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Volumn 39, Issue 4, 2016, Pages 438-451

Regulation of Smoothened Trafficking and Hedgehog Signaling by the SUMO Pathway

Author keywords

Gli; GPCR; hedgehog; PKA; primary cilium; Shh; Smo; SUMO; Ulp1; USP8

Indexed keywords

DEUBIQUITINASE; MEMBRANE PROTEIN; SMOOTHENED PROTEIN; SONIC HEDGEHOG PROTEIN; SUMO PROTEIN; UBPY PROTEIN; ULP1 PROTEIN; UNCLASSIFIED DRUG; DROSOPHILA PROTEIN; LYSINE; SMOOTHENED PROTEIN, DROSOPHILA;

EID: 84997542928     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2016.09.014     Document Type: Article
Times cited : (48)

References (59)
  • 1
    • 12344305145 scopus 로고    scopus 로고
    • Drosophila Smoothened phosphorylation sites essential for Hedgehog signal transduction
    • Apionishev, S., Katanayeva, N.M., Marks, S.A., Kalderon, D., Tomlinson, A., Drosophila Smoothened phosphorylation sites essential for Hedgehog signal transduction. Nat. Cell Biol. 7 (2005), 86–92.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 86-92
    • Apionishev, S.1    Katanayeva, N.M.2    Marks, S.A.3    Kalderon, D.4    Tomlinson, A.5
  • 2
    • 33847660443 scopus 로고    scopus 로고
    • An optimized transgenesis system for Drosophila using germ-line-specific phiC31 integrases
    • Bischof, J., Maeda, R.K., Hediger, M., Karch, F., Basler, K., An optimized transgenesis system for Drosophila using germ-line-specific phiC31 integrases. Proc. Natl. Acad. Sci. USA 104 (2007), 3312–3317.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3312-3317
    • Bischof, J.1    Maeda, R.K.2    Hediger, M.3    Karch, F.4    Basler, K.5
  • 3
    • 84879414522 scopus 로고    scopus 로고
    • The mechanisms of Hedgehog signalling and its roles in development and disease
    • Briscoe, J., Therond, P.P., The mechanisms of Hedgehog signalling and its roles in development and disease. Nat. Rev. Mol. Cell Biol. 14 (2013), 418–431.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 418-431
    • Briscoe, J.1    Therond, P.P.2
  • 4
    • 84873735792 scopus 로고    scopus 로고
    • Decoding the phosphorylation code in Hedgehog signal transduction
    • Chen, Y., Jiang, J., Decoding the phosphorylation code in Hedgehog signal transduction. Cell Res. 23 (2013), 186–200.
    • (2013) Cell Res. , vol.23 , pp. 186-200
    • Chen, Y.1    Jiang, J.2
  • 5
    • 0032413830 scopus 로고    scopus 로고
    • In vivo evidence that patched and smoothened constitute distinct binding and transducing components of a Hedgehog receptor complex
    • Chen, Y., Struhl, G., In vivo evidence that patched and smoothened constitute distinct binding and transducing components of a Hedgehog receptor complex. Development 125 (1998), 4943–4948.
    • (1998) Development , vol.125 , pp. 4943-4948
    • Chen, Y.1    Struhl, G.2
  • 6
    • 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
    • Chen, Y., Li, S., Tong, C., Zhao, Y., Wang, B., Liu, Y., Jia, J., Jiang, J., 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 (2010), 2054–2067.
    • (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
  • 7
    • 79959804711 scopus 로고    scopus 로고
    • Sonic Hedgehog dependent phosphorylation by CK1alpha and GRK2 is required for ciliary accumulation and activation of smoothened
    • Chen, Y., Sasai, N., Ma, G., Yue, T., Jia, J., Briscoe, J., Jiang, J., Sonic Hedgehog dependent phosphorylation by CK1alpha and GRK2 is required for ciliary accumulation and activation of smoothened. PLoS Biol., 9, 2011, e1001083.
    • (2011) PLoS Biol. , vol.9 , pp. e1001083
    • Chen, Y.1    Sasai, N.2    Ma, G.3    Yue, T.4    Jia, J.5    Briscoe, J.6    Jiang, J.7
  • 8
    • 35548935098 scopus 로고    scopus 로고
    • SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia
    • Cheng, J., Kang, X., Zhang, S., Yeh, E.T., SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia. Cell 131 (2007), 584–595.
    • (2007) Cell , vol.131 , pp. 584-595
    • Cheng, J.1    Kang, X.2    Zhang, S.3    Yeh, E.T.4
  • 9
    • 70450221494 scopus 로고    scopus 로고
    • Regulation of smoothened by Drosophila G-protein-coupled receptor kinases
    • Cheng, S., Maier, D., Neubueser, D., Hipfner, D.R., Regulation of smoothened by Drosophila G-protein-coupled receptor kinases. Dev. Biol. 337 (2010), 99–109.
    • (2010) Dev. Biol. , vol.337 , pp. 99-109
    • Cheng, S.1    Maier, D.2    Neubueser, D.3    Hipfner, D.R.4
  • 11
    • 77957774529 scopus 로고    scopus 로고
    • SUMOylation by Pias1 regulates the activity of the Hedgehog dependent Gli transcription factors
    • Cox, B., Briscoe, J., Ulloa, F., SUMOylation by Pias1 regulates the activity of the Hedgehog dependent Gli transcription factors. PLoS One, 5, 2010, e11996.
    • (2010) PLoS One , vol.5 , pp. e11996
    • Cox, B.1    Briscoe, J.2    Ulloa, F.3
  • 12
    • 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 (2000), 521–531.
    • (2000) Cell , vol.102 , pp. 521-531
    • Denef, N.1    Neubuser, D.2    Perez, L.3    Cohen, S.M.4
  • 13
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • Desterro, J.M., Rodriguez, M.S., Hay, R.T., SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol. Cell 2 (1998), 233–239.
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 14
    • 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
    • Fan, J., Liu, Y., Jia, J., 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 (2012), 172–184.
    • (2012) Dev. Biol. , vol.366 , pp. 172-184
    • Fan, J.1    Liu, Y.2    Jia, J.3
  • 15
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J.R., Lima, C.D., The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11 (2010), 861–871.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 17
    • 24344445216 scopus 로고    scopus 로고
    • Something about SUMO inhibits transcription
    • Gill, G., Something about SUMO inhibits transcription. Curr. Opin. Genet. Dev. 15 (2005), 536–541.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 536-541
    • Gill, G.1
  • 18
    • 84861998949 scopus 로고    scopus 로고
    • Small ubiquitin-like Modifier (SUMO) modification inhibits GLI2 protein transcriptional activity in vitro and in vivo
    • Han, L., Pan, Y., Wang, B., Small ubiquitin-like Modifier (SUMO) modification inhibits GLI2 protein transcriptional activity in vitro and in vivo. J. Biol. Chem. 287 (2012), 20483–20489.
    • (2012) J. Biol. Chem. , vol.287 , pp. 20483-20489
    • Han, L.1    Pan, Y.2    Wang, B.3
  • 19
    • 84929493246 scopus 로고    scopus 로고
    • Multisite interaction with Sufu regulates Ci/Gli activity through distinct mechanisms in Hh signal transduction
    • Han, Y., Shi, Q., Jiang, J., Multisite interaction with Sufu regulates Ci/Gli activity through distinct mechanisms in Hh signal transduction. Proc. Natl. Acad. Sci. USA 112 (2015), 6383–6388.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 6383-6388
    • Han, Y.1    Shi, Q.2    Jiang, J.3
  • 20
    • 0034993496 scopus 로고    scopus 로고
    • The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family
    • Hari, K.L., Cook, K.R., Karpen, G.H., The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family. Genes Dev. 15 (2001), 1334–1348.
    • (2001) Genes Dev. , vol.15 , pp. 1334-1348
    • Hari, K.L.1    Cook, K.R.2    Karpen, G.H.3
  • 21
    • 18844414816 scopus 로고    scopus 로고
    • The lesswright mutation activates Rel-related proteins, leading to overproduction of larval hemocytes in Drosophila melanogaster
    • Huang, L., Ohsako, S., Tanda, S., The lesswright mutation activates Rel-related proteins, leading to overproduction of larval hemocytes in Drosophila melanogaster. Dev. Biol. 280 (2005), 407–420.
    • (2005) Dev. Biol. , vol.280 , pp. 407-420
    • Huang, L.1    Ohsako, S.2    Tanda, S.3
  • 22
    • 31644442906 scopus 로고    scopus 로고
    • Signaling from Smo to Ci/Gli: conservation and divergence of Hedgehog pathways from Drosophila to vertebrates
    • Huangfu, D., Anderson, K.V., Signaling from Smo to Ci/Gli: conservation and divergence of Hedgehog pathways from Drosophila to vertebrates. Development 133 (2006), 3–14.
    • (2006) Development , vol.133 , pp. 3-14
    • Huangfu, D.1    Anderson, K.V.2
  • 23
    • 80054022786 scopus 로고    scopus 로고
    • Gli proteins in development and disease
    • Hui, C.C., Angers, S., Gli proteins in development and disease. Annu. Rev. Cell Dev. Biol. 27 (2011), 513–537.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 513-537
    • Hui, C.C.1    Angers, S.2
  • 24
    • 0035577854 scopus 로고    scopus 로고
    • Hedgehog signaling in animal development: paradigms and principles
    • Ingham, P.W., McMahon, A.P., Hedgehog signaling in animal development: paradigms and principles. Genes Dev. 15 (2001), 3059–3087.
    • (2001) Genes Dev. , vol.15 , pp. 3059-3087
    • Ingham, P.W.1    McMahon, A.P.2
  • 25
    • 0242361620 scopus 로고    scopus 로고
    • Smoothened transduces Hedgehog signal by physically interacting with Costal2/Fused complex through its C-terminal tail
    • Jia, J., Tong, C., Jiang, J., Smoothened transduces Hedgehog signal by physically interacting with Costal2/Fused complex through its C-terminal tail. Genes Dev. 17 (2003), 2709–2720.
    • (2003) Genes Dev. , vol.17 , pp. 2709-2720
    • Jia, J.1    Tong, C.2    Jiang, J.3
  • 26
    • 11144237279 scopus 로고    scopus 로고
    • Hedgehog signalling activity of Smoothened requires phosphorylation by protein kinase A and casein kinase I
    • Jia, J., Tong, C., Wang, B., Luo, L., Jiang, J., Hedgehog signalling activity of Smoothened requires phosphorylation by protein kinase A and casein kinase I. Nature 432 (2004), 1045–1050.
    • (2004) Nature , vol.432 , pp. 1045-1050
    • Jia, J.1    Tong, C.2    Wang, B.3    Luo, L.4    Jiang, J.5
  • 27
    • 62349102527 scopus 로고    scopus 로고
    • PP4 and PP2A regulate Hedgehog signaling by controlling Smo and Ci phosphorylation
    • Jia, H., Liu, Y., Yan, W., Jia, J., PP4 and PP2A regulate Hedgehog signaling by controlling Smo and Ci phosphorylation. Development 136 (2009), 307–316.
    • (2009) Development , vol.136 , pp. 307-316
    • Jia, H.1    Liu, Y.2    Yan, W.3    Jia, J.4
  • 28
    • 78549236202 scopus 로고    scopus 로고
    • Casein kinase 2 promotes Hedgehog signaling by regulating both smoothened and Cubitus interruptus
    • Jia, H., Liu, Y., Xia, R., Tong, C., Yue, T., Jiang, J., Jia, J., Casein kinase 2 promotes Hedgehog signaling by regulating both smoothened and Cubitus interruptus. J. Biol. Chem. 285 (2010), 37218–37226.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37218-37226
    • Jia, H.1    Liu, Y.2    Xia, R.3    Tong, C.4    Yue, T.5    Jiang, J.6    Jia, J.7
  • 29
    • 57049089995 scopus 로고    scopus 로고
    • Hedgehog signaling in development and cancer
    • Jiang, J., Hui, C.C., Hedgehog signaling in development and cancer. Dev. Cell 15 (2008), 801–812.
    • (2008) Dev. Cell , vol.15 , pp. 801-812
    • Jiang, J.1    Hui, C.C.2
  • 30
    • 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 80 (1995), 563–572.
    • (1995) Cell , vol.80 , pp. 563-572
    • Jiang, J.1    Struhl, G.2
  • 31
    • 84909606348 scopus 로고    scopus 로고
    • Hedgehog-regulated atypical PKC promotes phosphorylation and activation of Smoothened and Cubitus interruptus in Drosophila
    • Jiang, K., Liu, Y., Fan, J., Epperly, G., Gao, T., Jiang, J., Jia, J., Hedgehog-regulated atypical PKC promotes phosphorylation and activation of Smoothened and Cubitus interruptus in Drosophila. Proc. Natl. Acad. Sci. USA 111 (2014), E4842–E4850.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E4842-E4850
    • Jiang, K.1    Liu, Y.2    Fan, J.3    Epperly, G.4    Gao, T.5    Jiang, J.6    Jia, J.7
  • 32
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E.S., Protein modification by SUMO. Annu. Rev. Biochem. 73 (2004), 355–382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 33
    • 0035341376 scopus 로고    scopus 로고
    • Mosaic analysis with a repressible cell marker (MARCM) for Drosophila neural development
    • Lee, T., Luo, L., Mosaic analysis with a repressible cell marker (MARCM) for Drosophila neural development. Trends Neurosci. 24 (2001), 251–254.
    • (2001) Trends Neurosci. , vol.24 , pp. 251-254
    • Lee, T.1    Luo, L.2
  • 34
    • 84863012714 scopus 로고    scopus 로고
    • Hedgehog-regulated ubiquitination controls smoothened trafficking and cell surface expression in Drosophila
    • Li, S., Chen, Y., Shi, Q., Yue, T., Wang, B., Jiang, J., Hedgehog-regulated ubiquitination controls smoothened trafficking and cell surface expression in Drosophila. PLoS Biol., 10, 2012, e1001239.
    • (2012) PLoS Biol. , vol.10 , pp. e1001239
    • Li, S.1    Chen, Y.2    Shi, Q.3    Yue, T.4    Wang, B.5    Jiang, J.6
  • 35
    • 84903779617 scopus 로고    scopus 로고
    • Hedgehog induces formation of PKA-Smoothened complexes to promote Smoothened phosphorylation and pathway activation
    • Li, S., Ma, G., Wang, B., Jiang, J., Hedgehog induces formation of PKA-Smoothened complexes to promote Smoothened phosphorylation and pathway activation. Sci. Signal., 7, 2014, ra62.
    • (2014) Sci. Signal. , vol.7 , pp. ra62
    • Li, S.1    Ma, G.2    Wang, B.3    Jiang, J.4
  • 36
    • 84978943176 scopus 로고    scopus 로고
    • Regulation of smoothened phosphorylation and high-level hedgehog signaling activity by a plasma membrane associated kinase
    • Li, S., Li, S., Han, Y., Tong, C., Wang, B., Chen, Y., Jiang, J., Regulation of smoothened phosphorylation and high-level hedgehog signaling activity by a plasma membrane associated kinase. PLoS Biol., 14, 2016, e1002481.
    • (2016) PLoS Biol. , vol.14 , pp. e1002481
    • Li, S.1    Li, S.2    Han, Y.3    Tong, C.4    Wang, B.5    Chen, Y.6    Jiang, J.7
  • 37
    • 34547621412 scopus 로고    scopus 로고
    • Fused-Costal2 protein complex regulates Hedgehog-induced Smo phosphorylation and cell-surface accumulation
    • Liu, Y., Cao, X., Jiang, J., Jia, J., Fused-Costal2 protein complex regulates Hedgehog-induced Smo phosphorylation and cell-surface accumulation. Genes Dev. 21 (2007), 1949–1963.
    • (2007) Genes Dev. , vol.21 , pp. 1949-1963
    • Liu, Y.1    Cao, X.2    Jiang, J.3    Jia, J.4
  • 38
    • 10744233219 scopus 로고    scopus 로고
    • Hedgehog signal transduction via Smoothened association with a cytoplasmic complex scaffolded by the atypical kinesin, Costal-2
    • Lum, L., Zhang, C., Oh, S., Mann, R.K., von Kessler, D.P., Taipale, J., Weis-Garcia, F., Gong, R., Wang, B., Beachy, P.A., Hedgehog signal transduction via Smoothened association with a cytoplasmic complex scaffolded by the atypical kinesin, Costal-2. Mol. Cell 12 (2003), 1261–1274.
    • (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
  • 39
    • 37749021009 scopus 로고    scopus 로고
    • A role for SUMO modification in transcriptional repression and activation
    • Lyst, M.J., Stancheva, I., A role for SUMO modification in transcriptional repression and activation. Biochem. Soc. Trans. 35 (2007), 1389–1392.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1389-1392
    • Lyst, M.J.1    Stancheva, I.2
  • 40
    • 34249046463 scopus 로고    scopus 로고
    • SUMOylation regulates kainate-receptor-mediated synaptic transmission
    • Martin, S., Nishimune, A., Mellor, J.R., Henley, J.M., SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature 447 (2007), 321–325.
    • (2007) Nature , vol.447 , pp. 321-325
    • Martin, S.1    Nishimune, A.2    Mellor, J.R.3    Henley, J.M.4
  • 41
    • 77954903507 scopus 로고    scopus 로고
    • Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt
    • Mukai, A., Yamamoto-Hino, M., Awano, W., Watanabe, W., Komada, M., Goto, S., Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt. EMBO J. 29 (2010), 2114–2125.
    • (2010) EMBO J. , vol.29 , pp. 2114-2125
    • Mukai, A.1    Yamamoto-Hino, M.2    Awano, W.3    Watanabe, W.4    Komada, M.5    Goto, S.6
  • 42
    • 0032585515 scopus 로고    scopus 로고
    • Hedgehog stimulates maturation of Cubitus interruptus into a labile transcriptional activator
    • Ohlmeyer, J.T., Kalderon, D., Hedgehog stimulates maturation of Cubitus interruptus into a labile transcriptional activator. Nature 396 (1998), 749–753.
    • (1998) Nature , vol.396 , pp. 749-753
    • Ohlmeyer, J.T.1    Kalderon, D.2
  • 43
    • 34547110771 scopus 로고    scopus 로고
    • Patched1 regulates hedgehog signaling at the primary cilium
    • Rohatgi, R., Milenkovic, L., Scott, M.P., Patched1 regulates hedgehog signaling at the primary cilium. Science 317 (2007), 372–376.
    • (2007) Science , vol.317 , pp. 372-376
    • Rohatgi, R.1    Milenkovic, L.2    Scott, M.P.3
  • 44
    • 0141728540 scopus 로고    scopus 로고
    • Stability and association of smoothened, Costal2 and fused with cubitus interruptus are regulated by hedgehog
    • Ruel, L., Rodriguez, R., Gallet, A., Lavenant-Staccini, L., Therond, P.P., Stability and association of smoothened, Costal2 and fused with cubitus interruptus are regulated by hedgehog. Nat. Cell Biol. 5 (2003), 907–913.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 907-913
    • Ruel, L.1    Rodriguez, R.2    Gallet, A.3    Lavenant-Staccini, L.4    Therond, P.P.5
  • 45
  • 46
    • 84877101725 scopus 로고    scopus 로고
    • Smoothened oligomerization/higher order clustering in lipid rafts is essential for high Hedgehog activity transduction
    • Shi, D., Lv, X., Zhang, Z., Yang, X., Zhou, Z., Zhang, L., Zhao, Y., Smoothened oligomerization/higher order clustering in lipid rafts is essential for high Hedgehog activity transduction. J. Biol. Chem. 288 (2013), 12605–12614.
    • (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
  • 47
    • 79953220519 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) conjugation impedes transcriptional silencing by the polycomb group repressor Sex Comb on Midleg
    • Smith, M., Mallin, D.R., Simon, J.A., Courey, A.J., Small ubiquitin-like modifier (SUMO) conjugation impedes transcriptional silencing by the polycomb group repressor Sex Comb on Midleg. J. Biol. Chem. 286 (2011), 11391–11400.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11391-11400
    • Smith, M.1    Mallin, D.R.2    Simon, J.A.3    Courey, A.J.4
  • 49
    • 0035902140 scopus 로고    scopus 로고
    • The Hedgehog and Wnt signalling pathways in cancer
    • Taipale, J., Beachy, P.A., The Hedgehog and Wnt signalling pathways in cancer. Nature 411 (2001), 349–354.
    • (2001) Nature , vol.411 , pp. 349-354
    • Taipale, J.1    Beachy, P.A.2
  • 50
    • 36549074614 scopus 로고    scopus 로고
    • Using immunoprecipitation to study protein-protein interactions in the Hedgehog-signaling pathway
    • Tong, C., Jiang, J., Using immunoprecipitation to study protein-protein interactions in the Hedgehog-signaling pathway. Methods Mol. Biol. 397 (2007), 215–229.
    • (2007) Methods Mol. Biol. , vol.397 , pp. 215-229
    • Tong, C.1    Jiang, J.2
  • 51
    • 0033754122 scopus 로고    scopus 로고
    • The sonic hedgehog-patched-gli pathway in human development and disease
    • Villavicencio, E.H., Walterhouse, D.O., Iannaccone, P.M., The sonic hedgehog-patched-gli pathway in human development and disease. Am. J. Hum. Genet. 67 (2000), 1047–1054.
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 1047-1054
    • Villavicencio, E.H.1    Walterhouse, D.O.2    Iannaccone, P.M.3
  • 52
    • 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. 13 (1999), 2828–2837.
    • (1999) Genes Dev. , vol.13 , pp. 2828-2837
    • Wang, G.1    Wang, B.2    Jiang, J.3
  • 53
    • 77952566949 scopus 로고    scopus 로고
    • Mechanisms, regulation and consequences of protein SUMOylation
    • Wilkinson, K.A., Henley, J.M., Mechanisms, regulation and consequences of protein SUMOylation. Biochem. J. 428 (2010), 133–145.
    • (2010) Biochem. J. , vol.428 , pp. 133-145
    • Wilkinson, K.A.1    Henley, J.M.2
  • 54
    • 77953316514 scopus 로고    scopus 로고
    • Mechanism and evolution of cytosolic Hedgehog signal transduction
    • Wilson, C.W., Chuang, P.T., Mechanism and evolution of cytosolic Hedgehog signal transduction. Development 137 (2010), 2079–2094.
    • (2010) Development , vol.137 , pp. 2079-2094
    • Wilson, C.W.1    Chuang, P.T.2
  • 55
    • 84863012620 scopus 로고    scopus 로고
    • USP8 promotes smoothened signaling by preventing its ubiquitination and changing its subcellular localization
    • Xia, R., Jia, H., Fan, J., Liu, Y., Jia, J., USP8 promotes smoothened signaling by preventing its ubiquitination and changing its subcellular localization. PLoS Biol., 10, 2012, e1001238.
    • (2012) PLoS Biol. , vol.10 , pp. e1001238
    • Xia, R.1    Jia, H.2    Fan, J.3    Liu, Y.4    Jia, J.5
  • 56
    • 11144248964 scopus 로고    scopus 로고
    • Extensive phosphorylation of Smoothened in Hedgehog pathway activation
    • Zhang, C., Williams, E.H., Guo, Y., Lum, L., Beachy, P.A., Extensive phosphorylation of Smoothened in Hedgehog pathway activation. Proc. Natl. Acad. Sci. USA 101 (2004), 17900–17907.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17900-17907
    • Zhang, C.1    Williams, E.H.2    Guo, Y.3    Lum, L.4    Beachy, P.A.5
  • 57
    • 13344261322 scopus 로고    scopus 로고
    • Hedgehog-regulated costal2-kinase complexes control phosphorylation and proteolytic processing of cubitus interruptus
    • Zhang, W., Zhao, Y., Tong, C., Wang, G., Wang, B., Jia, J., Jiang, J., Hedgehog-regulated costal2-kinase complexes control phosphorylation and proteolytic processing of cubitus interruptus. Dev. Cell 8 (2005), 267–278.
    • (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
  • 58
    • 33646893705 scopus 로고    scopus 로고
    • A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor
    • Zhang, Q., Zhang, L., Wang, B., Ou, C.Y., Chien, C.T., Jiang, J., A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor. Dev. Cell 10 (2006), 719–729.
    • (2006) Dev. Cell , vol.10 , pp. 719-729
    • Zhang, Q.1    Zhang, L.2    Wang, B.3    Ou, C.Y.4    Chien, C.T.5    Jiang, J.6
  • 59
    • 36049033946 scopus 로고    scopus 로고
    • Hedgehog regulates smoothened activity by inducing a conformational switch
    • Zhao, Y., Tong, C., Jiang, J., Hedgehog regulates smoothened activity by inducing a conformational switch. Nature 450 (2007), 252–258.
    • (2007) Nature , vol.450 , pp. 252-258
    • Zhao, Y.1    Tong, C.2    Jiang, J.3


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