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Volumn 7, Issue 332, 2014, Pages

Hedgehog induces formation of PKA-smoothened complexes to promote smoothened phosphorylation and pathway activation

Author keywords

[No Author keywords available]

Indexed keywords

COSTAL2 PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; DOUBLE STRANDED RNA; PROTEIN; SMOOTHENED PROTEIN; SONIC HEDGEHOG PROTEIN; UNCLASSIFIED DRUG; CI PROTEIN, DROSOPHILA; DNA BINDING PROTEIN; DROSOPHILA PROTEIN; G PROTEIN COUPLED RECEPTOR; HEDGEHOG PROTEIN, DROSOPHILA; SMOOTHENED PROTEIN, DROSOPHILA; TRANSCRIPTION FACTOR;

EID: 84903779617     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2005414     Document Type: Article
Times cited : (39)

References (87)
  • 1
    • 57049089995 scopus 로고    scopus 로고
    • Hedgehog signaling in development and cancer
    • J. Jiang, C. C. Hui, Hedgehog signaling in development and cancer. Dev. Cell 15, 801-812 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 801-812
    • Jiang, J.1    Hui, C.C.2
  • 2
    • 79956308325 scopus 로고    scopus 로고
    • Mechanisms and functions of Hedgehog signalling across the metazoa
    • P. W. Ingham, Y. Nakano, C. Seger, Mechanisms and functions of Hedgehog signalling across the metazoa. Nat. Rev. Genet. 12, 393-406 (2011).
    • (2011) Nat. Rev. Genet. , vol.12 , pp. 393-406
    • Ingham, P.W.1    Nakano, Y.2    Seger, C.3
  • 3
    • 0035902140 scopus 로고    scopus 로고
    • The Hedgehog and Wnt signalling pathways in cancer
    • J. Taipale, P. A. Beachy, The Hedgehog and Wnt signalling pathways in cancer. Nature 411, 349-354 (2001).
    • (2001) Nature , vol.411 , pp. 349-354
    • Taipale, J.1    Beachy, P.A.2
  • 4
    • 84879414522 scopus 로고    scopus 로고
    • The mechanisms of Hedgehog signalling and its roles in development and disease
    • J. Briscoe, P. P. Thérond, The mechanisms of Hedgehog signalling and its roles in development and disease. Nat. Rev. Mol. Cell Biol. 14, 416-429 (2013).
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 416-429
    • Briscoe, J.1    Thérond, P.P.2
  • 5
    • 77953316514 scopus 로고    scopus 로고
    • Mechanism and evolution of cytosolic Hedgehog signal transduction
    • C. W. Wilson, P. T. Chuang, Mechanism and evolution of cytosolic Hedgehog signal transduction. Development 137, 2079-2094 (2010).
    • (2010) Development , vol.137 , pp. 2079-2094
    • Wilson, C.W.1    Chuang, P.T.2
  • 7
    • 0026201001 scopus 로고
    • Segment polarity genes and cell patterning within the Drosophila body segment
    • P. W. Ingham, Segment polarity genes and cell patterning within the Drosophila body segment. Curr. Opin. Genet. Dev. 1, 261-267 (1991).
    • (1991) Curr. Opin. Genet. Dev. , vol.1 , pp. 261-267
    • Ingham, P.W.1
  • 8
    • 0037158748 scopus 로고    scopus 로고
    • Patched acts catalytically to suppress the activity of Smoothened
    • J. Taipale, M. K. Cooper, T. Maiti, P. A. Beachy, Patched acts catalytically to suppress the activity of Smoothened. Nature 418, 892-897 (2002).
    • (2002) Nature , vol.418 , pp. 892-897
    • Taipale, J.1    Cooper, M.K.2    Maiti, T.3    Beachy, P.A.4
  • 10
    • 4544331178 scopus 로고    scopus 로고
    • Reading the Hedgehog morphogen gradient by measuring the ratio of bound to unbound Patched protein
    • A. Casali, G. Struhl, Reading the Hedgehog morphogen gradient by measuring the ratio of bound to unbound Patched protein. Nature 431, 76-80 (2004).
    • (2004) Nature , vol.431 , pp. 76-80
    • Casali, A.1    Struhl, G.2
  • 11
    • 84873735792 scopus 로고    scopus 로고
    • Decoding the phosphorylation code in Hedgehog signal transduction
    • Y. Chen, J. Jiang, Decoding the phosphorylation code in Hedgehog signal transduction. Cell Res. 23, 186-200 (2013).
    • (2013) Cell Res. , vol.23 , pp. 186-200
    • Chen, Y.1    Jiang, J.2
  • 12
    • 0034682719 scopus 로고    scopus 로고
    • Hedgehog induces opposite changes in turnover and subcellular localization of patched and smoothened
    • N. Denef, D. Neubüser, L. Perez, S. M. Cohen, 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    Neubüser, D.2    Perez, L.3    Cohen, S.M.4
  • 13
    • 11144237279 scopus 로고    scopus 로고
    • Hedgehog signalling activity of Smoothened requires phosphorylation by protein kinase A and casein kinase I
    • J. Jia, C. Tong, B. Wang, L. Luo, J. Jiang, Hedgehog signalling activity of Smoothened requires phosphorylation by protein kinase A and casein kinase I. Nature 432, 1045-1050 (2004).
    • (2004) Nature , vol.432 , pp. 1045-1050
    • Jia, J.1    Tong, C.2    Wang, B.3    Luo, L.4    Jiang, J.5
  • 15
    • 36049033946 scopus 로고    scopus 로고
    • Hedgehog regulates smoothened activity by inducing a conformational switch
    • Y. Zhao, C. Tong, J. Jiang, Hedgehog regulates smoothened activity by inducing a conformational switch. Nature 450, 252-258 (2007).
    • (2007) Nature , vol.450 , pp. 252-258
    • Zhao, Y.1    Tong, C.2    Jiang, J.3
  • 16
    • 79959804711 scopus 로고    scopus 로고
    • Sonic Hedgehog dependent phosphorylation by CK1a and GRK2 is required for ciliary accumulation and activation of smoothened
    • Y. Chen, N. Sasai, G. Ma, T. Yue, J. Jia, J. Briscoe, J. Jiang, Sonic Hedgehog dependent phosphorylation by CK1a and GRK2 is required for ciliary accumulation and activation of smoothened. PLOS Biol. 9, e1001083 (2011).
    • (2011) PLOS Biol. , vol.9
    • Chen, Y.1    Sasai, N.2    Ma, G.3    Yue, T.4    Jia, J.5    Briscoe, J.6    Jiang, J.7
  • 17
    • 80054022786 scopus 로고    scopus 로고
    • Gli proteins in development and disease
    • C. C. Hui, S. Angers, Gli proteins in development and disease. Annu. Rev. Cell Dev. Biol. 27, 513-537 (2011).
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 513-537
    • Hui, C.C.1    Angers, S.2
  • 18
    • 0028918468 scopus 로고
    • Protein kinase A and hedgehog signaling in drosophila limb development
    • J. Jiang, G. Struhl, Protein kinase A and hedgehog signaling in drosophila limb development. Cell 80, 563-572 (1995).
    • (1995) Cell , vol.80 , pp. 563-572
    • Jiang, J.1    Struhl, G.2
  • 19
    • 0028897883 scopus 로고
    • Function of protein kinase A in hedgehog signal transduction and Drosophila imaginal disc development
    • W. Li, J. T. Ohlmeyer, M. E. Lane, D. Kalderon, Function of protein kinase A in hedgehog signal transduction and Drosophila imaginal disc development. Cell 80, 553-562 (1995).
    • (1995) Cell , vol.80 , pp. 553-562
    • Li, W.1    Ohlmeyer, J.T.2    Lane, M.E.3    Kalderon, D.4
  • 20
    • 0028911915 scopus 로고
    • cAMP-dependent protein kinase and hedgehog act antagonistically in regulating decapentaplegic transcription in drosophila imaginal discs
    • D. Pan, G. M. Rubin, cAMP-dependent protein kinase and hedgehog act antagonistically in regulating decapentaplegic transcription in drosophila imaginal discs. Cell 80, 543-552 (1995).
    • (1995) Cell , vol.80 , pp. 543-552
    • Pan, D.1    Rubin, G.M.2
  • 21
    • 80054949733 scopus 로고    scopus 로고
    • Protein kinase A acts at the basal body of the primary cilium to prevent Gli2 activation and ventralization of the mouse neural tube
    • M. Tuson, M. He, K. V. Anderson, Protein kinase A acts at the basal body of the primary cilium to prevent Gli2 activation and ventralization of the mouse neural tube. Development 138, 4921 -4930 (2011).
    • (2011) Development , vol.138 , pp. 4921-4930
    • Tuson, M.1    He, M.2    Anderson, K.V.3
  • 22
    • 0032576777 scopus 로고    scopus 로고
    • Regulation of the Hedgehog and Wingless signalling pathways by the F- box/WD40-repeat protein Slimb
    • J. Jiang, G. Struhl, 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
  • 23
    • 0037041470 scopus 로고    scopus 로고
    • Shaggy/GSK3 antagonizes Hedgehog signalling by regulating Cubitus interruptus
    • J. Jia, K. Amanai, G. Wang, J. Tang, B. Wang, J. Jiang, Shaggy/GSK3 antagonizes Hedgehog signalling by regulating Cubitus interruptus. Nature 416, 548-552 (2002).
    • (2002) Nature , vol.416 , pp. 548-552
    • Jia, J.1    Amanai, K.2    Wang, G.3    Tang, J.4    Wang, B.5    Jiang, J.6
  • 24
    • 28444449828 scopus 로고    scopus 로고
    • Phosphorylation by double-time/CKIε and CKIα targets Cubitus interruptus for Slimb/β-TRCPmediated proteolytic processing
    • J. Jia, L. Zhang, Q. Zhang, C. Tong, B. Wang, F. Hou, K. Amanai, J. Jiang, Phosphorylation by double-time/CKIε and CKIα targets Cubitus interruptus for Slimb/β-TRCPmediated proteolytic processing. Dev. Cell 9, 819-830 (2005).
    • (2005) Dev. Cell , vol.9 , pp. 819-830
    • Jia, J.1    Zhang, L.2    Zhang, Q.3    Tong, C.4    Wang, B.5    Hou, F.6    Amanai, K.7    Jiang, J.8
  • 25
    • 0037155737 scopus 로고    scopus 로고
    • Proteolysis of the Hedgehog signaling effector Cubitus interruptus requires phosphorylation by glycogen synthase kinase 3 and casein kinase 1
    • M. A. Price, D. Kalderon, 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
  • 26
    • 34848892735 scopus 로고    scopus 로고
    • Slimb binding, Ci proteolysis, and Hedgehog pathway activity by Ci phosphorylation
    • Slimb binding, Ci proteolysis, and Hedgehog pathway activity by Ci phosphorylation. Dev. Cell 13, 481-495 (2007).
    • (2007) Dev. Cell , vol.13 , pp. 481-495
    • Smelkinson, M.G.1    Zhou, Q.2    Kalderon, D.3
  • 28
    • 30444437000 scopus 로고    scopus 로고
    • Evidence for the direct involvement of bTrCP in Gli3 protein processing
    • B. Wang, Y. Li, Evidence for the direct involvement of bTrCP in Gli3 protein processing. Proc. Natl. Acad. Sci. U.S.A. 103, 33-38 (2006).
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 33-38
    • Wang, B.1    Li, Y.2
  • 29
    • 0031587830 scopus 로고    scopus 로고
    • Proteolysis that is inhibited by Hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor
    • P. Aza-Blanc, F. Ramírez-Weber, M. Laget, C. Schwartz, T. Kornberg, Proteolysis that is inhibited by Hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor. Cell 89, 1043-1053 (1997).
    • (1997) Cell , vol.89 , pp. 1043-1053
    • Aza-Blanc, P.1    Ramírez-Weber, F.2    Laget, M.3    Schwartz, C.4    Kornberg, T.5
  • 30
    • 13344261322 scopus 로고    scopus 로고
    • Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus
    • W. Zhang, Y. Zhao, C. Tong, G. Wang, B. Wang, J. Jia, J. Jiang, Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus. Dev. Cell 8, 267-278 (2005).
    • (2005) Dev. Cell , vol.8 , pp. 267-278
    • Zhang, W.1    Zhao, Y.2    Tong, C.3    Wang, G.4    Wang, B.5    Jia, J.6    Jiang, J.7
  • 31
    • 0034681266 scopus 로고    scopus 로고
    • Hedgehog-regulated processing of Gli3 produces an anterior/posterior repressor gradient in the developing vertebrate limb
    • B. Wang, J. F. Fallon, P. A. Beachy, Hedgehog-regulated processing of Gli3 produces an anterior/posterior repressor gradient in the developing vertebrate limb. Cell 100, 423-434 (2000).
    • (2000) Cell , vol.100 , pp. 423-434
    • Wang, B.1    Fallon, J.F.2    Beachy, P.A.3
  • 32
    • 84861225973 scopus 로고    scopus 로고
    • Hh-induced Smoothened conformational switch is mediated by differential phosphorylation at its C-terminal tail in a dose- and position-dependent manner
    • J. Fan, Y. Liu, J. Jia, Hh-induced Smoothened conformational switch is mediated by differential phosphorylation at its C-terminal tail in a dose- and position-dependent manner. Dev. Biol. 366, 172-184 (2012).
    • (2012) Dev. Biol. , vol.366 , pp. 172-184
    • Fan, J.1    Liu, Y.2    Jia, J.3
  • 34
  • 35
    • 77956805860 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 2 promotes high-level Hedgehog signaling by regulating the active state of Smo through kinase-dependent and kinase-independent mechanisms in Drosophila
    • Y. Chen, S. Li, C. Tong, Y. Zhao, B. Wang, Y. Liu, J. Jia, J. Jiang, G protein-coupled receptor kinase 2 promotes high-level Hedgehog signaling by regulating the active state of Smo through kinase-dependent and kinase-independent mechanisms in Drosophila. Genes Dev. 24, 2054-2067 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 2054-2067
    • Chen, Y.1    Li, S.2    Tong, C.3    Zhao, Y.4    Wang, B.5    Liu, Y.6    Jia, J.7    Jiang, J.8
  • 36
    • 0034669178 scopus 로고    scopus 로고
    • Interactions with Costal2 and Suppressor of Fused regulate nuclear translocation and activity of Cubitus interruptus
    • G. Wang, K. Amanai, B. Wang, J. Jiang, Interactions with Costal2 and Suppressor of Fused regulate nuclear translocation and activity of Cubitus interruptus. Genes Dev. 14, 2893-2905 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 2893-2905
    • Wang, G.1    Amanai, K.2    Wang, B.3    Jiang, J.4
  • 39
    • 69449099121 scopus 로고    scopus 로고
    • Mouse Kif7/Costal2 is a ciliaassociated protein that regulates Sonic hedgehog signaling
    • K. F. Liem Jr., M. He, P. J. Ocbina, K. V. Anderson, Mouse Kif7/Costal2 is a ciliaassociated protein that regulates Sonic hedgehog signaling. Proc. Natl. Acad. Sci. U.S.A. 106, 13377-13382 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13377-13382
    • Liem Jr., K.F.1    He, M.2    Ocbina, P.J.3    Anderson, K.V.4
  • 41
    • 80052515585 scopus 로고    scopus 로고
    • The Hedgehog-induced Smoothened conformational switch assembles a signaling complex that activates Fused by promoting its dimerization and phosphorylation
    • Q. Shi, S. Li, J. Jia, J. Jiang, The Hedgehog-induced Smoothened conformational switch assembles a signaling complex that activates Fused by promoting its dimerization and phosphorylation. Development 138, 4219-4231 (2011).
    • (2011) Development , vol.138 , pp. 4219-4231
    • Shi, Q.1    Li, S.2    Jia, J.3    Jiang, J.4
  • 42
    • 84868528041 scopus 로고    scopus 로고
    • Smoothened transduces Hedgehog signal by forming a complex with Evc/Evc2
    • C. Yang, W. Chen, Y. Chen, J. Jiang, Smoothened transduces Hedgehog signal by forming a complex with Evc/Evc2. Cell Res. 22, 1593-1604 (2012).
    • (2012) Cell Res. , vol.22 , pp. 1593-1604
    • Yang, C.1    Chen, W.2    Chen, Y.3    Jiang, J.4
  • 43
    • 0025330489 scopus 로고
    • cAMP-dependent protein kinase: Framework for a diverse family of regulatory enzymes
    • S. S. Taylor, J. A. Buechler, W. Yonemoto, cAMP-dependent protein kinase: Framework for a diverse family of regulatory enzymes. Annu. Rev. Biochem. 59, 971- 1005 (1990).
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 971-1005
    • Taylor, S.S.1    Buechler, J.A.2    Yonemoto, W.3
  • 44
    • 57049085407 scopus 로고    scopus 로고
    • G protein Gai functions immediately downstream of Smoothened in Hedgehog signalling
    • S. K. Ogden, D. L. Fei, N. S. Schilling, Y. F. Ahmed, J. Hwa, D. J. Robbins, G protein Gai functions immediately downstream of Smoothened in Hedgehog signalling. Nature 456, 967-970 (2008).
    • (2008) Nature , vol.456 , pp. 967-970
    • Ogden, S.K.1    Fei, D.L.2    Schilling, N.S.3    Ahmed, Y.F.4    Hwa, J.5    Robbins, D.J.6
  • 45
    • 62349102527 scopus 로고    scopus 로고
    • PP4 and PP2A regulate Hedgehog signaling by controlling Smo and Ci phosphorylation
    • H. Jia, Y. Liu, W. Yan, J. Jia, PP4 and PP2A regulate Hedgehog signaling by controlling Smo and Ci phosphorylation. Development 136, 307-316 (2009).
    • (2009) Development , vol.136 , pp. 307-316
    • Jia, H.1    Liu, Y.2    Yan, W.3    Jia, J.4
  • 47
    • 0028329349 scopus 로고
    • Compartment boundaries and the control of Drosophila limb pattern by hedgehog protein
    • K. Basler, G. Struhl, Compartment boundaries and the control of Drosophila limb pattern by hedgehog protein. Nature 368, 208-214 (1994).
    • (1994) Nature , vol.368 , pp. 208-214
    • Basler, K.1    Struhl, G.2
  • 48
    • 0028178786 scopus 로고
    • Hedgehog is a signaling protein with a key role in patterning Drosophila imaginal discs
    • T. Tabata, T. B. Kornberg, Hedgehog is a signaling protein with a key role in patterning Drosophila imaginal discs. Cell 76, 89-102 (1994).
    • (1994) Cell , vol.76 , pp. 89-102
    • Tabata, T.1    Kornberg, T.B.2
  • 49
    • 0024440611 scopus 로고
    • A protein with several possible membrane-spanning domains encoded by the Drosophila segment polarity gene patched
    • Y. Nakano, I. Guerrero, A. Hidalgo, A. Taylor, J. R. Whittle, P. W. Ingham, A protein with several possible membrane-spanning domains encoded by the Drosophila segment polarity gene patched. Nature 341, 508-513 (1989).
    • (1989) Nature , vol.341 , pp. 508-513
    • Nakano, Y.1    Guerrero, I.2    Hidalgo, A.3    Taylor, A.4    Whittle, J.R.5    Ingham, P.W.6
  • 50
    • 25644446102 scopus 로고    scopus 로고
    • Insulin disrupts b-adrenergic signalling to protein kinase A in adipocytes
    • J. Zhang, C. J. Hupfeld, S. S. Taylor, J. M. Olefsky, R. Y. Tsien, Insulin disrupts b-adrenergic signalling to protein kinase A in adipocytes. Nature 437, 569-573 (2005).
    • (2005) Nature , vol.437 , pp. 569-573
    • Zhang, J.1    Hupfeld, C.J.2    Taylor, S.S.3    Olefsky, J.M.4    Tsien, R.Y.5
  • 51
    • 33746907024 scopus 로고    scopus 로고
    • Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters
    • M. D. Allen, J. Zhang, Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters. Biochem. Biophys. Res. Commun. 348, 716-721 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 716-721
    • Allen, M.D.1    Zhang, J.2
  • 52
    • 2342652901 scopus 로고
    • Forskolin: Unique diterpene activator of adenylate cyclase in membranes and in intact cells
    • K. B. Seamon, W. Padgett, J. W. Daly, Forskolin: Unique diterpene activator of adenylate cyclase in membranes and in intact cells. Proc. Natl. Acad. Sci. U.S.A. 78, 3363-3367 (1981).
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 3363-3367
    • Seamon, K.B.1    Padgett, W.2    Daly, J.W.3
  • 53
    • 10744233219 scopus 로고    scopus 로고
    • Hedgehog signal transduction via Smoothened association with a cytoplasmic complex scaffolded by the atypical kinesin, Costal-2
    • L. Lum, C. Zhang, S. Oh, R. K. Mann, D. P. von Kessler, J. Taipale, F. Weis-Garcia, R. Gong, B. Wang, P. A. Beachy, Hedgehog signal transduction via Smoothened association with a cytoplasmic complex scaffolded by the atypical kinesin, Costal-2. Mol. Cell 12, 1261-1274 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1261-1274
    • Lum, L.1    Zhang, C.2    Oh, S.3    Mann, R.K.4    Von Kessler, D.P.5    Taipale, J.6    Weis-Garcia, F.7    Gong, R.8    Wang, B.9    Beachy, P.A.10
  • 54
    • 0032728958 scopus 로고    scopus 로고
    • Protein kinase A antagonizes Hedgehog signaling by regulating both the activator and repressor forms of Cubitus interruptus
    • G. Wang, B. Wang, J. Jiang, Protein kinase A antagonizes Hedgehog signaling by regulating both the activator and repressor forms of Cubitus interruptus. Genes Dev. 13, 2828-2837 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2828-2837
    • Wang, G.1    Wang, B.2    Jiang, J.3
  • 55
    • 0032413830 scopus 로고    scopus 로고
    • In vivo evidence that Patched and Smoothened constitute distinct binding and transducing components of a Hedgehog receptor complex
    • Y. Chen, G. Struhl, In vivo evidence that Patched and Smoothened constitute distinct binding and transducing components of a Hedgehog receptor complex. Development 125, 4943-4948 (1998).
    • (1998) Development , vol.125 , pp. 4943-4948
    • Chen, Y.1    Struhl, G.2
  • 56
    • 84863012714 scopus 로고    scopus 로고
    • Hedgehog-regulated ubiquitination controls Smoothened trafficking and cell surface expression in Drosophila
    • S. Li, Y. Chen, Q. Shi, T. Yue, B. Wang, J. Jiang, Hedgehog-regulated ubiquitination controls Smoothened trafficking and cell surface expression in Drosophila. PLOS Biol. 10, e1001239 (2012).
    • (2012) PLOS Biol. , vol.10
    • Li, S.1    Chen, Y.2    Shi, Q.3    Yue, T.4    Wang, B.5    Jiang, J.6
  • 57
  • 58
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D. R. Knighton, J. H. Zheng, L. F. Ten Eyck, N. H. Xuong, S. S. Taylor, J. M. Sowadski, Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420 (1991).
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 60
    • 84877101725 scopus 로고    scopus 로고
    • Smoothened oligomerization/ higher order clustering in lipid rafts is essential for high Hedgehog activity transduction
    • D. Shi, X. Lv, Z. Zhang, X. Yang, Z. Zhou, L. Zhang, Y. Zhao, Smoothened oligomerization/ higher order clustering in lipid rafts is essential for high Hedgehog activity transduction. J. Biol. Chem. 288, 12605-12614 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 12605-12614
    • Shi, D.1    Lv, X.2    Zhang, Z.3    Yang, X.4    Zhou, Z.5    Zhang, L.6    Zhao, Y.7
  • 61
    • 0141728540 scopus 로고    scopus 로고
    • Stability and association of Smoothened, Costal2 and Fused with Cubitus interruptus are regulated by Hedgehog
    • L. Ruel, R. Rodriguez, A. Gallet, L. Lavenant-Staccini, P. P. Thérond, Stability and association of Smoothened, Costal2 and Fused with Cubitus interruptus are regulated by Hedgehog. Nat. Cell Biol. 5, 907-913 (2003).
    • (2003) Nat. Cell Biol. , vol.5 , pp. 907-913
    • Ruel, L.1    Rodriguez, R.2    Gallet, A.3    Lavenant-Staccini, L.4    Thérond, P.P.5
  • 62
    • 0242361620 scopus 로고    scopus 로고
    • Smoothened transduces Hedgehog signal by physically interacting with Costal2/Fused complex through its C-terminal tail
    • J. Jia, C. Tong, J. Jiang, Smoothened transduces Hedgehog signal by physically interacting with Costal2/Fused complex through its C-terminal tail. Genes Dev. 17, 2709-2720 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 2709-2720
    • Jia, J.1    Tong, C.2    Jiang, J.3
  • 63
    • 0242625184 scopus 로고    scopus 로고
    • Identification of a functional interaction between the transmembrane protein Smoothened and the kinesin-related protein Costal2
    • S. K. Ogden, M. Ascano Jr., M. A. Stegman, L. M. Suber, J. E. Hooper, D. J. Robbins, Identification of a functional interaction between the transmembrane protein Smoothened and the kinesin-related protein Costal2. Curr. Biol. 13, 1998-2003 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1998-2003
    • Ogden, S.K.1    Ascano Jr., M.2    Stegman, M.A.3    Suber, L.M.4    Hooper, J.E.5    Robbins, D.J.6
  • 64
    • 0030663064 scopus 로고    scopus 로고
    • A Hedgehog activity gradient contributes to AP axial patterning of the Drosophila wing
    • M. Strigini, S. M. Cohen, A Hedgehog activity gradient contributes to AP axial patterning of the Drosophila wing. Development 124, 4697-4705 (1997).
    • (1997) Development , vol.124 , pp. 4697-4705
    • Strigini, M.1    Cohen, S.M.2
  • 65
    • 0030297553 scopus 로고    scopus 로고
    • Dual roles for Patched in sequestering and transducing Hedgehog
    • Y. Chen, G. Struhl, Dual roles for Patched in sequestering and transducing Hedgehog. Cell 87, 553-563 (1996).
    • (1996) Cell , vol.87 , pp. 553-563
    • Chen, Y.1    Struhl, G.2
  • 66
    • 0032585515 scopus 로고    scopus 로고
    • Hedgehog stimulates maturation of Cubitus interruptus into a labile transcriptional activator
    • J. T. Ohlmeyer, D. Kalderon, Hedgehog stimulates maturation of Cubitus interruptus into a labile transcriptional activator. Nature 396, 749-753 (1998).
    • (1998) Nature , vol.396 , pp. 749-753
    • Ohlmeyer, J.T.1    Kalderon, D.2
  • 69
    • 84872508509 scopus 로고    scopus 로고
    • The ciliary G-protein-coupled receptor Gpr161 negatively regulates the Sonic hedgehog pathway via cAMP signaling
    • S. Mukhopadhyay, X. Wen, N. Ratti, A. Loktev, L. Rangell, S. J. Scales, P. K. Jackson, The ciliary G-protein-coupled receptor Gpr161 negatively regulates the Sonic hedgehog pathway via cAMP signaling. Cell 152, 210-223 (2013).
    • (2013) Cell , vol.152 , pp. 210-223
    • Mukhopadhyay, S.1    Wen, X.2    Ratti, N.3    Loktev, A.4    Rangell, L.5    Scales, S.J.6    Jackson, P.K.7
  • 71
    • 82855169173 scopus 로고    scopus 로고
    • Drosophila G-protein-coupled receptor kinase 2 regulates cAMP-dependent Hedgehog signaling
    • S. Cheng, D. Maier, D. R. Hipfner, Drosophila G-protein-coupled receptor kinase 2 regulates cAMP-dependent Hedgehog signaling. Development 139, 85-94 (2012).
    • (2012) Development , vol.139 , pp. 85-94
    • Cheng, S.1    Maier, D.2    Hipfner, D.R.3
  • 72
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • W. Wong, J. D. Scott, AKAP signalling complexes: Focal points in space and time. Nat. Rev. Mol. Cell Biol. 5, 959 -970 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 73
    • 72449171640 scopus 로고    scopus 로고
    • Sonic-hedgehog- mediated proliferation requires the localization of PKA to the cilium base
    • M. Barzi, J. Berenguer, A. Menendez, R. Alvarez-Rodriguez, S. Pons, Sonic-hedgehog- mediated proliferation requires the localization of PKA to the cilium base. J. Cell Sci. 123, 62-69 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 62-69
    • Barzi, M.1    Berenguer, J.2    Menendez, A.3    Alvarez-Rodriguez, R.4    Pons, S.5
  • 74
    • 31644442906 scopus 로고    scopus 로고
    • Signaling from Smo to Ci/Gli: Conservation and divergence of Hedgehog pathways from Drosophila to vertebrates
    • D. Huangfu, K. V. Anderson, Signaling from Smo to Ci/Gli: Conservation and divergence of Hedgehog pathways from Drosophila to vertebrates. Development 133, 3-14 (2006).
    • (2006) Development , vol.133 , pp. 3-14
    • Huangfu, D.1    Anderson, K.V.2
  • 76
    • 0029852209 scopus 로고    scopus 로고
    • Visualization of gene expression in living adult Drosophila
    • M. Calleja, E. Moreno, S. Pelaz, G. Morata, Visualization of gene expression in living adult Drosophila. Science 274, 252-255 (1996).
    • (1996) Science , vol.274 , pp. 252-255
    • Calleja, M.1    Moreno, E.2    Pelaz, S.3    Morata, G.4
  • 77
    • 0035341376 scopus 로고    scopus 로고
    • Mosaic analysis with a repressible cell marker (MARCM) for Drosophila neural development
    • T. Lee, L. Luo, Mosaic analysis with a repressible cell marker (MARCM) for Drosophila neural development. Trends Neurosci. 24, 251-254 (2001).
    • (2001) Trends Neurosci. , vol.24 , pp. 251-254
    • Lee, T.1    Luo, L.2
  • 78
    • 0021285532 scopus 로고
    • A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation
    • F. R. Cross, E. A. Garber, D. Pellman, H. Hanafusa, A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol. Cell. Biol. 4, 1834-1842 (1984).
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1834-1842
    • Cross, F.R.1    Garber, E.A.2    Pellman, D.3    Hanafusa, H.4
  • 79
    • 0022134524 scopus 로고
    • The nucleotide sequence and the tissue-specific expression of Drosophila c-src
    • M. A. Simon, B. Drees, T. Kornberg, J. M. Bishop, The nucleotide sequence and the tissue-specific expression of Drosophila c-src. Cell 42, 831-840 (1985).
    • (1985) Cell , vol.42 , pp. 831-840
    • Simon, M.A.1    Drees, B.2    Kornberg, T.3    Bishop, J.M.4
  • 80
    • 15744399873 scopus 로고    scopus 로고
    • Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase
    • G. H. Iyer, M. J. Moore, S. S. Taylor, Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase. J. Biol. Chem. 280, 8800-8807 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 8800-8807
    • Iyer, G.H.1    Moore, M.J.2    Taylor, S.S.3
  • 81
    • 0033598401 scopus 로고    scopus 로고
    • Casein kinase I transduces Wnt signals
    • J. M. Peters, R. M. McKay, J. P. McKay, J. M. Graff, Casein kinase I transduces Wnt signals. Nature 401, 345- 350 (1999).
    • (1999) Nature , vol.401 , pp. 345-350
    • Peters, J.M.1    McKay, R.M.2    McKay, J.P.3    Graff, J.M.4
  • 82
    • 33847660443 scopus 로고    scopus 로고
    • An optimized transgenesis system for Drosophila using germ-line-specific φC31 integrases
    • J. Bischof, R. K. Maeda, M. Hediger, F. Karch, K. Basler, An optimized transgenesis system for Drosophila using germ-line-specific φC31 integrases. Proc. Natl. Acad. Sci. U.S.A. 104, 3312-3317 (2007).
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 3312-3317
    • Bischof, J.1    Maeda, R.K.2    Hediger, M.3    Karch, F.4    Basler, K.5
  • 83
    • 34547621412 scopus 로고    scopus 로고
    • Fused-Costal2 protein complex regulates Hedgehoginduced Smo phosphorylation and cell-surface accumulation
    • Y. Liu, X. Cao, J. Jiang, J. Jia, Fused-Costal2 protein complex regulates Hedgehoginduced Smo phosphorylation and cell-surface accumulation. Genes Dev. 21, 1949-1963 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1949-1963
    • Liu, Y.1    Cao, X.2    Jiang, J.3    Jia, J.4
  • 84
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • G. M. Rubin, A. C. Spradling, Genetic transformation of Drosophila with transposable element vectors. Science 218, 348-353 (1982).
    • (1982) Science , vol.218 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 85
    • 0029126148 scopus 로고
    • The Drosophila cubitus interruptus protein and its role in the wingless and hedgehog signal transduction pathways
    • C. K. Motzny, R. Holmgren, The Drosophila cubitus interruptus protein and its role in the wingless and hedgehog signal transduction pathways. Mech. Dev. 52, 137-150 (1995).
    • (1995) Mech. Dev. , vol.52 , pp. 137-150
    • Motzny, C.K.1    Holmgren, R.2
  • 86
    • 0033529667 scopus 로고    scopus 로고
    • Nuclear trafficking of Cubitus interruptus in the transcriptional regulation of Hedgehog target gene expression
    • C. H. Chen, D. P. von Kessler, W. Park, B. Wang, Y. Ma, P. A. Beachy, 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    Von Kessler, D.P.2    Park, W.3    Wang, B.4    Ma, Y.5    Beachy, P.A.6
  • 87
    • 28444451148 scopus 로고    scopus 로고
    • A genome-wide RNA interference screen in Drosophila melanogaster cells for new components of the Hh signaling pathway
    • K. Nybakken, S. A. Vokes, T. Y. Lin, A. P. McMahon, N. Perrimon, A genome-wide RNA interference screen in Drosophila melanogaster cells for new components of the Hh signaling pathway. Nat. Genet. 37, 1323-1332 (2005).
    • (2005) Nat. Genet. , vol.37 , pp. 1323-1332
    • Nybakken, K.1    Vokes, S.A.2    Lin, T.Y.3    McMahon, A.P.4    Perrimon, N.5


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