elegans
    • Kraemer, B. et al. NANOS-3 and FBF proteins physically interact to control the sperm-oocyte switch in Caenorhabditis elegans. Curr. Biol. 9, 1009-1018 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1009-1018
    • Kraemer, B.1
  • 68
    • 0038747216 scopus 로고    scopus 로고
    • Conservation of a Pumilio-Nanos complex from Drosophila germ plasm to human germ cells
    • Jaruzelska, J. et al. Conservation of a Pumilio-Nanos complex from Drosophila germ plasm to human germ cells. Dev. Genes Evol. 213, 120-126 (2003).
    • (2003) Dev. Genes Evol. , vol.213 , pp. 120-126
    • Jaruzelska, J.1
  • 69
    • 0036066063 scopus 로고    scopus 로고
    • A TB-RBP and Ter ATPase complex accompanies specific mRNAs from nuclei through the nuclear pores and into intercellular bridges in muse male germ cells
    • Morales, C. R. et al. A TB-RBP and Ter ATPase complex accompanies specific mRNAs from nuclei through the nuclear pores and into intercellular bridges in muse male germ cells. Dev. Biol. 246, 480-494 (2002). This study shows that TB-RBP and TerATPase interact with prm-1 and prm-2 mRNA in the nucleus and accompany them into the cytoplasm, which indicates that the 'nuclear history' of these mRNAs might influence cytoplasmic activity.
    • (2002) Dev. Biol. , vol.246 , pp. 480-494
    • Morales, C.R.1
  • 70
    • 0025806761 scopus 로고
    • Cytoplasmic protein binding to highly conserved sequences in the 3′ untranslated region of mouse protamine 2 mRNA, a translationally regulated transcript of male germ cells
    • Kwon, Y. K. & Hecht, N. B. Cytoplasmic protein binding to highly conserved sequences in the 3′ untranslated region of mouse protamine 2 mRNA, a translationally regulated transcript of male germ cells. Proc. Natl Acad. Sci. USA 88, 3584-3588 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3584-3588
    • Kwon, Y.K.1    Hecht, N.B.2
  • 71
    • 0027493492 scopus 로고
    • Binding of a phosphoprotein to the 3′ untranslated region of the mouse protamine 2 mRNA temporally represses its translation
    • Kwon, Y. K. & Hecht, N. B. Binding of a phosphoprotein to the 3′ untranslated region of the mouse protamine 2 mRNA temporally represses its translation. Mol. Cell. Biol. 13, 6547-6557 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6547-6557
    • Kwon, Y.K.1    Hecht, N.B.2
  • 72
    • 0029166131 scopus 로고
    • Testis-brain RNA-binding protein, a testicular translational regulatory RNA-binding protein, is present in the brain and binds to the 3′ untranslated regions of transported brain mRNAs
    • Han, J. R., Gu, W. & Hecht, N. B. Testis-brain RNA-binding protein, a testicular translational regulatory RNA-binding protein, is present in the brain and binds to the 3′ untranslated regions of transported brain mRNAs. Biol. Reprod. 53, 707-717 (1995).
    • (1995) Biol. Reprod. , vol.53 , pp. 707-717
    • Han, J.R.1    Gu, W.2    Hecht, N.B.3
  • 73
    • 0030940297 scopus 로고    scopus 로고
    • The RNA-binding protein, TB-RBP, is the mouse homologue of translin, a recombination protein associated with chromosomal translocations
    • Wu, X. Q., Gu, W., Meng, X. & Hecht, N. B. The RNA-binding protein, TB-RBP, is the mouse homologue of translin, a recombination protein associated with chromosomal translocations. Proc. Natl Acad. Sci. USA 94, 5640-5645 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5640-5645
    • Wu, X.Q.1    Gu, W.2    Meng, X.3    Hecht, N.B.4
  • 74
    • 0032545356 scopus 로고    scopus 로고
    • The dendritic translocation of translin protein in the form of BC1 RNA protein particles in developing rat hippocampal neurons in primary culture
    • Kobayashi, S., Takashima, A. & Anzai, K. The dendritic translocation of translin protein in the form of BC1 RNA protein particles in developing rat hippocampal neurons in primary culture. Biochem. Biophys. Res. Commun. 253, 448-453 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 448-453
    • Kobayashi, S.1    Takashima, A.2    Anzai, K.3
  • 75
    • 0033812370 scopus 로고    scopus 로고
    • Somatodendritic localization of Translin, a component of the Translin/Trax RNA binding complex
    • Finkenstadt, P. M. et al. Somatodendritic localization of Translin, a component of the Translin/Trax RNA binding complex. J. Neurochem. 75, 1754-1762 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 1754-1762
    • Finkenstadt, P.M.1
  • 76
    • 0032147094 scopus 로고    scopus 로고
    • Gene regulation by Y-box proteins: Coupling control of transcription and translation
    • Matsumoto, K. & Wolffe, A. P. Gene regulation by Y-box proteins: coupling control of transcription and translation. Trends Cell Biol. 8, 318-323 (1998).
    • (1998) Trends Cell Biol. , vol.8 , pp. 318-323
    • Matsumoto, K.1    Wolffe, A.P.2
  • 77
    • 0036678329 scopus 로고    scopus 로고
    • Translational repression by MSY4 inhibits spermatid differentiation in mice
    • Giorgini, F., Davies, H. G. & Braun, R, E. Translational repression by MSY4 inhibits spermatid differentiation in mice. Development 129, 3669-3679 (2002).
    • (2002) Development , vol.129 , pp. 3669-3679
    • Giorgini, F.1    Davies, H.G.2    Braun, R.E.3
  • 78
    • 0034806975 scopus 로고    scopus 로고
    • MSY2 and MSY4 bind a conserved sequence in the 3′ untranslated region of protamine 1 mRNA in vitro and in vivo
    • Giorgini, F., Davies, H. G. & Braun, R. E. MSY2 and MSY4 bind a conserved sequence in the 3′ untranslated region of protamine 1 mRNA in vitro and in vivo. Mol. Cell. Biol. 21, 7010-7019 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7010-7019
    • Giorgini, F.1    Davies, H.G.2    Braun, R.E.3
  • 79
    • 0034072921 scopus 로고    scopus 로고
    • Temporal control of protein synthesis during spermatogenesis
    • Braun, R. E. Temporal control of protein synthesis during spermatogenesis. Int. J. Androl. 23 Suppl. 2, 92-94 (2000).
    • (2000) Int. J. Androl. , vol.23 , Issue.SUPPL. 2 , pp. 92-94
    • Braun, R.E.1
  • 80
    • 0034194544 scopus 로고    scopus 로고
    • A sequence-specific RNA binding complex expressed in murine germ cells contains MSY2 and MSY4
    • Davies, H. G., Giorgini, F., Fajardo, M. A. & Braun, R. E. A sequence-specific RNA binding complex expressed in murine germ cells contains MSY2 and MSY4. Dev. Biol. 221, 87-100 (2000).
    • (2000) Dev. Biol. , vol.221 , pp. 87-100
    • Davies, H.G.1    Giorgini, F.2    Fajardo, M.A.3    Braun, R.E.4
  • 81
    • 0033052048 scopus 로고    scopus 로고
    • A double-stranded RNA binding protein required for activation of repressed messages in mammalian germ cells
    • Zhong, J., Peters, A. H., Lee, K. & Braun, R. E. A double-stranded RNA binding protein required for activation of repressed messages in mammalian germ cells. Nature Genet. 22, 171-174 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 171-174
    • Zhong, J.1    Peters, A.H.2    Lee, K.3    Braun, R.E.4
  • 82
    • 0027751663 scopus 로고
    • The C. elegans heterochronic gene lin-4 encodes small RNAs with antisense complementarity to lin-14
    • Lee, R. C., Feinbaum, R. L. & Ambros, V. The C. elegans heterochronic gene lin-4 encodes small RNAs with antisense complementarity to lin-14. Cell 75, 843-845 (1993). Reference 85 reports the cloning and characterization of the lin-4 mRNA, the first miRNA to be cloned.
    • (1993) Cell , vol.75 , pp. 843-845
    • Lee, R.C.1    Feinbaum, R.L.2    Ambros, V.3
  • 83
    • 0028766128 scopus 로고
    • RNA. deviants - Or emissaries
    • Wickens, M. & Takayama, K. RNA. Deviants - or emissaries. Nature 367, 17-18 (1994).
    • (1994) Nature , vol.367 , pp. 17-18
    • Wickens, M.1    Takayama, K.2
  • 84
    • 0037108567 scopus 로고    scopus 로고
    • MicroRNAs: Something new under the sun
    • Moss, E. G. & Poethig, R. S. MicroRNAs: something new under the sun. Curr. Biol. 12, R688-R690 (2002).
    • (2002) Curr. Biol. , vol.12
    • Moss, E.G.1    Poethig, R.S.2
  • 85
    • 0036534284 scopus 로고    scopus 로고
    • MicroRNAs: Deviants no longer
    • Pasquinelli, A. E. MicroRNAs: deviants no longer. Trends Genet, 18, 171-173 (2002).
    • (2002) Trends Genet. , vol.18 , pp. 171-173
    • Pasquinelli, A.E.1
  • 86
    • 0035955361 scopus 로고    scopus 로고
    • An abundant class of tiny RNAs with probable regulatory roles in Caenorhabditis elegans
    • Lau, N. C., Lim, L. P. Weinstein, E. G. & Bartel, D. P. An abundant class of tiny RNAs with probable regulatory roles in Caenorhabditis elegans. Science 294, 858-862 (2001).
    • (2001) Science , vol.294 , pp. 858-862
    • Lau, N.C.1    Lim, L.P.2    Weinstein, E.G.3    Bartel, D.P.4
  • 87
    • 0035955366 scopus 로고    scopus 로고
    • An extensive class of small RNAs in Caenorhabditis elegans
    • Lee, R. C. & Ambros, V. An extensive class of small RNAs in Caenorhabditis elegans. Science 294, 862-864 (2001).
    • (2001) Science , vol.294 , pp. 862-864
    • Lee, R.C.1    Ambros, V.2
  • 90
    • 0037418839 scopus 로고    scopus 로고
    • Bantam encodes a developmentally regulated microRNA that controls cell proliferation and regulates the proapoptotic gene hid in Drosophila
    • Brennecke, J., Hipfner, D. R., Stark, A., Russell, R. B. & Cohen, S. M. bantam encodes a developmentally regulated microRNA that controls cell proliferation and regulates the proapoptotic gene hid in Drosophila. Cell 113, 25-36 (2003).
    • (2003) Cell , vol.113 , pp. 25-36
    • Brennecke, J.1    Hipfner, D.R.2    Stark, A.3    Russell, R.B.4    Cohen, S.M.5
  • 91
    • 0035458760 scopus 로고    scopus 로고
    • Control of developmental timing in animals
    • Rougvie, A. E. Control of developmental timing in animals. Nature Rev. Genet. 2, 690-701 (2001).
    • (2001) Nature Rev. Genet. , vol.2 , pp. 690-701
    • Rougvie, A.E.1
  • 92
    • 0034708122 scopus 로고    scopus 로고
    • The 21-nucleotide let-7 RNA regulates developmental timing in Caenorhabditis elegans
    • Reinhart, B. J. et al. The 21-nucleotide let-7 RNA regulates developmental timing in Caenorhabditis elegans. Nature 403, 901-906 (2000).
    • (2000) Nature , vol.403 , pp. 901-906
    • Reinhart, B.J.1
  • 93
    • 0033634943 scopus 로고    scopus 로고
    • The lin-41 RBCC gene acts in the C. elegans heterochronic pathway between the let-7 regulatory RNA and the LIN-29 transcription factor
    • Slack, F. J. et al. The lin-41 RBCC gene acts in the C. elegans heterochronic pathway between the let-7 regulatory RNA and the LIN-29 transcription factor. Mol. Cell 5, 659-669 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 659-669
    • Slack, F.J.1
  • 94
    • 0034735936 scopus 로고    scopus 로고
    • The Caenorhabditis elegans heterochronic gene lin-29 coordinates the vulval-uterine-epidermal connections
    • Newman, A. P., Inoue, T., Wang, M. & Sternberg, P. W. The Caenorhabditis elegans heterochronic gene lin-29 coordinates the vulval-uterine-epidermal connections. Curr. Biol. 10, 1479-1488 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 1479-1488
    • Newman, A.P.1    Inoue, T.2    Wang, M.3    Sternberg, P.W.4
  • 95
    • 0037693842 scopus 로고    scopus 로고
    • The C. elegans hunchback homologue, hbl-1, controls temporal patteming and is a probably microRNA target
    • Lin, S. et al. The C. elegans hunchback homologue, hbl-1, controls temporal patteming and is a probably microRNA target. Dev. Cell 4, 639-650 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 639-650
    • Lin, S.1
  • 96
    • 0038708326 scopus 로고    scopus 로고
    • The Caenorhaditis elegans hunchback-like gene lin57/hbl-1 controls developmental time and is regulated by microRNAs
    • Abrahante, J. E. et al. The Caenorhaditis elegans hunchback-like gene lin57/hbl-1 controls developmental time and is regulated by microRNAs. Dev. Cell 4, 625-637 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 625-637
    • Abrahante, J.E.1
  • 97
    • 0034597777 scopus 로고    scopus 로고
    • Conservation of the sequence and temporal expression of let-7 heterochronic regulatory RNA
    • Pasquinelli, A. E, et al. Conservation of the sequence and temporal expression of let-7 heterochronic regulatory RNA. Nature 408, 86-89 (2000). Evidence that let-7, an miRNA, is highly conserved and that it is processed from a stem-loop precursor.
    • (2000) Nature , vol.408 , pp. 86-89
    • Pasquinelli, A.E.1
  • 98
    • 0032437667 scopus 로고    scopus 로고
    • Control of translation initiation in animals
    • Gray, N. K. & Wickens, M. Control of translation initiation in animals. Annu. Rev. Cell Dev. Biol. 14, 399-458 (1998).
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 399-458
    • Gray, N.K.1    Wickens, M.2
  • 99
    • 0031864465 scopus 로고    scopus 로고
    • Sex-lethal, the master sex-determining gene in Drosophila, is not sex-specifically regulated in Musca domestica
    • Meise, M. et al. Sex-lethal, the master sex-determining gene in Drosophila, is not sex-specifically regulated in Musca domestica. Development 125, 1487-1494 (1998).
    • (1998) Development , vol.125 , pp. 1487-1494
    • Meise, M.1
  • 100
    • 0031894413 scopus 로고    scopus 로고
    • The Drosophila splicing regulator sex-lethal directly inhibits translation of male-specific-lethal 2 mRNA
    • Gebauer, F., Merendino, L., Hentze, M. W. & Valcarcel, J. The Drosophila splicing regulator sex-lethal directly inhibits translation of male-specific-lethal 2 mRNA. RNA 4, 142-150 (1998).
    • (1998) RNA , vol.4 , pp. 142-150
    • Gebauer, F.1    Merendino, L.2    Hentze, M.W.3    Valcarcel, J.4
  • 101
    • 0030678550 scopus 로고    scopus 로고
    • The regulation of the Drosophila msl-2 gene reveals a function for sex-lethal in translational control
    • Bashaw, G. J. & Baker, B. S. The regulation of the Drosophila msl-2 gene reveals a function for Sex-lethal in translational control. Cell 89, 789-798 (1997).
    • (1997) Cell , vol.89 , pp. 789-798
    • Bashaw, G.J.1    Baker, B.S.2
  • 102
    • 0030913367 scopus 로고    scopus 로고
    • Sex lethal controls dosage compensation in Drosophila by a non-splicing mechanism
    • Kelley, R. L., Wang, J., Bell, L. & Kuroda, M. I. Sex lethal controls dosage compensation in Drosophila by a non-splicing mechanism. Nature 387, 195-199 (1997).
    • (1997) Nature , vol.387 , pp. 195-199
    • Kelley, R.L.1    Wang, J.2    Bell, L.3    Kuroda, M.I.4
  • 103
    • 0042483881 scopus 로고    scopus 로고
    • Translational control of dosage compensation in Drosophila: Sex-lethal inhibits the stable association of the 40S ribosomal subunit with msl-2 mRNA
    • in the press
    • Gebauer, F., Grskovic, M. & Hentze, M. W. Translational control of dosage compensation in Drosophila: Sex-lethal inhibits the stable association of the 40S ribosomal subunit with msl-2 mRNA. Mol. Cell (in the press). This report shows that sex-lethal protein binds to poly(U) elements in the msl-2 mRNA and controls translation by preventing stable binding of the 40S ribosomal subunit to the transcript.
    • Mol. Cell
    • Gebauer, F.1    Grskovic, M.2    Hentze, M.W.3
  • 104
    • 0033229825 scopus 로고    scopus 로고
    • Translational control of dosage compensation in Drosophila by Sex-lethal: Cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail
    • Gebauer, F., Corona, D. F., Preiss, T., Becker, P. B. & Hentze, M. W. Translational control of dosage compensation in Drosophila by Sex-lethal: cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail. EMBO J. 18, 6146-6154 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6146-6154
    • Gebauer, F.1    Corona, D.F.2    Preiss, T.3    Becker, P.B.4    Hentze, M.W.5
  • 105
    • 0028201735 scopus 로고
    • Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region
    • Ostareck-Lederer, A., Ostareck, D, H., Standart, N. & Thiele, B. J. Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region. EMBO J. 13, 1476-1481 (1994).
    • (1994) EMBO J. , vol.13 , pp. 1476-1481
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Standart, N.3    Thiele, B.J.4
  • 106
    • 0030772963 scopus 로고    scopus 로고
    • mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end
    • Ostareck, D. H. et al. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89, 597-606 (1997).
    • (1997) Cell , vol.89 , pp. 597-606
    • Ostareck, D.H.1
  • 107
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: The 3′UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck, D. H., Ostareck-Lederer, A., Shatsky, I. N. & Hentze, M. W. Lipoxygenase mRNA silencing in erythroid differentiation: the 3′UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104, 281-290 (2001). Work showing the translational control of LOX mRNA by the binding of hnRNPs K and E1 to the DICE in the LOX 3′ UTR and inhibition of the association of the 60S subunit.
    • (2001) Cell , vol.104 , pp. 281-290
    • Ostareck, D.H.1    Ostareck-Lederer, A.2    Shatsky, I.N.3    Hentze, M.W.4
  • 108
    • 0036276219 scopus 로고    scopus 로고
    • c-Src-mediated phosphorylation of hnRNP K drives translational activation of specifically silenced mRNAs
    • Ostareck-Lederer, A, et al. c-Src-mediated phosphorylation of hnRNP K drives translational activation of specifically silenced mRNAs. Mol. Cell. Biol. 22, 4535-4543 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4535-4543
    • Ostareck-Lederer, A.1
  • 109
    • 0035404265 scopus 로고    scopus 로고
    • Translational control by CPEB: A means to the end
    • Mendez, R. & Richter, J. D. Translational control by CPEB: a means to the end. Nature Rev. Mol. Cell Biol. 2, 521-529 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 521-529
    • Mendez, R.1    Richter, J.D.2
  • 110
    • 0037099704 scopus 로고    scopus 로고
    • Dissolution of the maskin-elF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation
    • Cao, Q. & Richter, J. D. Dissolution of the maskin-elF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation. EMBO J. 21, 3852-3862 (2002). Reference 113 shows how Maskin silences mRNA translation by binding to and sequestering eIF4E during oocyte maturation. On maturation, the mRNA is actively polyadenylated and recruits PAB. The activity of PAB is needed to dissolve the Maskin-elF4E complex and allow translation.
    • (2002) EMBO J. , vol.21 , pp. 3852-3862
    • Cao, Q.1    Richter, J.D.2
  • 111
    • 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 6, 1253-1259 (2000).
    • (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
  • 112
    • 0034673706 scopus 로고    scopus 로고
    • Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA
    • Mendez, R. et al. Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA. Nature 404, 302-307 (2000).
    • (2000) Nature , vol.404 , pp. 302-307
    • Mendez, R.1
  • 114
    • 0035433727 scopus 로고    scopus 로고
    • Germ cell differentiation and synaptonemal complex formation are disrupted in CPEB knockout mice
    • Tay, J. & Richter, J. D. Germ cell differentiation and synaptonemal complex formation are disrupted in CPEB knockout mice. Dev. Cell 1, 201-213 (2001).
    • (2001) Dev. Cell , vol.1 , pp. 201-213
    • Tay, J.1    Richter, J.D.2
  • 115
    • 0031444409 scopus 로고    scopus 로고
    • Synapse-specific, long-term facilitation of aplysia sensory to motor synapses: A function for local protein synthesis in memory storage
    • Martin, K. C. et al. Synapse-specific, long-term facilitation of aplysia sensory to motor synapses: a function for local protein synthesis in memory storage. Cell 91, 927-938 (1997).
    • (1997) Cell , vol.91 , pp. 927-938
    • Martin, K.C.1
  • 116
    • 0034687228 scopus 로고    scopus 로고
    • Synthesis of the posterior determinant Nanos is spatially restricted by a novel cotranslational regulatory mechanism
    • Clark, I. E., Wyckoff, D. & Gavis, E. R. Synthesis of the posterior determinant Nanos is spatially restricted by a novel cotranslational regulatory mechanism. Curr. Biol. 10, 1311-1314 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 1311-1314
    • Clark, I.E.1    Wyckoff, D.2    Gavis, E.R.3
  • 117
    • 0033572284 scopus 로고    scopus 로고
    • The lin-4 regulatory RNA controls developmental timing in Caenorhabditis elegans by blocking LIN-14 protein synthesis after the initiation of translation
    • Olsen, P. H. & Ambros, V. The lin-4 regulatory RNA controls developmental timing in Caenorhabditis elegans by blocking LIN-14 protein synthesis after the initiation of translation. Dev. Biol. 216, 671-680 (1999).
    • (1999) Dev. Biol. , vol.216 , pp. 671-680
    • Olsen, P.H.1    Ambros, V.2
  • 118
    • 0030753073 scopus 로고    scopus 로고
    • The role of the cap structure in RNA processing and nuclear export
    • Lewis, J. D. & Izaurralde, E. The role of the cap structure in RNA processing and nuclear export. Eur. J. Biochem. 247, 461-469 (1997).
    • (1997) Eur. J. Biochem. , vol.247 , pp. 461-469
    • Lewis, J.D.1    Izaurralde, E.2
  • 119
    • 0033636895 scopus 로고    scopus 로고
    • The yeast nuclear cap binding complex can interact with translation factor elF4G and mediate translation initiation
    • Fortes, P. et al. The yeast nuclear cap binding complex can interact with translation factor elF4G and mediate translation initiation. Mol. Cell 6, 191-196 (2000). This study describes a genetic and physical interaction between CBC and elF4G, and shows that CBC can support translation initiation using an in vitro assay. It indicates that there is an initial round of translation that is perhaps distinct from subsequent rounds.
    • (2000) Mol. Cell , vol.6 , pp. 191-196
    • Fortes, P.1
  • 120
    • 0035823036 scopus 로고    scopus 로고
    • Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20
    • Ishigaki, Y., Li, X., Serin, G. & Maquat, L. E. Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell 106, 607-617 (2001). Provides evidence that mRNAs containing premature termination codons that co-immunoprecipitate with anti-CBC antibodies are subject to nonsense-mediated decay, whereas mRNAs that co-immunoprecipitate with anti-elF4E antibodies are not.
    • (2001) Cell , vol.106 , pp. 607-617
    • Ishigaki, Y.1    Li, X.2    Serin, G.3    Maquat, L.E.4
  • 121
    • 0032055114 scopus 로고    scopus 로고
    • Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA
    • Matsumoto, K., Wassarman, K. M. & Wolffe, A. P. Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA. EMBO J. 17, 2107-2121 (1998). This work shows that the presence, and even the position, of an intron in a pre-mRNA can influence the amount of protein that is synthesized in the nucleus. It indicates that nuclear events, such as pre-mRNA processing, can ultimately affect the cytoplasmic fate of the mRNA.
    • (1998) EMBO J. , vol.17 , pp. 2107-2121
    • Matsumoto, K.1    Wassarman, K.M.2    Wolffe, A.P.3
  • 122
    • 0037406116 scopus 로고    scopus 로고
    • A quantitative analysis of intron effects in mammalian gene expression
    • in the press
    • Nott, A., Meislin, S. H. & Moore, M. J. A quantitative analysis of intron effects in mammalian gene expression. RNA (in the press).
    • RNA
    • Nott, A.1    Meislin, S.H.2    Moore, M.J.3
  • 123
    • 0041481985 scopus 로고    scopus 로고
    • Analysis of the stimulatory effect of splicing in mRNA production and utilization in mammalian cells
    • in the press
    • S., L. & Cullen, B. R. Analysis of the stimulatory effect of splicing in mRNA production and utilization in mammalian cells. RNA (in the press).
    • RNA
    • Cullen, B.R.1
  • 124
    • 0042483880 scopus 로고    scopus 로고
    • How introns influence and enhance eukaryotic gene expression
    • in the press
    • Le Hir, H., Nott, A. & Moore, M. J. How introns influence and enhance eukaryotic gene expression. Trends Biol. Sci. (in the press).
    • Trends Biol. Sci.
    • Le Hir, H.1    Nott, A.2    Moore, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.