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Volumn 2, Issue , 2002, Pages 1-9

Hedgehog signal transduction proteins: Contacts of the Fused kinase and Citranscription factor with the kinesin-related protein Costal2

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE INHIBITOR; PROTEIN COSTAL2; PROTEIN FUSED; PROTEIN SERINE THREONINE KINASE; SONIC HEDGEHOG PROTEIN; SUPPRESSOR OF FUSED PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR CUBITUS INTERRUPTUS; UNCLASSIFIED DRUG;

EID: 0013014880     PISSN: 1471213X     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-213X-2-4     Document Type: Article
Times cited : (52)

References (54)
  • 1
    • 0032126734 scopus 로고    scopus 로고
    • Transducing Hedgehog: The story so far
    • Ingham PW: Transducing Hedgehog: the story so far. Embo J 1998, 17:3505-3511
    • (1998) Embo J , vol.17 , pp. 3505-3511
    • Ingham, P.W.1
  • 2
    • 0031663608 scopus 로고    scopus 로고
    • New players and puzzles in the Hedgehog signaling pathway
    • Johnson RL, Scott MP: New players and puzzles in the Hedgehog signaling pathway. Curr Opin Genet Dev 1998, 8:450-456
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 450-456
    • Johnson, R.L.1    Scott, M.P.2
  • 4
    • 0033710347 scopus 로고    scopus 로고
    • Hedgehog signaling in vertebrate and invertebrate limb patterning
    • Capdevila J, Johnson RL: Hedgehog signaling in vertebrate and invertebrate limb patterning. Cell Mol Life Sci 2000, 57:1682-1694
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1682-1694
    • Capdevila, J.1    Johnson, R.L.2
  • 5
    • 0033590110 scopus 로고    scopus 로고
    • The hedgehog signalling pathway in tumorigenesis and development
    • Wicking C, Smyth I, Bale A: The hedgehog signalling pathway in tumorigenesis and development. Oncogene 1999, 18:7844-7851
    • (1999) Oncogene , vol.18 , pp. 7844-7851
    • Wicking, C.1    Smyth, I.2    Bale, A.3
  • 6
    • 0035902140 scopus 로고    scopus 로고
    • The Hedgehog and Wnt signalling pathways in cancer
    • Taipale J, Beachy PA: The Hedgehog and Wnt signalling pathways in cancer. Nature 2001, 411:349-354
    • (2001) Nature , vol.411 , pp. 349-354
    • Taipale, J.1    Beachy, P.A.2
  • 7
    • 0033711384 scopus 로고    scopus 로고
    • Hedgehog signalling in cancer
    • Toftgard R: Hedgehog signalling in cancer. Cell Mol Life Sci 2000, 57:1720-1731
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1720-1731
    • Toftgard, R.1
  • 8
    • 0033230757 scopus 로고    scopus 로고
    • Ci: A complex transducer of the hedgehog signal
    • Aza BP, Kornberg TB: Ci: a complex transducer of the hedgehog signal. Trends Genet 1999, 15:458-462
    • (1999) Trends Genet , vol.15 , pp. 458-462
    • Aza, B.P.1    Kornberg, T.B.2
  • 9
    • 0034721665 scopus 로고    scopus 로고
    • Transducing the hedgehog signal
    • Kalderon D: Transducing the hedgehog signal. Cell 2000, 103:371-374
    • (2000) Cell , vol.103 , pp. 371-374
    • Kalderon, D.1
  • 10
    • 0031587830 scopus 로고    scopus 로고
    • Proteolysis that is inhibited by hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor
    • Aza BP, Ramirez WF, Laget MP, Schwartz C, Kornberg TB: Proteolysis that is inhibited by hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor. Cell 1997, 89:1043-1053
    • (1997) Cell , vol.89 , pp. 1043-1053
    • Aza, B.P.1    Ramirez, W.F.2    Laget, M.P.3    Schwartz, C.4    Kornberg, T.B.5
  • 11
    • 0033582908 scopus 로고    scopus 로고
    • Hedgehog controls limb development by regulating the activities of distinct transcriptional activator and repressor forms of Cubitus interruptus
    • Methot N, Basler K: Hedgehog controls limb development by regulating the activities of distinct transcriptional activator and repressor forms of Cubitus interruptus. Cell 1999, 96:819-831
    • (1999) Cell , vol.96 , pp. 819-831
    • Methot, N.1    Basler, K.2
  • 12
    • 0343431516 scopus 로고    scopus 로고
    • The repressor and activator forms of Cubitus interruptus control Hedgehog target genes through common generic gli-binding sites
    • Muller B, Basler K: The repressor and activator forms of Cubitus interruptus control Hedgehog target genes through common generic gli-binding sites. Development 2000, 127:2999-3007
    • (2000) Development , vol.127 , pp. 2999-3007
    • Muller, B.1    Basler, K.2
  • 13
    • 0032478107 scopus 로고    scopus 로고
    • Protein kinase A directly regulates the activity and proteolysis of cubitus interruptus
    • Chen Y, Gallaher N, Goodman RH, Smolik SM: Protein kinase A directly regulates the activity and proteolysis of cubitus interruptus. Proc Natl Acad Sci USA 1998, 95:2349-2354
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2349-2354
    • Chen, Y.1    Gallaher, N.2    Goodman, R.H.3    Smolik, S.M.4
  • 14
    • 0033529667 scopus 로고    scopus 로고
    • Nuclear trafficking of Cubitus interruptus in the transcriptional regulation of Hedgehog target gene expression
    • Chen CH, von KD, Park W, Wang B, Ma Y, Beachy PA: Nuclear trafficking of Cubitus interruptus in the transcriptional regulation of Hedgehog target gene expression. Cell 1999, 98:305-316
    • (1999) Cell , vol.98 , pp. 305-316
    • Chen, C.H.1    Von, K.D.2    Park, W.3    Wang, B.4    Ma, Y.5    Beachy, P.A.6
  • 15
    • 0032873774 scopus 로고    scopus 로고
    • Mutants of cubitus interruptus that are independent of PKA regulation are independent of hedgehog signaling
    • Chen Y, Cardinaux JR, Goodman RH, Smolik SM: Mutants of cubitus interruptus that are independent of PKA regulation are independent of hedgehog signaling. Development 1999, 126:3607-3616
    • (1999) Development , vol.126 , pp. 3607-3616
    • Chen, Y.1    Cardinaux, J.R.2    Goodman, R.H.3    Smolik, S.M.4
  • 16
    • 0032756914 scopus 로고    scopus 로고
    • Proteolysis of cubitus interruptus in Drosophila requires phosphorylation by protein kinase
    • Price MA, Kalderon D: Proteolysis of cubitus interruptus in Drosophila requires phosphorylation by protein kinase Development 1999, 126:4331-4339
    • (1999) Development , vol.126 , pp. 4331-4339
    • Price, M.A.1    Kalderon, D.2
  • 17
    • 0032728958 scopus 로고    scopus 로고
    • Protein kinase A antagonizes Hedgehog signaling by regulating both the activator and repressor forms of Cubitus interruptus
    • Wang G, Wang B, Jiang J: Protein kinase A antagonizes Hedgehog signaling by regulating both the activator and repressor forms of Cubitus interruptus. Genes Dev 1999, 13:2828-2837
    • (1999) Genes Dev , vol.13 , pp. 2828-2837
    • Wang, G.1    Wang, B.2    Jiang, J.3
  • 18
    • 0033404607 scopus 로고    scopus 로고
    • The subcellular localization and activity of Drosophila cubitus interruptus are regulated at multiple levels
    • Wang QT, Holmgren RA: The subcellular localization and activity of Drosophila cubitus interruptus are regulated at multiple levels. Development 1999, 126:5097-5106
    • (1999) Development , vol.126 , pp. 5097-5106
    • Wang, Q.T.1    Holmgren, R.A.2
  • 19
    • 0033789068 scopus 로고    scopus 로고
    • Suppressor of fused opposes hedgehog signal transduction by impeding nuclear accumulation of the activator form of Cubitus interruptus
    • Methot N, Basler K: Suppressor of fused opposes hedgehog signal transduction by impeding nuclear accumulation of the activator form of Cubitus interruptus. Development 2000, 127:4001-4010
    • (2000) Development , vol.127 , pp. 4001-4010
    • Methot, N.1    Basler, K.2
  • 20
    • 0028918468 scopus 로고
    • Protein kinase A and hedgehog signaling in Drosophila limb development
    • Jiang J, Struhl G: Protein kinase A and hedgehog signaling in Drosophila limb development. Cell 1995, 80:563-572
    • (1995) Cell , vol.80 , pp. 563-572
    • Jiang, J.1    Struhl, G.2
  • 21
    • 0034917610 scopus 로고    scopus 로고
    • Genetic evidence for a protein kinase a/cubitus interruptus complex that facilitates processing of cubitus interruptus in drosophila
    • Kiger JJ, O'Shea C: Genetic evidence for a protein kinase a/cubitus interruptus complex that facilitates processing of cubitus interruptus in drosophila. Genetics 2000, 158:1157-1166
    • (2000) Genetics , vol.158 , pp. 1157-1166
    • Kiger, J.J.1    O'Shea, C.2
  • 23
    • 0034669178 scopus 로고    scopus 로고
    • Interactions with Costal2 and suppressor of fused regulate nuclear translocation and activity of cubitus interruptus
    • Wang G, Amanai K, Wang B, Jiang J: Interactions with Costal2 and suppressor of fused regulate nuclear translocation and activity of cubitus interruptus. Genes Dev 2000, 14:2893-2905
    • (2000) Genes Dev , vol.14 , pp. 2893-2905
    • Wang, G.1    Amanai, K.2    Wang, B.3    Jiang, J.4
  • 24
    • 0033859849 scopus 로고    scopus 로고
    • Nuclear import of cubitus interruptus is regulated by hedgehog via a mechanism distinct from Ci stabilization and Ci activation
    • Wang QT, Holmgren RA: Nuclear import of cubitus interruptus is regulated by hedgehog via a mechanism distinct from Ci stabilization and Ci activation. Development 2000, 127:3131-3139
    • (2000) Development , vol.127 , pp. 3131-3139
    • Wang, Q.T.1    Holmgren, R.A.2
  • 25
    • 0035881953 scopus 로고    scopus 로고
    • Genetic dissection of the Drosophila Cubitus interruptus signaling complex
    • Lefers MA, Wang QT, Holmgren RA: Genetic dissection of the Drosophila Cubitus interruptus signaling complex. Dev Bid 2001, 236:411-420
    • (2001) Dev Bid , vol.236 , pp. 411-420
    • Lefers, M.A.1    Wang, Q.T.2    Holmgren, R.A.3
  • 26
    • 0031647941 scopus 로고    scopus 로고
    • Modulation of Hedgehog target gene expression by the Fused serine-threonine kinase in wing imaginal discs
    • Alves G, Limbourg BB, Tricoire H, Brissard ZJ, Lamour IC, Busson D: Modulation of Hedgehog target gene expression by the Fused serine-threonine kinase in wing imaginal discs. Mech Dev 1998, 78:17-31
    • (1998) Mech Dev , vol.78 , pp. 17-31
    • Alves, G.1    Limbourg, B.B.2    Tricoire, H.3    Brissard, Z.J.4    Lamour, I.C.5    Busson, D.6
  • 27
    • 0032585515 scopus 로고    scopus 로고
    • Hedgehog stimulates maturation of Cubitus interruptus into a labile transcriptional activator
    • Ohlmeyer JT, Kalderon D: Hedgehog stimulates maturation of Cubitus interruptus into a labile transcriptional activator. Nature 1998, 396:749-753
    • (1998) Nature , vol.396 , pp. 749-753
    • Ohlmeyer, J.T.1    Kalderon, D.2
  • 28
    • 0030838880 scopus 로고    scopus 로고
    • Hedgehog elicits signal transduction by means of a large complex containing the kinesin-related protein costal2
    • Robbins DJ, Nybakken KE, Kobayashi R, Sisson JC, Bishop JM, Therond PP: Hedgehog elicits signal transduction by means of a large complex containing the kinesin-related protein costal2. Cell 1997, 90:225-234
    • (1997) Cell , vol.90 , pp. 225-234
    • Robbins, D.J.1    Nybakken, K.E.2    Kobayashi, R.3    Sisson, J.C.4    Bishop, J.M.5    Therond, P.P.6
  • 29
    • 0030754171 scopus 로고    scopus 로고
    • Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway
    • Sisson JC, Ho KS, Suyama K, Scott MP: Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway. Cell 1997, 90:235-245
    • (1997) Cell , vol.90 , pp. 235-245
    • Sisson, J.C.1    Ho, K.S.2    Suyama, K.3    Scott, M.P.4
  • 31
    • 0032492995 scopus 로고    scopus 로고
    • Suppressor of fused links fused and Cubitus interruptus on the hedgehog signalling pathway
    • Monnier V, Dussillol F, Alves G, Lamour IC, Plessis A: Suppressor of fused links fused and Cubitus interruptus on the hedgehog signalling pathway. Curr Biol 1998, 8:583-586
    • (1998) Curr Biol , vol.8 , pp. 583-586
    • Monnier, V.1    Dussillol, F.2    Alves, G.3    Lamour, I.C.4    Plessis, A.5
  • 32
    • 0029961659 scopus 로고    scopus 로고
    • Phosphorylation of the fused protein kinase in response to signaling from hedgehog
    • Thérond PP, Knight JD, Kornberg TB, Bishop JM: Phosphorylation of the fused protein kinase in response to signaling from hedgehog. Proc. Natl. Acad. Sci. 1996, 93:4224-4228
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 4224-4228
    • Thérond, P.P.1    Knight, J.D.2    Kornberg, T.B.3    Bishop, J.M.4
  • 33
    • 0026680723 scopus 로고
    • Fused protein domains inhibit DNA binding by LexA
    • Golemis EA, Brent R: Fused protein domains inhibit DNA binding by LexA. Mol Cell Biol 1992, 12:3006-3014
    • (1992) Mol Cell Biol , vol.12 , pp. 3006-3014
    • Golemis, E.A.1    Brent, R.2
  • 34
    • 0032559690 scopus 로고    scopus 로고
    • Leading the procession: New insights into kinesin motors
    • Block SM: Leading the procession: new insights into kinesin motors. J Cell Biol 1998, 140:1281-1284
    • (1998) J Cell Biol , vol.140 , pp. 1281-1284
    • Block, S.M.1
  • 35
    • 0034628619 scopus 로고    scopus 로고
    • Role of the kinesin neck linker and catalytic core in microtubule-based motility
    • Case RB, Rice S, Hart CL, Ly B, Vale RD: Role of the kinesin neck linker and catalytic core in microtubule-based motility. Curr Biol 2000, 10:157-160
    • (2000) Curr Biol , vol.10 , pp. 157-160
    • Case, R.B.1    Rice, S.2    Hart, C.L.3    Ly, B.4    Vale, R.D.5
  • 36
    • 0032555532 scopus 로고    scopus 로고
    • Determinants of kinesin motor polarity
    • Endow SA, Waligora KW: Determinants of kinesin motor polarity. Science 1998, 281:1200-1202
    • (1998) Science , vol.281 , pp. 1200-1202
    • Endow, S.A.1    Waligora, K.W.2
  • 37
    • 0001089368 scopus 로고    scopus 로고
    • Determinants of molecular motor directionality
    • Endow SA: Determinants of molecular motor directionality. Nat Cell Biol 1999, 1:E163-167
    • (1999) Nat Cell Biol , vol.1
    • Endow, S.A.1
  • 38
    • 0034710696 scopus 로고    scopus 로고
    • A mutant of the motor protein kinesin that moves in both directions on microtubules
    • Endow SA, Higuchi H: A mutant of the motor protein kinesin that moves in both directions on microtubules. Nature 2000, 406:A913-916
    • (2000) Nature , vol.406
    • Endow, S.A.1    Higuchi, H.2
  • 39
    • 0032189949 scopus 로고    scopus 로고
    • Importance of a flexible hinge near the motor domain in kinesin-driven motility
    • Grummt M, Woehlke G, Henningsen U, Fuchs S, Schleicher M, Schliwa M: Importance of a flexible hinge near the motor domain in kinesin-driven motility. Embo J 1998, 17:5536-5542
    • (1998) Embo J , vol.17 , pp. 5536-5542
    • Grummt, M.1    Woehlke, G.2    Henningsen, U.3    Fuchs, S.4    Schleicher, M.5    Schliwa, M.6
  • 41
    • 0032559824 scopus 로고    scopus 로고
    • Role of the kinesin neck region in processive microtubule-based motility
    • Romberg L, Pierce DW, Vale RD: Role of the kinesin neck region in processive microtubule-based motility. J Cell Biol 1998, 140:1407-1416
    • (1998) J Cell Biol , vol.140 , pp. 1407-1416
    • Romberg, L.1    Pierce, D.W.2    Vale, R.D.3
  • 44
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale RD, Milligan RA: The way things move: looking under the hood of molecular motor proteins. Science 2000, 288:88-95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 45
    • 0030874883 scopus 로고    scopus 로고
    • The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
    • Case RB, Pierce DW, Hom BN, Hart CL, Vale RD: The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain. Cell 1997, 90:959-966
    • (1997) Cell , vol.90 , pp. 959-966
    • Case, R.B.1    Pierce, D.W.2    Hom, B.N.3    Hart, C.L.4    Vale, R.D.5
  • 46
    • 0027817446 scopus 로고
    • Genetic analysis of hedgehog signalling in the Drosophila embryo
    • Forbes AJ, Nakano Y, Taylor AM, Ingham PW: Genetic analysis of hedgehog signalling in the Drosophila embryo. Dev. Suppl. 1993, 115-124
    • (1993) Dev Suppl , pp. 115-124
    • Forbes, A.J.1    Nakano, Y.2    Taylor, A.M.3    Ingham, P.W.4
  • 47
    • 0027383291 scopus 로고
    • Segmental polarity in Drosophila melanogaster: Genetic dissection of fused in a Suppressor of fused background reveals interaction with costal-2
    • Preat T, Therond P, Limbourg BB, Pham A, Tricoire H, Busson D, Lamour IC: Segmental polarity in Drosophila melanogaster: genetic dissection of fused in a Suppressor of fused background reveals interaction with costal-2. Genetics 1993, 135:1047-1062
    • (1993) Genetics , vol.135 , pp. 1047-1062
    • Preat, T.1    Therond, P.2    Limbourg, B.B.3    Pham, A.4    Tricoire, H.5    Busson, D.6    Lamour, I.C.7
  • 48
    • 0030020940 scopus 로고    scopus 로고
    • Microtubules and microtubule motors: Mechanisms of regulation
    • Thaler CD, Haimo LT: Microtubules and microtubule motors: mechanisms of regulation. Int Rev Cytol 1996, 164:269-327
    • (1996) Int Rev Cytol , vol.164 , pp. 269-327
    • Thaler, C.D.1    Haimo, L.T.2
  • 49
    • 0030612145 scopus 로고    scopus 로고
    • Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150
    • Blangy A, Arnaud L, Nigg EA: Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150. J Biol Chem 1997, 272:19418-19424
    • (1997) J Biol Chem , vol.272 , pp. 19418-19424
    • Blangy, A.1    Arnaud, L.2    Nigg, E.A.3
  • 51
    • 0028568056 scopus 로고
    • Interaction mating reveals binary and ternary connections between Drosophila cell cycle regulators
    • Finley RLJ, Brent R: Interaction mating reveals binary and ternary connections between Drosophila cell cycle regulators. Proc Natl Acad Sci 1994, 91:12980-12984
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 12980-12984
    • Finley, R.L.J.1    Brent, R.2
  • 52
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with in vitro measurements
    • Estojak J, Brent R, Golemis EA: Correlation of two-hybrid affinity data with in vitro measurements. Mol Cell Biol 1995, 15:5820-5829
    • (1995) Mol Cell Biol , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 53
    • 0030018262 scopus 로고    scopus 로고
    • Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II
    • Johannes L, Perez F, Laran CM, Henry JP, Darchen F: Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II. Eur J Biochem 1996, 239:362-368
    • (1996) Eur J Biochem , vol.239 , pp. 362-368
    • Johannes, L.1    Perez, F.2    Laran, C.M.3    Henry, J.P.4    Darchen, F.5
  • 54
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont RM, Rain JC, Legrain P: Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat Genet 1997, 16:277-282
    • (1997) Nat Genet , vol.16 , pp. 277-282
    • Fromont, R.M.1    Rain, J.C.2    Legrain, P.3


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