메뉴 건너뛰기




Volumn 37, Issue 12, 2005, Pages 1323-1332

A genome-wide RNA interference screen in Drosophila melanogaster cells for new components of the Hh signaling pathway

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN COMPLEX I; CYCLIN DEPENDENT KINASE 9; MESSENGER RNA; NUCLEOPORIN; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOTRANSFERASE; PROTEASOME; RNA; SONIC HEDGEHOG PROTEIN;

EID: 28444451148     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1682     Document Type: Article
Times cited : (166)

References (49)
  • 2
    • 0036778132 scopus 로고    scopus 로고
    • Hedgehog signal transduction: Recent findings
    • Nybakken, K. & Perrimon, N. Hedgehog signal transduction: recent findings. Curr. Opin. Genet. Dev. 12, 503-511 (2002).
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 503-511
    • Nybakken, K.1    Perrimon, N.2
  • 3
    • 2942738996 scopus 로고    scopus 로고
    • The Hedgehog response network: Sensors, switches, and routers
    • Lum, L. & Beachy, P.A. The Hedgehog response network: sensors, switches, and routers. Science 304, 1755-1759 (2004).
    • (2004) Science , vol.304 , pp. 1755-1759
    • Lum, L.1    Beachy, P.A.2
  • 4
    • 4644336023 scopus 로고    scopus 로고
    • Revealing the world of RNA interference
    • Mello, C.C. & Conte, D., Jr. Revealing the world of RNA interference. Nature 431, 338-342 (2004).
    • (2004) Nature , vol.431 , pp. 338-342
    • Mello, C.C.1    Conte Jr., D.2
  • 5
    • 0842309871 scopus 로고    scopus 로고
    • Genome-wide RNAi analysis of growth and viability in Drosophila cells
    • Boutros, M. et al. Genome-wide RNAi analysis of growth and viability in Drosophila cells. Science 303, 832-835 (2004).
    • (2004) Science , vol.303 , pp. 832-835
    • Boutros, M.1
  • 6
    • 13844250535 scopus 로고    scopus 로고
    • Genome-wide RNAi screen reveals a specific sensitivity of IRES-containing RNA viruses to host translation inhibition
    • Cherry, S. et al. Genome-wide RNAi screen reveals a specific sensitivity of IRES-containing RNA viruses to host translation inhibition. Genes Dev. 19, 445-452 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 445-452
    • Cherry, S.1
  • 7
    • 19344370696 scopus 로고    scopus 로고
    • Functional dissection of an innate immune response by a genome-wide RNAi screen
    • Foley, E. & O'Farrell, P.H. Functional dissection of an innate immune response by a genome-wide RNAi screen. PLoS Biol. 2, E203 (2004).
    • (2004) PLoS Biol. , vol.2
    • Foley, E.1    O'Farrell, P.H.2
  • 8
    • 0242361514 scopus 로고    scopus 로고
    • A functional genomic analysis of cell morphology using RNA interference
    • Kiger, A.A. et al. A functional genomic analysis of cell morphology using RNA interference. J. Biol. 2, 27 (2003).
    • (2003) J. Biol. , vol.2 , pp. 27
    • Kiger, A.A.1
  • 9
    • 0037470952 scopus 로고    scopus 로고
    • Identification of Hedgehog pathway components by RNAi in Drosophila cultured cells
    • Lum, L. et al. Identification of Hedgehog pathway components by RNAi in Drosophila cultured cells. Science 299, 2039-2045 (2003).
    • (2003) Science , vol.299 , pp. 2039-2045
    • Lum, L.1
  • 10
    • 0033529667 scopus 로고    scopus 로고
    • Nuclear trafficking of Cubitus interruptus in the transcriptional regulation of Hedgehog target gene expression
    • Chen, C.H. et al. Nuclear trafficking of Cubitus interruptus in the transcriptional regulation of Hedgehog target gene expression. Cell 98, 305-316 (1999).
    • (1999) Cell , vol.98 , pp. 305-316
    • Chen, C.H.1
  • 11
    • 18244400410 scopus 로고    scopus 로고
    • Functional genomic analysis of the Wnt-wingless signaling pathway
    • DasGupta, R., Kaykas, A., Moon, R.T. & Perrimon, N. Functional genomic analysis of the Wnt-wingless signaling pathway. Science 308, 826-833 (2005).
    • (2005) Science , vol.308 , pp. 826-833
    • DasGupta, R.1    Kaykas, A.2    Moon, R.T.3    Perrimon, N.4
  • 12
    • 19344366251 scopus 로고    scopus 로고
    • Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells
    • Lejeune, F. & Maquat, L.E. Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells. Curr. Opin. Cell Biol. 17, 309-315 (2005).
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 309-315
    • Lejeune, F.1    Maquat, L.E.2
  • 13
    • 21144455814 scopus 로고    scopus 로고
    • Alternative splicing facilitates internal ribosome entry on the ornithine decarboxylase mRNA
    • Pyronnet, S., Pradayrol, L. & Sonenberg, N. Alternative splicing facilitates internal ribosome entry on the ornithine decarboxylase mRNA. Cell. Mol. Life Sci. 62, 1267-1274 (2005).
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1267-1274
    • Pyronnet, S.1    Pradayrol, L.2    Sonenberg, N.3
  • 14
    • 0036083677 scopus 로고    scopus 로고
    • Drosophila Roc1a encodes a RING-H2 protein with a unique function in processing the Hh signal transducer Ci by the SCF E3 ubiquitin ligase
    • Noureddine, M.A., Donaldson, T.D., Thacker, S.A. & Duronio, R.J. Drosophila Roc1a encodes a RING-H2 protein with a unique function in processing the Hh signal transducer Ci by the SCF E3 ubiquitin ligase. Dev. Cell 2, 757-770 (2002).
    • (2002) Dev. Cell , vol.2 , pp. 757-770
    • Noureddine, M.A.1    Donaldson, T.D.2    Thacker, S.A.3    Duronio, R.J.4
  • 15
    • 0037106185 scopus 로고    scopus 로고
    • Distinct protein degradation mechanisms mediated by Cul1 and Cul3 controlling Ci stability in Drosophila eye development
    • Ou, C.Y., Lin, Y.F., Chen, Y.J. & Chien, C.T. Distinct protein degradation mechanisms mediated by Cul1 and Cul3 controlling Ci stability in Drosophila eye development. Genes Dev. 16, 2403-2414 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2403-2414
    • Ou, C.Y.1    Lin, Y.F.2    Chen, Y.J.3    Chien, C.T.4
  • 16
    • 0032576777 scopus 로고    scopus 로고
    • Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb
    • Jiang, J. & Struhl, G. Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb. Nature 391, 493-496 (1998).
    • (1998) Nature , vol.391 , pp. 493-496
    • Jiang, J.1    Struhl, G.2
  • 17
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies, R.J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15, 435-467 (1999).
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 18
    • 0031792768 scopus 로고    scopus 로고
    • CDK9 (PITALRE): A multifunctional cdc2-related kinase
    • de Falco, G. & Giordano, A. CDK9 (PITALRE): a multifunctional cdc2-related kinase. J. Cell. Physiol. 177, 501-506 (1998).
    • (1998) J. Cell. Physiol. , vol.177 , pp. 501-506
    • De Falco, G.1    Giordano, A.2
  • 19
    • 0037294769 scopus 로고    scopus 로고
    • Cyclin T: Three forms for different roles in physiological and pathological functions
    • De Luca, A., De Falco, M., Baldi, A. & Paggi, M.G. Cyclin T: three forms for different roles in physiological and pathological functions. J. Cell. Physiol. 194, 101-107 (2003).
    • (2003) J. Cell. Physiol. , vol.194 , pp. 101-107
    • De Luca, A.1    De Falco, M.2    Baldi, A.3    Paggi, M.G.4
  • 20
    • 3242769187 scopus 로고    scopus 로고
    • Cellular control of gene expression by T-type cyclin/CDK9 complexes
    • Garriga, J. & Grana, X. Cellular control of gene expression by T-type cyclin/CDK9 complexes. Gene 337, 15-23 (2004).
    • (2004) Gene , vol.337 , pp. 15-23
    • Garriga, J.1    Grana, X.2
  • 23
    • 0037169530 scopus 로고    scopus 로고
    • PITSLRE p110 protein kinases associate with transcription complexes and affect their activity
    • Trembley, J.H. et al. PITSLRE p110 protein kinases associate with transcription complexes and affect their activity. J. Biol. Chem. 277, 2589-2596 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 2589-2596
    • Trembley, J.H.1
  • 24
    • 0025809046 scopus 로고
    • The crooked neck gene of Drosophila contains a motif found in a family of yeast cell cycle genes
    • Zhang, K., Smouse, D. & Perrimon, N. The crooked neck gene of Drosophila contains a motif found in a family of yeast cell cycle genes. Genes Dev. 5, 1080-1091 (1991).
    • (1991) Genes Dev. , vol.5 , pp. 1080-1091
    • Zhang, K.1    Smouse, D.2    Perrimon, N.3
  • 25
    • 0036391997 scopus 로고    scopus 로고
    • Drosophila crooked-neck protein co-fractionates in a multiprotein complex with splicing factors
    • Raisin-Tani, S. & Leopold, P. Drosophila crooked-neck protein co-fractionates in a multiprotein complex with splicing factors. Biochem. Biophys. Res. Commun. 296, 288-292 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 288-292
    • Raisin-Tani, S.1    Leopold, P.2
  • 26
    • 0032877215 scopus 로고    scopus 로고
    • Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition
    • Chung, S., McLean, M.R. & Rymond, B.C. Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition. RNA 5, 1042-1054 (1999).
    • (1999) RNA , vol.5 , pp. 1042-1054
    • Chung, S.1    McLean, M.R.2    Rymond, B.C.3
  • 28
    • 0032945738 scopus 로고    scopus 로고
    • Trans-acting factors required for inclusion of regulated exons in the Ultrabithorax mRNAs of Drosophila melanogaster
    • Burnette, J.M., Hatton, A.R. & Lopez, A.J. Trans-acting factors required for inclusion of regulated exons in the Ultrabithorax mRNAs of Drosophila melanogaster. Genetics 151, 1517-1529 (1999).
    • (1999) Genetics , vol.151 , pp. 1517-1529
    • Burnette, J.M.1    Hatton, A.R.2    Lopez, A.J.3
  • 29
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • Black, D.L. Mechanisms of alternative pre-messenger RNA splicing. Annu. Rev. Biochem. 72, 291-336 (2003).
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 291-336
    • Black, D.L.1
  • 30
  • 31
    • 0027176790 scopus 로고
    • Initial organization of the Drosophila dorsoventral axis depends on an RNA-binding protein encoded by the squid gene
    • Kelley, R.L. Initial organization of the Drosophila dorsoventral axis depends on an RNA-binding protein encoded by the squid gene. Genes Dev. 7, 948-960 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 948-960
    • Kelley, R.L.1
  • 32
    • 0033597716 scopus 로고    scopus 로고
    • Squid hnRNP protein promotes apical cytoplasmic transport and localization of Drosophila pair-rule transcripts
    • Lall, S. et al. Squid hnRNP protein promotes apical cytoplasmic transport and localization of Drosophila pair-rule transcripts. Cell 98, 171-180 (1999).
    • (1999) Cell , vol.98 , pp. 171-180
    • Lall, S.1
  • 33
    • 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 119, 641-651 (2004).
    • (2004) Cell , vol.119 , pp. 641-651
    • Barnard, D.C.1    Ryan, K.2    Manley, J.L.3    Richter, J.D.4
  • 34
    • 0029743063 scopus 로고    scopus 로고
    • Targeting and function in mRNA export of nuclear pore complex protein Nup153
    • Bastos, R., Lin, A., Enarson, M. & Burke, B. Targeting and function in mRNA export of nuclear pore complex protein Nup153. J. Cell Biol. 134, 1141-1156 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 1141-1156
    • Bastos, R.1    Lin, A.2    Enarson, M.3    Burke, B.4
  • 35
    • 0031046477 scopus 로고    scopus 로고
    • The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways
    • Powers, M.A., Forbes, D.J., Dahlberg, J.E. & Lund, E. The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. J. Cell Biol. 136, 241-250 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 241-250
    • Powers, M.A.1    Forbes, D.J.2    Dahlberg, J.E.3    Lund, E.4
  • 36
    • 0032963082 scopus 로고    scopus 로고
    • The nucleoporin nup153 plays a critical role in multiple types of nuclear export
    • Ullman, K.S., Shah, S., Powers, M.A. & Forbes, D.J. The nucleoporin nup153 plays a critical role in multiple types of nuclear export. Mol. Biol. Cell 10, 649-664 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 649-664
    • Ullman, K.S.1    Shah, S.2    Powers, M.A.3    Forbes, D.J.4
  • 37
    • 0029961659 scopus 로고    scopus 로고
    • Phosphorylation of the fused protein kinase in response to signaling from hedgehog
    • Therond, P.P., Knight, J.D., Kornberg, T.B. & Bishop, J.M. Phosphorylation of the fused protein kinase in response to signaling from hedgehog. Proc. Natl. Acad. Sci. USA 93, 4224-4228 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4224-4228
    • Therond, P.P.1    Knight, J.D.2    Kornberg, T.B.3    Bishop, J.M.4
  • 38
    • 0030838880 scopus 로고    scopus 로고
    • Hedgehog elicits signal transduction by means of a large complex containing the kinesin-related protein costal2
    • Robbins, D.J. et al. Hedgehog elicits signal transduction by means of a large complex containing the kinesin-related protein costal2. Cell 90, 225-234 (1997).
    • (1997) Cell , vol.90 , pp. 225-234
    • Robbins, D.J.1
  • 39
    • 0033404607 scopus 로고    scopus 로고
    • The subcellular localization and activity of Drosophila cubitus interruptus are regulated at multiple levels
    • Wang, Q.T. & Holmgren, R.A. The subcellular localization and activity of Drosophila cubitus interruptus are regulated at multiple levels. Development 126, 5097-5106 (1999).
    • (1999) Development , vol.126 , pp. 5097-5106
    • Wang, Q.T.1    Holmgren, R.A.2
  • 40
    • 0037025382 scopus 로고    scopus 로고
    • Hedgehog-stimulated phosphorylation of the kinesin-related protein Costal2 is mediated by the serine/threonine kinase fused
    • Nybakken, K.E., Turck, C.W., Robbins, D.J. & Bishop, J.M. Hedgehog-stimulated phosphorylation of the kinesin-related protein Costal2 is mediated by the serine/threonine kinase fused. J. Biol. Chem. 277, 24638-24647 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 24638-24647
    • Nybakken, K.E.1    Turck, C.W.2    Robbins, D.J.3    Bishop, J.M.4
  • 41
    • 0037155737 scopus 로고    scopus 로고
    • Proteolysis of the Hedgehog signaling effector Cubitus interruptus requires phosphorylation by Glycogen Synthase Kinase 3 and Casein Kinase 1
    • Price, M.A. & Kalderon, D. Proteolysis of the Hedgehog signaling effector Cubitus interruptus requires phosphorylation by Glycogen Synthase Kinase 3 and Casein Kinase 1. Cell 108, 823-835 (2002).
    • (2002) Cell , vol.108 , pp. 823-835
    • Price, M.A.1    Kalderon, D.2
  • 42
    • 0034682719 scopus 로고    scopus 로고
    • Hedgehog induces opposite changes in turnover and subcellular localization of patched and smoothened
    • Denef, N., Neubuser, D., Perez, L. & Cohen, S.M. Hedgehog induces opposite changes in turnover and subcellular localization of patched and smoothened. Cell 102, 521-531 (2000).
    • (2000) Cell , vol.102 , pp. 521-531
    • Denef, N.1    Neubuser, D.2    Perez, L.3    Cohen, S.M.4
  • 43
    • 0037041470 scopus 로고    scopus 로고
    • Shaggy/GSK3 antagonizes Hedgehog signalling by regulating Cubitus interruptus
    • Jia, J. et al. Shaggy/GSK3 antagonizes Hedgehog signalling by regulating Cubitus interruptus. Nature 416, 548-552 (2002).
    • (2002) Nature , vol.416 , pp. 548-552
    • Jia, J.1
  • 44
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens, V. & Goris, J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353, 417-439 (2001).
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 45
    • 0034235860 scopus 로고    scopus 로고
    • Polyhomeotic controls engrailed expression and the hedgehog signaling pathway in imaginal discs
    • Randsholt, N.B., Maschat, F. & Santamaria, P. Polyhomeotic controls engrailed expression and the hedgehog signaling pathway in imaginal discs. Mech. Dev. 95, 89-99 (2000).
    • (2000) Mech. Dev. , vol.95 , pp. 89-99
    • Randsholt, N.B.1    Maschat, F.2    Santamaria, P.3
  • 46
    • 20444431256 scopus 로고    scopus 로고
    • A genetic screen in Drosophila for identifying novel components of the hedgehog signaling pathway
    • Collins, R.T. & Cohen, S.M. A genetic screen in Drosophila for identifying novel components of the hedgehog signaling pathway. Genetics 170, 173-184 (2005).
    • (2005) Genetics , vol.170 , pp. 173-184
    • Collins, R.T.1    Cohen, S.M.2
  • 47
    • 0022727711 scopus 로고
    • The Drosophila melanogaster actin 5C gene uses two transcription initiation sites and three polyadenylation sites to express multiple mRNA species
    • Bond, B.J. & Davidson, N. The Drosophila melanogaster actin 5C gene uses two transcription initiation sites and three polyadenylation sites to express multiple mRNA species. Mol. Cell. Biol. 6, 2080-2088 (1986).
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2080-2088
    • Bond, B.J.1    Davidson, N.2
  • 48
    • 0035836505 scopus 로고    scopus 로고
    • Enhanced potency of human Sonic hedgehog by hydrophobic modification
    • Taylor, F.R. et al. Enhanced potency of human Sonic hedgehog by hydrophobic modification. Biochemistry 40, 4359-4371 (2001).
    • (2001) Biochemistry , vol.40 , pp. 4359-4371
    • Taylor, F.R.1
  • 49
    • 0036173545 scopus 로고    scopus 로고
    • The carboxyl-terminal domain of the protein kinase fused can function as a dominant inhibitor of hedgehog signaling
    • Ascano, M. Jr., Nybakken, K.E., Sosinski, J., Stegman, M.A. & Robbins, D.J. The carboxyl-terminal domain of the protein kinase fused can function as a dominant inhibitor of hedgehog signaling. Mol. Cell. Biol. 22, 1555-1566 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1555-1566
    • Ascano Jr., M.1    Nybakken, K.E.2    Sosinski, J.3    Stegman, M.A.4    Robbins, D.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.