메뉴 건너뛰기




Volumn 5, Issue 246, 2012, Pages

The hedgehog signal transduction network

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN PATCHED; RECEPTOR; SMOOTHENED PROTEIN; SONIC HEDGEHOG PROTEIN; SONIC HEDGEHOG PROTEIN RECEPTOR; TRANSCRIPTION FACTOR GLI; TRANSCRIPTION FACTOR GLI1; UNCLASSIFIED DRUG;

EID: 84867799739     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2002906     Document Type: Review
Times cited : (346)

References (232)
  • 1
    • 0035577854 scopus 로고    scopus 로고
    • Hedgehog signaling in animal development: Paradigms and principles
    • P. W. Ingham, A. P. McMahon, Hedgehog signaling in animal development: Paradigms and principles. Genes Dev. 15, 3059-3087 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 3059-3087
    • Ingham, P.W.1    McMahon, A.P.2
  • 2
    • 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
  • 3
    • 9244221172 scopus 로고    scopus 로고
    • Tissue repair and stem cell renewal in carcinogenesis
    • P. A. Beachy, S. S. Karhadkar, D. M. Berman, Tissue repair and stem cell renewal in carcinogenesis. Nature 432, 324-331 (2004).
    • (2004) Nature , vol.432 , pp. 324-331
    • Beachy, P.A.1    Karhadkar, S.S.2    Berman, D.M.3
  • 4
    • 81855173503 scopus 로고    scopus 로고
    • Hedgehog signaling and the Gli code in stem cells, cancer, and metastases
    • A. Ruiz i Altaba, Hedgehog signaling and the Gli code in stem cells, cancer, and metastases. Sci. Signal. 4, pt9 (2011).
    • (2011) Sci. Signal. , vol.4 , Issue.PART9
    • Ruiz I Altaba, A.1
  • 5
    • 0036406843 scopus 로고    scopus 로고
    • Hedgehog signaling and human disease
    • A. E. Bale, Hedgehog signaling and human disease. Annu. Rev. Genomics Hum. Genet. 3, 47-65 (2002).
    • (2002) Annu. Rev. Genomics Hum. Genet. , vol.3 , pp. 47-65
    • Bale, A.E.1
  • 6
    • 52149110383 scopus 로고    scopus 로고
    • Cancer: Hedgehog's other great trick
    • T. Curran, J. M. Ng, Cancer: Hedgehog's other great trick. Nature 455, 293-294 (2008).
    • (2008) Nature , vol.455 , pp. 293-294
    • Curran, T.1    Ng, J.M.2
  • 7
    • 77649337790 scopus 로고    scopus 로고
    • Hedgehog beyond medulloblastoma and basal cell carcinoma
    • S. Teglund, R. Toftgård, Hedgehog beyond medulloblastoma and basal cell carcinoma. Biochim. Biophys. Acta 1805, 181-208 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1805 , pp. 181-208
    • Teglund, S.1    Toftgård, R.2
  • 8
    • 33751549095 scopus 로고    scopus 로고
    • Targeting the Hedgehog pathway in cancer
    • L. L. Rubin, F. J. de Sauvage, Targeting the Hedgehog pathway in cancer. Nat. Rev. Drug Discov. 5, 1026-1033 (2006).
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 1026-1033
    • Rubin, L.L.1    De Sauvage, F.J.2
  • 9
    • 80955181031 scopus 로고    scopus 로고
    • The Hedgehog's tale: Developing strategies for targeting cancer
    • J. M. Ng, T. Curran, The Hedgehog's tale: Developing strategies for targeting cancer. Nat. Rev. Cancer 11, 493-501 (2011).
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 493-501
    • Ng, J.M.1    Curran, T.2
  • 10
    • 84859321979 scopus 로고    scopus 로고
    • Hedgehog inhibitor gets landmark skin cancer approval, but questions remain for wider potential
    • M. Guha, Hedgehog inhibitor gets landmark skin cancer approval, but questions remain for wider potential. Nat. Rev. Drug Discov. 11, 257-258 (2012).
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 257-258
    • Guha, M.1
  • 11
    • 0019133661 scopus 로고
    • Mutations affecting segment number and polarity in Drosophila
    • C. Nüsslein-Volhard, E. Wieschaus, Mutations affecting segment number and polarity in Drosophila. Nature 287, 795-801 (1980).
    • (1980) Nature , vol.287 , pp. 795-801
    • Nüsslein-Volhard, C.1    Wieschaus, E.2
  • 12
    • 0021930186 scopus 로고
    • Parasegments and compartments in the Drosophila embryo
    • A. Martinez-Arias, P. A. Lawrence, Parasegments and compartments in the Drosophila embryo. Nature 313, 639-642 (1985).
    • (1985) Nature , vol.313 , pp. 639-642
    • Martinez-Arias, A.1    Lawrence, P.A.2
  • 13
    • 0027817446 scopus 로고
    • Genetic analysis of hedgehog signalling in the Drosophila embryo
    • A. J. Forbes, Y. Nakano, A. M. Taylor, P. W. Ingham, Genetic analysis of hedgehog signalling in the Drosophila embryo. Dev. Suppl. 1993, 115-124 (1993).
    • (1993) Dev. Suppl. , vol.1993 , pp. 115-124
    • Forbes, A.J.1    Nakano, Y.2    Taylor, A.M.3    Ingham, P.W.4
  • 15
    • 0034865315 scopus 로고    scopus 로고
    • The development of the Drosophila genital disc
    • L. Sánchez, I. Guerrero, The development of the Drosophila genital disc. Bioessays 23, 698-707 (2001).
    • (2001) Bioessays , vol.23 , pp. 698-707
    • Sánchez, L.1    Guerrero, I.2
  • 16
    • 0029320637 scopus 로고
    • Morphogenetic signalling. Responses to hedgehog
    • D. Kalderon, Morphogenetic signalling. Responses to hedgehog. Curr. Biol. 5, 580-582 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 580-582
    • Kalderon, D.1
  • 17
    • 0029278637 scopus 로고
    • Compartments and appendage development in Drosophila
    • S. S. Blair, Compartments and appendage development in Drosophila. Bioessays 17, 299-309 (1995).
    • (1995) Bioessays , vol.17 , pp. 299-309
    • Blair, S.S.1
  • 18
    • 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
  • 19
    • 0029896212 scopus 로고    scopus 로고
    • Sending and receiving the hedgehog signal: Control by the Drosophila Gli protein Cubitus interruptus
    • M. Domínguez, M. Brunner, E. Hafen, K. Basler, Sending and receiving the hedgehog signal: Control by the Drosophila Gli protein Cubitus interruptus. Science 272, 1621-1625 (1996).
    • (1996) Science , vol.272 , pp. 1621-1625
    • Domínguez, M.1    Brunner, M.2    Hafen, E.3    Basler, K.4
  • 21
    • 42049104913 scopus 로고    scopus 로고
    • The adventures of sonic hedgehog in development and repair. III. Hedgehog processing and biological activity
    • S. F. Farzan, S. Singh, N. S. Schilling, D. J. Robbins, The adventures of sonic hedgehog in development and repair. III. Hedgehog processing and biological activity. Am. J. Physiol. Gastrointest. Liver Physiol. 294, G844-G849 (2008).
    • (2008) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.294
    • Farzan, S.F.1    Singh, S.2    Schilling, N.S.3    Robbins, D.J.4
  • 22
    • 2942742564 scopus 로고    scopus 로고
    • Novel lipid modifications of secreted protein signals
    • R. K. Mann, P. A. Beachy, Novel lipid modifications of secreted protein signals. Annu. Rev. Biochem. 73, 891-923 (2004).
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 891-923
    • Mann, R.K.1    Beachy, P.A.2
  • 24
    • 0036008549 scopus 로고    scopus 로고
    • Sonic Hedgehog as a mediator of long-range signaling
    • J. A. Goetz, L. M. Suber, X. Zeng, D. J. Robbins, Sonic Hedgehog as a mediator of long-range signaling. Bioessays 24, 157-165 (2002).
    • (2002) Bioessays , vol.24 , pp. 157-165
    • Goetz, J.A.1    Suber, L.M.2    Zeng, X.3    Robbins, D.J.4
  • 25
    • 81855183845 scopus 로고    scopus 로고
    • Barcoding Hedgehog for intracellular transport
    • T. B. Kornberg, Barcoding Hedgehog for intracellular transport. Sci. Signal. 4, pe44 (2011).
    • (2011) Sci. Signal. , vol.4
    • Kornberg, T.B.1
  • 26
    • 33845873602 scopus 로고    scopus 로고
    • A conserved mechanism of Hedgehog gradient formation by lipid modifications
    • I. Guerrero, C. Chiang, A conserved mechanism of Hedgehog gradient formation by lipid modifications. Trends Cell Biol. 17, 1-5 (2007).
    • (2007) Trends Cell Biol. , vol.17 , pp. 1-5
    • Guerrero, I.1    Chiang, C.2
  • 27
    • 79953161898 scopus 로고    scopus 로고
    • Hedgehog morphogen: From secretion to reception
    • A. Gallet, Hedgehog morphogen: From secretion to reception. Trends Cell Biol. 21, 238-246 (2011).
    • (2011) Trends Cell Biol. , vol.21 , pp. 238-246
    • Gallet, A.1
  • 28
    • 64849094028 scopus 로고    scopus 로고
    • Hedgehog signalling: Emerging evidence for non-canonical pathways
    • D. Jenkins, Hedgehog signalling: Emerging evidence for non-canonical pathways. Cell. Signal. 21, 1023-1034 (2009).
    • (2009) Cell. Signal. , vol.21 , pp. 1023-1034
    • Jenkins, D.1
  • 30
    • 0029948270 scopus 로고    scopus 로고
    • Biochemical evidence that patched is the Hedgehog receptor
    • V. Marigo, R. A. Davey, Y. Zuo, J. M. Cunningham, C. J. Tabin, Biochemical evidence that patched is the Hedgehog receptor. Nature 384, 176-179 (1996).
    • (1996) Nature , vol.384 , pp. 176-179
    • Marigo, V.1    Davey, R.A.2    Zuo, Y.3    Cunningham, J.M.4    Tabin, C.J.5
  • 32
    • 0024468746 scopus 로고
    • The Drosophila patched gene encodes a putative membrane protein required for segmental patterning
    • J. E. Hooper, M. P. Scott, The Drosophila patched gene encodes a putative membrane protein required for segmental patterning. Cell 59, 751-765 (1989).
    • (1989) Cell , vol.59 , pp. 751-765
    • Hooper, J.E.1    Scott, M.P.2
  • 33
    • 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
  • 34
    • 0025815911 scopus 로고
    • Role of the Drosophila patched gene in positional signalling
    • P. W. Ingham, A. M. Taylor, Y. Nakano, Role of the Drosophila patched gene in positional signalling. Nature 353, 184-187 (1991).
    • (1991) Nature , vol.353 , pp. 184-187
    • Ingham, P.W.1    Taylor, A.M.2    Nakano, Y.3
  • 35
    • 79960956450 scopus 로고    scopus 로고
    • Efflux pumps of the resistance-nodulation-division family: A perspective of their structure, function, and regulation in gram-negative bacteria
    • M. D. Routh, Y. Zalucki, C.-C. Su, F. Long, Q. Zhang, W. M. Shafer, E. W. Yu, Efflux pumps of the resistance-nodulation-division family: A perspective of their structure, function, and regulation in gram-negative bacteria. Adv. Enzymol. Relat. Areas Mol. Biol. 77, 109-146 (2011).
    • (2011) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.77 , pp. 109-146
    • Routh, M.D.1    Zalucki, Y.2    Su, C.-C.3    Long, F.4    Zhang, Q.5    Shafer, W.M.6    Yu, E.W.7
  • 36
    • 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
  • 37
    • 0037083492 scopus 로고    scopus 로고
    • Distinct consequences of sterol sensor mutations in Drosophila and mouse patched homologs
    • R. L. Johnson, L. Zhou, E. C. Bailey, Distinct consequences of sterol sensor mutations in Drosophila and mouse patched homologs. Dev. Biol. 242, 224-235 (2002).
    • (2002) Dev. Biol. , vol.242 , pp. 224-235
    • Johnson, R.L.1    Zhou, L.2    Bailey, E.C.3
  • 38
    • 0036534286 scopus 로고    scopus 로고
    • The sterolsensing domain: Multiple families, a unique role?
    • P. E. Kuwabara, M. Labouesse, The sterolsensing domain: Multiple families, a unique role? Trends Genet. 18, 193-201 (2002).
    • (2002) Trends Genet. , vol.18 , pp. 193-201
    • Kuwabara, P.E.1    Labouesse, M.2
  • 39
    • 0035901616 scopus 로고    scopus 로고
    • The sterol-sensing domain of Patched protein seems to control Smoothened activity through Patched vesicular trafficking
    • V. Martín, G. Carrillo, C. Torroja, I. Guerrero, The sterol-sensing domain of Patched protein seems to control Smoothened activity through Patched vesicular trafficking. Curr. Biol. 11, 601-607 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 601-607
    • Martín, V.1    Carrillo, G.2    Torroja, C.3    Guerrero, I.4
  • 40
    • 0035901572 scopus 로고    scopus 로고
    • Mutations in the sterol-sensing domain of Patched suggest a role for vesicular trafficking in Smoothened regulation
    • H. Strutt, C. Thomas, Y. Nakano, D. Stark, B. Neave, A. M. Taylor, P. W. Ingham, Mutations in the sterol-sensing domain of Patched suggest a role for vesicular trafficking in Smoothened regulation. Curr. Biol. 11, 608-613 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 608-613
    • Strutt, H.1    Thomas, C.2    Nakano, Y.3    Stark, D.4    Neave, B.5    Taylor, A.M.6    Ingham, P.W.7
  • 41
    • 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
  • 43
    • 0031989439 scopus 로고    scopus 로고
    • Ptch2, a second mouse Patched gene is coexpressed with Sonic hedgehog
    • J. Motoyama, T. Takabatake, K. Takeshima, C. Hui, Ptch2, a second mouse Patched gene is coexpressed with Sonic hedgehog. Nat. Genet. 18, 104-106 (1998).
    • (1998) Nat. Genet. , vol.18 , pp. 104-106
    • Motoyama, J.1    Takabatake, T.2    Takeshima, K.3    Hui, C.4
  • 44
    • 0033557853 scopus 로고    scopus 로고
    • PTCH2, a novel human patched gene, undergoing alternative splicing and up-regulated in basal cell carcinomas
    • P. G. Zaphiropoulos, A. B. Undén, F. Rahnama, R. E. Hollingsworth, R. Toftgård, PTCH2, a novel human patched gene, undergoing alternative splicing and up-regulated in basal cell carcinomas. Cancer Res. 59, 787-792 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 787-792
    • Zaphiropoulos, P.G.1    Undén, A.B.2    Rahnama, F.3    Hollingsworth, R.E.4    Toftgård, R.5
  • 45
    • 0029975823 scopus 로고    scopus 로고
    • Conservation in hedgehog signaling: Induction of a chicken patched homolog by Sonic hedgehog in the developing limb
    • V. Marigo, M. P. Scott, R. L. Johnson, L. V. Goodrich, C. J. Tabin, Conservation in hedgehog signaling: Induction of a chicken patched homolog by Sonic hedgehog in the developing limb. Development 122, 1225-1233 (1996).
    • (1996) Development , vol.122 , pp. 1225-1233
    • Marigo, V.1    Scott, M.P.2    Johnson, R.L.3    Goodrich, L.V.4    Tabin, C.J.5
  • 46
    • 0029843937 scopus 로고    scopus 로고
    • Regulation of patched by sonic hedgehog in the developing neural tube
    • V. Marigo, C. J. Tabin, Regulation of patched by sonic hedgehog in the developing neural tube. Proc. Natl. Acad. Sci. U.S.A. 93, 9346-9351 (1996).
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 9346-9351
    • Marigo, V.1    Tabin, C.J.2
  • 47
    • 0030027059 scopus 로고    scopus 로고
    • Conservation of the hedgehog/patched signaling pathway from flies to mice: Induction of a mouse patched gene by Hedgehog
    • L. V. Goodrich, R. L. Johnson, L. Milenkovic, J. A. McMahon, M. P. Scott, Conservation of the hedgehog/patched signaling pathway from flies to mice: Induction of a mouse patched gene by Hedgehog. Genes Dev. 10, 301-312 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 301-312
    • Goodrich, L.V.1    Johnson, R.L.2    Milenkovic, L.3    McMahon, J.A.4    Scott, M.P.5
  • 48
    • 77956814604 scopus 로고    scopus 로고
    • Interactions between Hedgehog proteins and their binding partners come into view
    • P. A. Beachy, S. G. Hymowitz, R. A. Lazarus, D. J. Leahy, C. Siebold, Interactions between Hedgehog proteins and their binding partners come into view. Genes Dev. 24, 2001-2012 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 2001-2012
    • Beachy, P.A.1    Hymowitz, S.G.2    Lazarus, R.A.3    Leahy, D.J.4    Siebold, C.5
  • 49
  • 50
    • 33646035770 scopus 로고    scopus 로고
    • The ihog cell-surface proteins bind Hedgehog and mediate pathway activation
    • S. Yao, L. Lum, P. Beachy, The ihog cell-surface proteins bind Hedgehog and mediate pathway activation. Cell 125, 343-357 (2006).
    • (2006) Cell , vol.125 , pp. 343-357
    • Yao, S.1    Lum, L.2    Beachy, P.3
  • 51
    • 73549083198 scopus 로고    scopus 로고
    • Genetic and biochemical definition of the Hedgehog receptor
    • X. Zheng, R. K. Mann, N. Sever, P. A. Beachy, Genetic and biochemical definition of the Hedgehog receptor. Genes Dev. 24, 57-71 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 57-71
    • Zheng, X.1    Mann, R.K.2    Sever, N.3    Beachy, P.A.4
  • 53
    • 33646103902 scopus 로고    scopus 로고
    • The cell surface membrane proteins Cdo and Boc are components and targets of the Hedgehog signaling pathway and feedback network in mice
    • T. Tenzen, B. L. Allen, F. Cole, J. S. Kang, R. S. Krauss, A. P. McMahon, The cell surface membrane proteins Cdo and Boc are components and targets of the Hedgehog signaling pathway and feedback network in mice. Dev. Cell 10, 647-656 (2006).
    • (2006) Dev. Cell , vol.10 , pp. 647-656
    • Tenzen, T.1    Allen, B.L.2    Cole, F.3    Kang, J.S.4    Krauss, R.S.5    McMahon, A.P.6
  • 54
    • 33646120095 scopus 로고    scopus 로고
    • Cdo functions at multiple points in the Sonic Hedgehog pathway, and Cdo-deficient mice accurately model human holoprosencephaly
    • W. Zhang, J. S. Kang, F. Cole, M. J. Yi, R. S. Krauss, Cdo functions at multiple points in the Sonic Hedgehog pathway, and Cdo-deficient mice accurately model human holoprosencephaly. Dev. Cell 10, 657-665 (2006).
    • (2006) Dev. Cell , vol.10 , pp. 657-665
    • Zhang, W.1    Kang, J.S.2    Cole, F.3    Yi, M.J.4    Krauss, R.S.5
  • 55
    • 34249007279 scopus 로고    scopus 로고
    • The Hedgehog-binding proteins Gas1 and Cdo cooperate to positively regulate Shh signaling during mouse development
    • B. L. Allen, T. Tenzen, A. P. McMahon, The Hedgehog-binding proteins Gas1 and Cdo cooperate to positively regulate Shh signaling during mouse development. Genes Dev. 21, 1244-1257 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1244-1257
    • Allen, B.L.1    Tenzen, T.2    McMahon, A.P.3
  • 56
    • 79958207835 scopus 로고    scopus 로고
    • Overlapping roles and collective requirement for the coreceptors GAS1, CDO, and BOC in SHH pathway function
    • B. L. Allen, J. Y. Song, L. Izzi, I. W. Althaus, J. S. Kang, F. Charron, R. S. Krauss, A. P. McMahon, Overlapping roles and collective requirement for the coreceptors GAS1, CDO, and BOC in SHH pathway function. Dev. Cell 20, 775-787 (2011).
    • (2011) Dev. Cell , vol.20 , pp. 775-787
    • Allen, B.L.1    Song, J.Y.2    Izzi, L.3    Althaus, I.W.4    Kang, J.S.5    Charron, F.6    Krauss, R.S.7    McMahon, A.P.8
  • 58
    • 79956110764 scopus 로고    scopus 로고
    • Boc modifies the holoprosencephaly spectrum of Cdo mutant mice
    • W. Zhang, M. Hong, G. U. Bae, J. S. Kang, R. S. Krauss, Boc modifies the holoprosencephaly spectrum of Cdo mutant mice. Dis. Model Mech. 4, 368-380 (2011).
    • (2011) Dis. Model Mech. , vol.4 , pp. 368-380
    • Zhang, W.1    Hong, M.2    Bae, G.U.3    Kang, J.S.4    Krauss, R.S.5
  • 59
    • 77955298373 scopus 로고    scopus 로고
    • All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner
    • J. M. Kavran, M. D. Ward, O. O. Oladosu, S. Mulepati, D. J. Leahy, All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner. J. Biol. Chem. 285, 24584-24590 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 24584-24590
    • Kavran, J.M.1    Ward, M.D.2    Oladosu, O.O.3    Mulepati, S.4    Leahy, D.J.5
  • 60
    • 0035949695 scopus 로고    scopus 로고
    • Evidence that the WNT-inducible growth arrest-specific gene 1 encodes an antagonist of sonic hedgehog signaling in the somite
    • C. S. Lee, L. Buttitta, C. M. Fan, Evidence that the WNT-inducible growth arrest-specific gene 1 encodes an antagonist of sonic hedgehog signaling in the somite. Proc. Natl. Acad. Sci. U.S.A. 98, 11347-11352 (2001).
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 11347-11352
    • Lee, C.S.1    Buttitta, L.2    Fan, C.M.3
  • 61
    • 54049122121 scopus 로고    scopus 로고
    • The mode of Hedgehog binding to Ihog homologues is not conserved across different phyla
    • J. S. McLellan, X. Zheng, G. Hauk, R. Ghirlando, P. A. Beachy, D. J. Leahy, The mode of Hedgehog binding to Ihog homologues is not conserved across different phyla. Nature 455, 979-983(2008).
    • (2008) Nature , vol.455 , pp. 979-983
    • McLellan, J.S.1    Zheng, X.2    Hauk, G.3    Ghirlando, R.4    Beachy, P.A.5    Leahy, D.J.6
  • 62
    • 80051665525 scopus 로고    scopus 로고
    • Mutations in CDON, encoding a hedgehog receptor, result in holoprosencephaly and defective interactions with other hedgehog receptors
    • G. U. Bae, S. Domené, E. Roessler, K. Schachter, J. S. Kang, M. Muenke, R. S. Krauss, Mutations in CDON, encoding a hedgehog receptor, result in holoprosencephaly and defective interactions with other hedgehog receptors. Am. J. Hum. Genet. 89, 231-240 (2011).
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 231-240
    • Bae, G.U.1    Domené, S.2    Roessler, E.3    Schachter, K.4    Kang, J.S.5    Muenke, M.6    Krauss, R.S.7
  • 63
    • 67749097999 scopus 로고    scopus 로고
    • A sonic hedgehog missense mutation associated with holoprosencephaly causes defective binding to GAS1
    • D. C. Martinelli, C. M. Fan, A sonic hedgehog missense mutation associated with holoprosencephaly causes defective binding to GAS1. J. Biol. Chem. 284, 19169-19172 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 19169-19172
    • Martinelli, D.C.1    Fan, C.M.2
  • 64
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • K. Kristiansen, Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103, 21-80 (2004).
    • (2004) Pharmacol. Ther. , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 65
    • 0029784223 scopus 로고    scopus 로고
    • Smoothened encodes a receptor-like serpentine protein required for hedgehog signalling
    • M. van den Heuvel, P. W. Ingham, smoothened encodes a receptor-like serpentine protein required for hedgehog signalling. Nature 382, 547-551 (1996).
    • (1996) Nature , vol.382 , pp. 547-551
    • Van Den Heuvel, M.1    Ingham, P.W.2
  • 66
    • 0030602796 scopus 로고    scopus 로고
    • The Drosophila smoothened gene encodes a seven-pass membrane protein, a putative receptor for the hedgehog signal
    • J. Alcedo, M. Ayzenzon, T. Von Ohlen, M. Noll, J. E. Hooper, The Drosophila smoothened gene encodes a seven-pass membrane protein, a putative receptor for the hedgehog signal. Cell 86, 221-232 (1996).
    • (1996) Cell , vol.86 , pp. 221-232
    • Alcedo, J.1    Ayzenzon, M.2    Von Ohlen, T.3    Noll, M.4    Hooper, J.E.5
  • 67
    • 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
  • 68
    • 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
  • 69
    • 62449174504 scopus 로고    scopus 로고
    • Selective translocation of intracellular Smoothened to the primary cilium in response to Hedgehog pathway modulation
    • Y. Wang, Z. Zhou, C. T. Walsh, A. P. McMahon, Selective translocation of intracellular Smoothened to the primary cilium in response to Hedgehog pathway modulation. Proc. Natl. Acad. Sci. U.S.A. 106, 2623-2628 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2623-2628
    • Wang, Y.1    Zhou, Z.2    Walsh, C.T.3    McMahon, A.P.4
  • 71
    • 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
  • 72
    • 79959804711 scopus 로고    scopus 로고
    • Sonic Hedgehog dependent phosphorylation by CK1á 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 CK1á 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
  • 73
    • 78549236202 scopus 로고    scopus 로고
    • Casein kinase 2 promotes Hedgehog signaling by regulating both smoothened and Cubitus interruptus
    • H. Jia, Y. Liu, R. Xia, C. Tong, T. Yue, J. Jiang, J. Jia, Casein kinase 2 promotes Hedgehog signaling by regulating both smoothened and Cubitus interruptus. J. Biol. Chem. 285, 37218-37226 (2010).
    • (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
  • 74
    • 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
  • 75
    • 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
  • 76
  • 77
    • 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
  • 79
    • 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
  • 80
    • 84863012620 scopus 로고    scopus 로고
    • USP8 promotes smoothened signaling by preventing its ubiquitination and changing its subcellular localization
    • R. Xia, H. Jia, J. Fan, Y. Liu, J. Jia, USP8 promotes smoothened signaling by preventing its ubiquitination and changing its subcellular localization. PLoS Biol. 10, e1001238 (2012).
    • (2012) PLoS Biol. , vol.10
    • Xia, R.1    Jia, H.2    Fan, J.3    Liu, Y.4    Jia, J.5
  • 84
    • 57049085407 scopus 로고    scopus 로고
    • G protein Galphai 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 Galphai 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
  • 85
    • 0035398487 scopus 로고    scopus 로고
    • G-protein-coupled receptors and signaling networks: Emerging paradigms
    • M. J. Marinissen, J. S. Gutkind, G-protein-coupled receptors and signaling networks: Emerging paradigms. Trends Pharmacol. Sci. 22, 368-376 (2001).
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 368-376
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 86
    • 0032756914 scopus 로고    scopus 로고
    • Proteolysis of cubitus interruptus in Drosophila requires phosphorylation by protein kinase A
    • M. A. Price, D. Kalderon, Proteolysis of cubitus interruptus in Drosophila requires phosphorylation by protein kinase A. Development 126, 4331-4339 (1999).
    • (1999) Development , vol.126 , pp. 4331-4339
    • Price, M.A.1    Kalderon, D.2
  • 87
    • 0032478107 scopus 로고    scopus 로고
    • Protein kinase A directly regulates the activity and proteolysis of cubitus interruptus
    • Y. Chen, N. Gallaher, R. H. Goodman, S. M. Smolik, Protein kinase A directly regulates the activity and proteolysis of cubitus interruptus. Proc. Natl. Acad. Sci. U.S.A. 95, 2349-2354 (1998).
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2349-2354
    • Chen, Y.1    Gallaher, N.2    Goodman, R.H.3    Smolik, S.M.4
  • 88
    • 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
  • 89
    • 0034681266 scopus 로고    scopus 로고
    • Hedgehogregulated processing of Gli3 produces an anterior/ posterior repressor gradient in the developing vertebrate limb
    • B. Wang, J. F. Fallon, P. A. Beachy, Hedgehogregulated 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
  • 90
    • 0031051444 scopus 로고    scopus 로고
    • Signalling functions and biochemical properties of pertussis toxin-resistant G-proteins
    • T. A. Fields, P. J. Casey, Signalling functions and biochemical properties of pertussis toxin-resistant G-proteins. Biochem. J. 321, 561-571 (1997).
    • (1997) Biochem. J. , vol.321 , pp. 561-571
    • Fields, T.A.1    Casey, P.J.2
  • 91
    • 0032519906 scopus 로고    scopus 로고
    • The effect of pertussis toxin on zebrafish development: A possible role for inhibitory G-proteins in hedgehog signaling
    • M. Hammerschmidt, A. P. McMahon, The effect of pertussis toxin on zebrafish development: A possible role for inhibitory G-proteins in hedgehog signaling. Dev. Biol. 194, 166-171 (1998).
    • (1998) Dev. Biol. , vol.194 , pp. 166-171
    • Hammerschmidt, M.1    McMahon, A.P.2
  • 92
    • 0034713934 scopus 로고    scopus 로고
    • Smoothened activates Galphaimediated signaling in frog melanophores
    • D. L. DeCamp, T. M. Thompson, F. J. de Sauvage, M. R. Lerner, Smoothened activates Galphaimediated signaling in frog melanophores. J. Biol. Chem. 275, 26322-26327 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26322-26327
    • DeCamp, D.L.1    Thompson, T.M.2    De Sauvage, F.J.3    Lerner, M.R.4
  • 93
    • 79953138390 scopus 로고    scopus 로고
    • Sonic Hedgehog-induced proliferation requires specific Gá inhibitory proteins
    • M. Barzi, D. Kostrz, A. Menendez, S. Pons, Sonic Hedgehog-induced proliferation requires specific Gá inhibitory proteins. J. Biol. Chem. 286, 8067-8074 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 8067-8074
    • Barzi, M.1    Kostrz, D.2    Menendez, A.3    Pons, S.4
  • 94
    • 49049108307 scopus 로고    scopus 로고
    • The decoupling of Smoothened from Galphai proteins has little effect on Gli3 protein processing and Hedgehog-regulated chick neural tube patterning
    • W. C. Low, C. Wang, Y. Pan, X. Y. Huang, J. K. Chen, B. Wang, The decoupling of Smoothened from Galphai proteins has little effect on Gli3 protein processing and Hedgehog-regulated chick neural tube patterning. Dev. Biol. 321, 188-196 (2008).
    • (2008) Dev. Biol. , vol.321 , pp. 188-196
    • Low, W.C.1    Wang, C.2    Pan, Y.3    Huang, X.Y.4    Chen, J.K.5    Wang, B.6
  • 96
    • 0036829397 scopus 로고    scopus 로고
    • Inhibition of Hedgehog signaling by direct binding of cyclopamine to Smoothened
    • J. K. Chen, J. Taipale, M. K. Cooper, P. A. Beachy, Inhibition of Hedgehog signaling by direct binding of cyclopamine to Smoothened. Genes Dev. 16, 2743-2748 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2743-2748
    • Chen, J.K.1    Taipale, J.2    Cooper, M.K.3    Beachy, P.A.4
  • 98
    • 33744788672 scopus 로고    scopus 로고
    • Oxysterols stimulate Sonic hedgehog signal transduction and proliferation of medulloblastoma cells
    • R. B. Corcoran, M. P. Scott, Oxysterols stimulate Sonic hedgehog signal transduction and proliferation of medulloblastoma cells. Proc. Natl. Acad. Sci. U.S.A. 103, 8408-8413 (2006).
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8408-8413
    • Corcoran, R.B.1    Scott, M.P.2
  • 99
    • 34247844371 scopus 로고    scopus 로고
    • Oxysterols are novel activators of the hedgehog signaling pathway in pluripotent mesenchymal cells
    • J. R. Dwyer, N. Sever, M. Carlson, S. F. Nelson, P. A. Beachy, F. Parhami, Oxysterols are novel activators of the hedgehog signaling pathway in pluripotent mesenchymal cells. J. Biol. Chem. 282, 8959-8968 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 8959-8968
    • Dwyer, J.R.1    Sever, N.2    Carlson, M.3    Nelson, S.F.4    Beachy, P.A.5    Parhami, F.6
  • 102
    • 0033230757 scopus 로고    scopus 로고
    • Ci: A complex transducer of the hedgehog signal
    • P. Aza-Blanc, T. B. Kornberg, Ci: A complex transducer of the hedgehog signal. Trends Genet. 15, 458-462 (1999).
    • (1999) Trends Genet. , vol.15 , pp. 458-462
    • Aza-Blanc, P.1    Kornberg, T.B.2
  • 103
    • 0025331133 scopus 로고
    • Cloning and characterization of the segment polarity gene cubitus interruptus Dominant of Drosophila
    • T. V. Orenic, D. C. Slusarski, K. L. Kroll, R. A. Holmgren, Cloning and characterization of the segment polarity gene cubitus interruptus Dominant of Drosophila. Genes Dev. 4, 1053-1067 (1990).
    • (1990) Genes Dev. , vol.4 , pp. 1053-1067
    • Orenic, T.V.1    Slusarski, D.C.2    Kroll, K.L.3    Holmgren, R.A.4
  • 104
    • 0025283924 scopus 로고
    • Repression of ci-D in posterior compartments of Drosophila by engrailed
    • S. Eaton, T. B. Kornberg, Repression of ci-D in posterior compartments of Drosophila by engrailed. Genes Dev. 4, 1068-1077 (1990).
    • (1990) Genes Dev. , vol.4 , pp. 1068-1077
    • Eaton, S.1    Kornberg, T.B.2
  • 105
    • 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. A. Ramírez-Weber, M. P. Laget, C. Schwartz, T. B. 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.A.2    Laget, M.P.3    Schwartz, C.4    Kornberg, T.B.5
  • 106
    • 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
  • 107
    • 0033582908 scopus 로고    scopus 로고
    • Hedgehog controls limb development by regulating the activities of distinct transcriptional activator and repressor forms of Cubitus interruptus
    • N. Méthot, K. Basler, Hedgehog controls limb development by regulating the activities of distinct transcriptional activator and repressor forms of Cubitus interruptus. Cell 96, 819-831 (1999).
    • (1999) Cell , vol.96 , pp. 819-831
    • Méthot, N.1    Basler, K.2
  • 108
    • 0343431516 scopus 로고    scopus 로고
    • The repressor and activator forms of Cubitus interruptus control Hedgehog target genes through common generic gli-binding sites
    • B. Müller, K. Basler, The repressor and activator forms of Cubitus interruptus control Hedgehog target genes through common generic gli-binding sites. Development 127, 2999-3007 (2000).
    • (2000) Development , vol.127 , pp. 2999-3007
    • Müller, B.1    Basler, K.2
  • 109
    • 78149236053 scopus 로고    scopus 로고
    • Hedgehog targets in the Drosophila embryo and the mechanisms that generate tissue-specific outputs of Hedgehog signaling
    • B. Biehs, K. Kechris, S. Liu, T. B. Kornberg, Hedgehog targets in the Drosophila embryo and the mechanisms that generate tissue-specific outputs of Hedgehog signaling. Development 137, 3887-3898 (2010).
    • (2010) Development , vol.137 , pp. 3887-3898
    • Biehs, B.1    Kechris, K.2    Liu, S.3    Kornberg, T.B.4
  • 110
    • 0031437362 scopus 로고    scopus 로고
    • Hedgehog signaling regulates transcription through Gli/Ci binding sites in the wingless enhancer
    • T. Von Ohlen, J. E. Hooper, Hedgehog signaling regulates transcription through Gli/Ci binding sites in the wingless enhancer. Mech. Dev. 68, 149-156 (1997).
    • (1997) Mech. Dev. , vol.68 , pp. 149-156
    • Von Ohlen, T.1    Hooper, J.E.2
  • 111
    • 0031443718 scopus 로고    scopus 로고
    • Hedgehog signalling: Ci complex cuts and clasps
    • D. Kalderon, Hedgehog signalling: Ci complex cuts and clasps. Curr. Biol. 7, R759-R762 (1997).
    • (1997) Curr. Biol. , vol.7
    • Kalderon, D.1
  • 112
    • 33751208606 scopus 로고    scopus 로고
    • Regulation of Hh/Gli signaling by dual ubiquitin pathways
    • J. Jiang, Regulation of Hh/Gli signaling by dual ubiquitin pathways. Cell Cycle 5, 2457-2463 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 2457-2463
    • Jiang, J.1
  • 113
    • 70549100903 scopus 로고    scopus 로고
    • Regulation of cell death by the ubiquitin-proteasome system
    • M. Bader, H. Steller, Regulation of cell death by the ubiquitin-proteasome system. Curr. Opin. Cell Biol. 21, 878-884 (2009).
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 878-884
    • Bader, M.1    Steller, H.2
  • 114
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • T. Ravid, M. Hochstrasser, Diversity of degradation signals in the ubiquitin-proteasome system. Nat. Rev. Mol. Cell Biol. 9, 679-690 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 115
    • 33646893705 scopus 로고    scopus 로고
    • A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor
    • Q. Zhang, L. Zhang, B. Wang, C. Y. Ou, C. T. Chien, J. Jiang, A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor. Dev. Cell 10, 719-729 (2006).
    • (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
  • 116
    • 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
  • 117
    • 28444449828 scopus 로고    scopus 로고
    • Phosphorylation by double-time/CKIepsilon and CKIalpha targets cubitus interruptus for Slimb/beta-TRCP-mediated proteolytic processing
    • J. Jia, L. Zhang, Q. Zhang, C. Tong, B. Wang, F. Hou, K. Amanai, J. Jiang, Phosphorylation by double-time/CKIepsilon and CKIalpha targets cubitus interruptus for Slimb/beta-TRCP-mediated 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
  • 118
    • 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
  • 119
    • 34848892735 scopus 로고    scopus 로고
    • Regulation of Ci-SCFSlimb binding, Ci proteolysis, and hedgehog pathway activity by Ci phosphorylation
    • M. G. Smelkinson, Q. Zhou, D. Kalderon, Regulation of Ci-SCFSlimb 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
  • 120
    • 30044442183 scopus 로고    scopus 로고
    • Processing of the Drosophila hedgehog signaling effector Ci-155 to the repressor Ci-75 is mediated by direct binding to the SCF component Slimb
    • M. G. Smelkinson, D. Kalderon, Processing of the Drosophila hedgehog signaling effector Ci-155 to the repressor Ci-75 is mediated by direct binding to the SCF component Slimb. Curr. Biol. 16, 110-116 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 110-116
    • Smelkinson, M.G.1    Kalderon, D.2
  • 121
    • 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
  • 122
    • 51349156246 scopus 로고    scopus 로고
    • A unique protection signal in Cubitus interruptus prevents its complete proteasomal degradation
    • Y. Wang, M. A. Price, A unique protection signal in Cubitus interruptus prevents its complete proteasomal degradation. Mol. Cell. Biol. 28, 5555- 5568 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5555-5568
    • Wang, Y.1    Price, M.A.2
  • 123
    • 75849129292 scopus 로고    scopus 로고
    • Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase
    • Q. Zhang, Q. Shi, Y. Chen, T. Yue, S. Li, B. Wang, J. Jiang, Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase. Proc. Natl. Acad. Sci. U.S.A. 106, 21191-21196 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21191-21196
    • Zhang, Q.1    Shi, Q.2    Chen, Y.3    Yue, T.4    Li, S.5    Wang, B.6    Jiang, J.7
  • 124
    • 33646875414 scopus 로고    scopus 로고
    • Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus
    • D. Kent, E. W. Bush, J. E. Hooper, Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus. Development 133, 2001- 2010 (2006).
    • (2006) Development , vol.133 , pp. 2001-2010
    • Kent, D.1    Bush, E.W.2    Hooper, J.E.3
  • 125
    • 0033761448 scopus 로고    scopus 로고
    • Expression of the vertebrate Gli proteins in Drosophila reveals a distribution of activator and repressor activities
    • P. Aza-Blanc, H. Y. Lin, A. Ruiz i Altaba, T. B. Kornberg, Expression of the vertebrate Gli proteins in Drosophila reveals a distribution of activator and repressor activities. Development 127, 4293- 4301 (2000).
    • (2000) Development , vol.127 , pp. 4293-4301
    • Aza-Blanc, P.1    Lin, H.Y.2    Ruiz I Altaba, A.3    Kornberg, T.B.4
  • 126
    • 0033581926 scopus 로고    scopus 로고
    • Distinct and regulated activities of human Gli proteins in Drosophila
    • C. von Mering, K. Basler, Distinct and regulated activities of human Gli proteins in Drosophila. Curr. Biol. 9, 1319-1322 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1319-1322
    • Von Mering, C.1    Basler, K.2
  • 127
    • 0033583035 scopus 로고    scopus 로고
    • Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3
    • P. Dai, H. Akimaru, Y. Tanaka, T. Maekawa, M. Nakafuku, S. Ishii, Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3. J. Biol. Chem. 274, 8143-8152 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8143-8152
    • Dai, P.1    Akimaru, H.2    Tanaka, Y.3    Maekawa, T.4    Nakafuku, M.5    Ishii, S.6
  • 128
    • 0032848136 scopus 로고    scopus 로고
    • Regulation of Gli2 and Gli3 activities by an amino-terminal repression domain: Implication of Gli2 and Gli3 as primary mediators of Shh signaling
    • H. Sasaki, Y. Nishizaki, C. Hui, M. Nakafuku, H. Kondoh, Regulation of Gli2 and Gli3 activities by an amino-terminal repression domain: Implication of Gli2 and Gli3 as primary mediators of Shh signaling. Development 126, 3915-3924 (1999).
    • (1999) Development , vol.126 , pp. 3915-3924
    • Sasaki, H.1    Nishizaki, Y.2    Hui, C.3    Nakafuku, M.4    Kondoh, H.5
  • 129
    • 0036801765 scopus 로고    scopus 로고
    • Gli2, but not Gli1, is required for initial Shh signaling and ectopic activation of the Shh pathway
    • C. B. Bai, W. Auerbach, J. S. Lee, D. Stephen, A. L. Joyner, Gli2, but not Gli1, is required for initial Shh signaling and ectopic activation of the Shh pathway. Development 129, 4753-4761 (2002).
    • (2002) Development , vol.129 , pp. 4753-4761
    • Bai, C.B.1    Auerbach, W.2    Lee, J.S.3    Stephen, D.4    Joyner, A.L.5
  • 130
    • 0034055649 scopus 로고    scopus 로고
    • Mouse Gli1 mutants are viable but have defects in SHH signaling in combination with a Gli2 mutation
    • H. L. Park, C. Bai, K. A. Platt, M. P. Matise, A. Beeghly, C. C. Hui, M. Nakashima, A. L. Joyner, Mouse Gli1 mutants are viable but have defects in SHH signaling in combination with a Gli2 mutation. Development 127, 1593-1605 (2000).
    • (2000) Development , vol.127 , pp. 1593-1605
    • Park, H.L.1    Bai, C.2    Platt, K.A.3    Matise, M.P.4    Beeghly, A.5    Hui, C.C.6    Nakashima, M.7    Joyner, A.L.8
  • 131
    • 0346888543 scopus 로고    scopus 로고
    • Interplays of Gli2 and Gli3 and their requirement in mediating Shh-dependent sclerotome induction
    • L. Buttitta, R. Mo, C. C. Hui, C. M. Fan, Interplays of Gli2 and Gli3 and their requirement in mediating Shh-dependent sclerotome induction. Development 130, 6233-6243 (2003).
    • (2003) Development , vol.130 , pp. 6233-6243
    • Buttitta, L.1    Mo, R.2    Hui, C.C.3    Fan, C.M.4
  • 132
    • 0031855859 scopus 로고    scopus 로고
    • Diminished Sonic hedgehog signaling and lack of floor plate differentiation in Gli2 mutant mice
    • Q. Ding, J. Motoyama, S. Gasca, R. Mo, H. Sasaki, J. Rossant, C. C. Hui, Diminished Sonic hedgehog signaling and lack of floor plate differentiation in Gli2 mutant mice. Development 125, 2533-2543 (1998).
    • (1998) Development , vol.125 , pp. 2533-2543
    • Ding, Q.1    Motoyama, J.2    Gasca, S.3    Mo, R.4    Sasaki, H.5    Rossant, J.6    Hui, C.C.7
  • 134
    • 33244463281 scopus 로고    scopus 로고
    • GLI3- dependent transcriptional repression of Gli1, Gli2 and kidney patterning genes disrupts renal morphogenesis
    • M. C. Hu, R. Mo, S. Bhella, C. W. Wilson, P. T. Chuang, C. C. Hui, N. D. Rosenblum, GLI3- dependent transcriptional repression of Gli1, Gli2 and kidney patterning genes disrupts renal morphogenesis. Development 133, 569-578 (2006).
    • (2006) Development , vol.133 , pp. 569-578
    • Hu, M.C.1    Mo, R.2    Bhella, S.3    Wilson, C.W.4    Chuang, P.T.5    Hui, C.C.6    Rosenblum, N.D.7
  • 135
    • 33846192047 scopus 로고    scopus 로고
    • Gli2 and Gli3 play distinct roles in the dorsoventral patterning of the mouse hindbrain
    • M. Lebel, R. Mo, K. Shimamura, C. C. Hui, Gli2 and Gli3 play distinct roles in the dorsoventral patterning of the mouse hindbrain. Dev. Biol. 302, 345-355 (2007).
    • (2007) Dev. Biol. , vol.302 , pp. 345-355
    • Lebel, M.1    Mo, R.2    Shimamura, K.3    Hui, C.C.4
  • 136
    • 0037439152 scopus 로고    scopus 로고
    • Sonic hedgehog-dependent activation of Gli2 is essential for embryonic hair follicle development
    • P. Mill, R. Mo, H. Fu, M. Grachtchouk, P. C. Kim, A. A. Dlugosz, C. C. Hui, Sonic hedgehog-dependent activation of Gli2 is essential for embryonic hair follicle development. Genes Dev. 17, 282- 294 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 282-294
    • Mill, P.1    Mo, R.2    Fu, H.3    Grachtchouk, M.4    Kim, P.C.5    Dlugosz, A.A.6    Hui, C.C.7
  • 138
    • 0031683165 scopus 로고    scopus 로고
    • Essential function of Gli2 and Gli3 in the formation of lung, trachea and oesophagus
    • J. Motoyama, J. Liu, R. Mo, Q. Ding, M. Post, C. C. Hui, Essential function of Gli2 and Gli3 in the formation of lung, trachea and oesophagus. Nat. Genet. 20, 54-57 (1998).
    • (1998) Nat. Genet. , vol.20 , pp. 54-57
    • Motoyama, J.1    Liu, J.2    Mo, R.3    Ding, Q.4    Post, M.5    Hui, C.C.6
  • 139
    • 0030805592 scopus 로고    scopus 로고
    • Gli1 is a target of Sonic hedgehog that induces ventral neural tube development
    • J. Lee, K. A. Platt, P. Censullo, A. Ruiz i Altaba, Gli1 is a target of Sonic hedgehog that induces ventral neural tube development. Development 124, 2537-2552 (1997).
    • (1997) Development , vol.124 , pp. 2537-2552
    • Lee, J.1    Platt, K.A.2    Censullo, P.3    Ruiz I Altaba, A.4
  • 140
    • 67650289584 scopus 로고    scopus 로고
    • Mechanisms of Hedgehog pathway activation in cancer and implications for therapy
    • S. J. Scales, F. J. de Sauvage, Mechanisms of Hedgehog pathway activation in cancer and implications for therapy. Trends Pharmacol. Sci. 30, 303-312 (2009).
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 303-312
    • Scales, S.J.1    De Sauvage, F.J.2
  • 143
    • 23344453462 scopus 로고    scopus 로고
    • Mice deficient in the fused homolog do not exhibit phenotypes indicative of perturbed hedgehog signaling during embryonic development
    • M. H. Chen, N. Gao, T. Kawakami, P. T. Chuang, Mice deficient in the fused homolog do not exhibit phenotypes indicative of perturbed hedgehog signaling during embryonic development. Mol. Cell. Biol. 25, 7042-7053 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7042-7053
    • Chen, M.H.1    Gao, N.2    Kawakami, T.3    Chuang, P.T.4
  • 144
    • 0012843926 scopus 로고    scopus 로고
    • Genetic analysis of zebrafish gli1 and gli2 reveals divergent requirements for gli genes in vertebrate development
    • R. O. Karlstrom, O. V. Tyurina, A. Kawakami, N. Nishioka, W. S. Talbot, H. Sasaki, A. F. Schier, Genetic analysis of zebrafish gli1 and gli2 reveals divergent requirements for gli genes in vertebrate development. Development 130, 1549-1564 (2003).
    • (2003) Development , vol.130 , pp. 1549-1564
    • Karlstrom, R.O.1    Tyurina, O.V.2    Kawakami, A.3    Nishioka, N.4    Talbot, W.S.5    Sasaki, H.6    Schier, A.F.7
  • 145
    • 77952723685 scopus 로고    scopus 로고
    • Quantitative insight into models of Hedgehog signal transduction
    • S. F. Farzan, S. K. Ogden, D. J. Robbins, Quantitative insight into models of Hedgehog signal transduction. Fly (Austin) 4, 141-144 (2010).
    • (2010) Fly (Austin) , vol.4 , pp. 141-144
    • Farzan, S.F.1    Ogden, S.K.2    Robbins, D.J.3
  • 146
    • 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
  • 147
    • 0242625184 scopus 로고    scopus 로고
    • Identification of a functional interaction between the transmembrane protein Smoothened and the kinesinrelated 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 kinesinrelated 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
  • 148
    • 1342282946 scopus 로고    scopus 로고
    • The Kinesin-related protein Costal2 associates with membranes in a Hedgehog-sensitive, Smoothened-independent manner
    • M. A. Stegman, J. A. Goetz, M. Ascano, Jr., S. K. Ogden, K. E. Nybakken, D. J. Robbins, The Kinesin-related protein Costal2 associates with membranes in a Hedgehog-sensitive, Smoothened-independent manner. J. Biol. Chem. 279, 7064-7071 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 7064-7071
    • Stegman, M.A.1    Goetz, J.A.2    Ascano Jr., M.3    Ogden, S.K.4    Nybakken, K.E.5    Robbins, D.J.6
  • 149
    • 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
  • 150
    • 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
  • 151
    • 34547621412 scopus 로고    scopus 로고
    • Fused-Costal2 protein complex regulates Hedgehog-induced Smo phosphorylation and cell-surface accumulation
    • Y. Liu, X. Cao, J. Jiang, J. Jia, Fused-Costal2 protein complex regulates Hedgehog-induced 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
  • 152
    • 0032492995 scopus 로고    scopus 로고
    • Suppressor of fused links fused and Cubitus interruptus on the hedgehog signalling pathway
    • V. Monnier, F. Dussillol, G. Alves, C. Lamour-Isnard, A. Plessis, Suppressor of fused links fused and Cubitus interruptus on the hedgehog signalling pathway. Curr. Biol. 8, 583-586 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 583-586
    • Monnier, V.1    Dussillol, F.2    Alves, G.3    Lamour-Isnard, C.4    Plessis, A.5
  • 153
    • 0027383291 scopus 로고
    • Segmental polarity in Drosophila melanogaster: Genetic dissection of fused in a Suppressor of fused background reveals interaction with costal-2
    • T. Préat, P. Thérond, B. Limbourg-Bouchon, A. Pham, H. Tricoire, D. Busson, C. Lamour-Isnard, Segmental polarity in Drosophila melanogaster: Genetic dissection of fused in a Suppressor of fused background reveals interaction with costal-2. Genetics 135, 1047-1062 (1993).
    • (1993) Genetics , vol.135 , pp. 1047-1062
    • Préat, T.1    Thérond, P.2    Limbourg-Bouchon, B.3    Pham, A.4    Tricoire, H.5    Busson, D.6    Lamour-Isnard, C.7
  • 154
    • 0037025382 scopus 로고    scopus 로고
    • Hedgehog-stimulated phosphorylation of the kinesin-related protein Costal2 is mediated by the serine/threonine kinase fused
    • K. E. Nybakken, C. W. Turck, D. J. Robbins, J. M. Bishop, 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
  • 155
    • 0030838880 scopus 로고    scopus 로고
    • Hedgehog elicits signal transduction by means of a large complex containing the kinesin-related protein costal2
    • D. J. Robbins, K. E. Nybakken, R. Kobayashi, J. C. Sisson, J. M. Bishop, P. P. Thérond, 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    Nybakken, K.E.2    Kobayashi, R.3    Sisson, J.C.4    Bishop, J.M.5    Thérond, P.P.6
  • 158
    • 0030754171 scopus 로고    scopus 로고
    • Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway
    • J. C. Sisson, K. S. Ho, K. Suyama, M. P. Scott, Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway. Cell 90, 235-245 (1997).
    • (1997) Cell , vol.90 , pp. 235-245
    • Sisson, J.C.1    Ho, K.S.2    Suyama, K.3    Scott, M.P.4
  • 159
    • 0013014880 scopus 로고    scopus 로고
    • Hedgehog signal transduction proteins: Contacts of the Fused kinase and Ci transcription factor with the kinesin-related protein Costal2
    • V. Monnier, K. S. Ho, M. Sanial, M. P. Scott, A. Plessis, Hedgehog signal transduction proteins: contacts of the Fused kinase and Ci transcription factor with the kinesin-related protein Costal2. BMC Dev. Biol. 2, 4 (2002).
    • (2002) BMC Dev. Biol. , vol.2 , pp. 4
    • Monnier, V.1    Ho, K.S.2    Sanial, M.3    Scott, M.P.4    Plessis, A.5
  • 160
    • 17144402650 scopus 로고    scopus 로고
    • Differential regulation of Hedgehog target gene transcription by Costal2 and Suppressor of Fused
    • K. S. Ho, K. Suyama, M. Fish, M. P. Scott, Differential regulation of Hedgehog target gene transcription by Costal2 and Suppressor of Fused. Development 132, 1401-1412 (2005).
    • (2005) Development , vol.132 , pp. 1401-1412
    • Ho, K.S.1    Suyama, K.2    Fish, M.3    Scott, M.P.4
  • 161
    • 79958243351 scopus 로고    scopus 로고
    • Hedgehog activates fused through phosphorylation to elicit a full spectrum of pathway responses
    • Q. Zhou, D. Kalderon, Hedgehog activates fused through phosphorylation to elicit a full spectrum of pathway responses. Dev. Cell 20, 802-814 (2011).
    • (2011) Dev. Cell , vol.20 , pp. 802-814
    • Zhou, Q.1    Kalderon, D.2
  • 162
    • 80053647419 scopus 로고    scopus 로고
    • Transduction of the Hedgehog signal through the dimerization of Fused and the nuclear translocation of Cubitus interruptus
    • Y. Zhang, F. Mao, Y. Lu, W. Wu, L. Zhang, Y. Zhao, Transduction of the Hedgehog signal through the dimerization of Fused and the nuclear translocation of Cubitus interruptus. Cell Res. 21, 1436-1451 (2011).
    • (2011) Cell Res. , vol.21 , pp. 1436-1451
    • Zhang, Y.1    Mao, F.2    Lu, Y.3    Wu, W.4    Zhang, L.5    Zhao, Y.6
  • 163
    • 80052515585 scopus 로고    scopus 로고
    • The Hedgehoginduced 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 Hedgehoginduced 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
  • 164
    • 84857033496 scopus 로고    scopus 로고
    • Distinct phosphorylations on kinesin costal-2 mediate differential hedgehog signaling strength
    • N. Ranieri, L. Ruel, A. Gallet, S. Raisin, P. P. Thérond, Distinct phosphorylations on kinesin costal-2 mediate differential hedgehog signaling strength. Dev. Cell 22, 279-294 (2012).
    • (2012) Dev. Cell , vol.22 , pp. 279-294
    • Ranieri, N.1    Ruel, L.2    Gallet, A.3    Raisin, S.4    Thérond, P.P.5
  • 166
    • 33646379372 scopus 로고    scopus 로고
    • Smoothened regulates activator and repressor functions of Hedgehog signaling via two distinct mechanisms
    • S. K. Ogden, D. J. Casso, M. Ascano Jr., M. M. Yore, T. B. Kornberg, D. J. Robbins, Smoothened regulates activator and repressor functions of Hedgehog signaling via two distinct mechanisms. J. Biol. Chem. 281, 7237-7243 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 7237-7243
    • Ogden, S.K.1    Casso, D.J.2    Ascano Jr., M.3    Yore, M.M.4    Kornberg, T.B.5    Robbins, D.J.6
  • 167
    • 0041827271 scopus 로고    scopus 로고
    • Smoothened translates Hedgehog levels into distinct responses
    • J. E. Hooper, Smoothened translates Hedgehog levels into distinct responses. Development 130, 3951-3963 (2003).
    • (2003) Development , vol.130 , pp. 3951-3963
    • Hooper, J.E.1
  • 170
    • 0035881953 scopus 로고    scopus 로고
    • Genetic dissection of the Drosophila Cubitus interruptus signaling complex
    • M. A. Lefers, Q. T. Wang, R. A. Holmgren, Genetic dissection of the Drosophila Cubitus interruptus signaling complex. Dev. Biol. 236, 411-420 (2001).
    • (2001) Dev. Biol. , vol.236 , pp. 411-420
    • Lefers, M.A.1    Wang, Q.T.2    Holmgren, R.A.3
  • 171
    • 77955057511 scopus 로고    scopus 로고
    • Dynamic phosphorylation of the kinesin Costal-2 in vivo reveals requirement of fused kinase activity for all levels of hedgehog signalling
    • S. Raisin, L. Ruel, N. Ranieri, L. Staccini-Lavenant, P. P. Thérond, Dynamic phosphorylation of the kinesin Costal-2 in vivo reveals requirement of fused kinase activity for all levels of hedgehog signalling. Dev. Biol. 344, 119-128 (2010).
    • (2010) Dev. Biol. , vol.344 , pp. 119-128
    • Raisin, S.1    Ruel, L.2    Ranieri, N.3    Staccini-Lavenant, L.4    Thérond, P.P.5
  • 172
    • 8644240163 scopus 로고    scopus 로고
    • An intramolecular association between two domains of the protein kinase Fused is necessary for Hedgehog signaling
    • M. Ascano, Jr, D. J. Robbins, An intramolecular association between two domains of the protein kinase Fused is necessary for Hedgehog signaling. Mol. Cell. Biol. 24, 10397-10405 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10397-10405
    • Ascano Jr., M.1    Robbins, D.J.2
  • 173
    • 34547608994 scopus 로고    scopus 로고
    • Evidence for a novel feedback loop in the Hedgehog pathway involving Smoothened and Fused
    • S. Claret, M. Sanial, A. Plessis, Evidence for a novel feedback loop in the Hedgehog pathway involving Smoothened and Fused. Curr. Biol. 17, 1326-1333 (2007).
    • (2007) Curr. Biol. , vol.17 , pp. 1326-1333
    • Claret, S.1    Sanial, M.2    Plessis, A.3
  • 175
    • 84857732765 scopus 로고    scopus 로고
    • Mammalian homologues of Drosophila fused kinase
    • A. Maloverjan, M. Piirsoo, Mammalian homologues of Drosophila fused kinase. Vitam. Horm. 88, 91-113 (2012).
    • (2012) Vitam. Horm. , vol.88 , pp. 91-113
    • Maloverjan, A.1    Piirsoo, M.2
  • 176
    • 0026761497 scopus 로고
    • Characterization of Suppressor of fused, a complete suppressor of the fused segment polarity gene of Drosophila melanogaster
    • T. Préat, Characterization of Suppressor of fused, a complete suppressor of the fused segment polarity gene of Drosophila melanogaster. Genetics 132, 725-736 (1992).
    • (1992) Genetics , vol.132 , pp. 725-736
    • Préat, T.1
  • 177
    • 56849116719 scopus 로고    scopus 로고
    • Role and regulation of human tumor suppressor SUFU in Hedgehog signaling
    • S. Y. Cheng, S. Yue, Role and regulation of human tumor suppressor SUFU in Hedgehog signaling. Adv. Cancer Res. 101, 29-43 (2008).
    • (2008) Adv. Cancer Res. , vol.101 , pp. 29-43
    • Cheng, S.Y.1    Yue, S.2
  • 179
    • 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
  • 180
    • 0033859849 scopus 로고    scopus 로고
    • Nuclear import of cubitus interruptus is regulated by hedgehog via a mechanism distinct from Ci stabilization and Ci activation
    • Q. T. Wang, R. A. Holmgren, Nuclear import of cubitus interruptus is regulated by hedgehog via a mechanism distinct from Ci stabilization and Ci activation. Development 127, 3131-3139 (2000).
    • (2000) Development , vol.127 , pp. 3131-3139
    • Wang, Q.T.1    Holmgren, R.A.2
  • 181
    • 0033789068 scopus 로고    scopus 로고
    • Suppressor of fused opposes hedgehog signal transduction by impeding nuclear accumulation of the activator form of Cubitus interruptus
    • N. Méthot, K. Basler, Suppressor of fused opposes hedgehog signal transduction by impeding nuclear accumulation of the activator form of Cubitus interruptus. Development 127, 4001-4010 (2000).
    • (2000) Development , vol.127 , pp. 4001-4010
    • Méthot, N.1    Basler, K.2
  • 182
    • 43149104980 scopus 로고    scopus 로고
    • Genetic analysis of the two zebrafish patched homologues identifies novel roles for the hedgehog signaling pathway
    • M. J. Koudijs, M. J. den Broeder, E. Groot, F. J. van Eeden, Genetic analysis of the two zebrafish patched homologues identifies novel roles for the hedgehog signaling pathway. BMC Dev. Biol. 8, 15 (2008).
    • (2008) BMC Dev. Biol. , vol.8 , pp. 15
    • Koudijs, M.J.1    Den Broeder, M.J.2    Groot, E.3    Van Eeden, F.J.4
  • 183
    • 77950463564 scopus 로고    scopus 로고
    • The output of Hedgehog signaling is controlled by the dynamic association between Suppressor of Fused and the Gli proteins
    • E. W. Humke, K. V. Dorn, L. Milenkovic, M. P. Scott, R. Rohatgi, The output of Hedgehog signaling is controlled by the dynamic association between Suppressor of Fused and the Gli proteins. Genes Dev. 24, 670-682 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 670-682
    • Humke, E.W.1    Dorn, K.V.2    Milenkovic, L.3    Scott, M.P.4    Rohatgi, R.5
  • 184
    • 69249245332 scopus 로고    scopus 로고
    • Cilium-independent regulation of Gli protein function by Sufu in Hedgehog signaling is evolutionarily conserved
    • M. H. Chen, C. W. Wilson, Y. J. Li, K. K. Law, C. S. Lu, R. Gacayan, X. Zhang, C. C. Hui, P. T. Chuang, Cilium-independent regulation of Gli protein function by Sufu in Hedgehog signaling is evolutionarily conserved. Genes Dev. 23, 1910-1928 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 1910-1928
    • Chen, M.H.1    Wilson, C.W.2    Li, Y.J.3    Law, K.K.4    Lu, C.S.5    Gacayan, R.6    Zhang, X.7    Hui, C.C.8    Chuang, P.T.9
  • 185
    • 31744450041 scopus 로고    scopus 로고
    • Negative regulation of Gli1 and Gli2 activator function by Suppressor of fused through multiple mechanisms
    • P. C. Barnfield, X. Zhang, V. Thanabalasingham, M. Yoshida, C. C. Hui, Negative regulation of Gli1 and Gli2 activator function by Suppressor of fused through multiple mechanisms. Differentiation 73, 397-405 (2005).
    • (2005) Differentiation , vol.73 , pp. 397-405
    • Barnfield, P.C.1    Zhang, X.2    Thanabalasingham, V.3    Yoshida, M.4    Hui, C.C.5
  • 186
    • 77958508124 scopus 로고    scopus 로고
    • A mechanism for vertebrate Hedgehog signaling: Recruitment to cilia and dissociation of SuFu-Gli protein complexes
    • H. Tukachinsky, L. V. Lopez, A. Salic, A mechanism for vertebrate Hedgehog signaling: Recruitment to cilia and dissociation of SuFu-Gli protein complexes. J. Cell Biol. 191, 415-428 (2010).
    • (2010) J. Cell Biol. , vol.191 , pp. 415-428
    • Tukachinsky, H.1    Lopez, L.V.2    Salic, A.3
  • 187
    • 77953050811 scopus 로고    scopus 로고
    • Suppressor of fused and Spop regulate the stability, processing and function of Gli2 and Gli3 full-length activators but not their repressors
    • C. Wang, Y. Pan, B. Wang, Suppressor of fused and Spop regulate the stability, processing and function of Gli2 and Gli3 full-length activators but not their repressors. Development 137, 2001-2009 (2010).
    • (2010) Development , vol.137 , pp. 2001-2009
    • Wang, C.1    Pan, Y.2    Wang, B.3
  • 188
    • 36849008176 scopus 로고    scopus 로고
    • The primary cilia, a 'Rab-id' transit system for hedgehog signaling
    • A. E. Oro, The primary cilia, a 'Rab-id' transit system for hedgehog signaling. Curr. Opin. Cell Biol. 19, 691-696 (2007).
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 691-696
    • Oro, A.E.1
  • 189
    • 33947384151 scopus 로고    scopus 로고
    • Overview of structure and function of mammalian cilia
    • P. Satir, S. T. Christensen, Overview of structure and function of mammalian cilia. Annu. Rev. Physiol. 69, 377-400 (2007).
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 377-400
    • Satir, P.1    Christensen, S.T.2
  • 190
    • 34547110771 scopus 로고    scopus 로고
    • Patched1 regulates hedgehog signaling at the primary cilium
    • R. Rohatgi, L. Milenkovic, M. P. Scott, Patched1 regulates hedgehog signaling at the primary cilium. Science 317, 372-376 (2007).
    • (2007) Science , vol.317 , pp. 372-376
    • Rohatgi, R.1    Milenkovic, L.2    Scott, M.P.3
  • 193
    • 75549090700 scopus 로고    scopus 로고
    • Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium
    • L. Milenkovic, M. P. Scott, R. Rohatgi, Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium. J. Cell Biol. 187, 365-374 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 365-374
    • Milenkovic, L.1    Scott, M.P.2    Rohatgi, R.3
  • 194
    • 79953858623 scopus 로고    scopus 로고
    • Dual Phosphorylation of suppressor of fused (Sufu) by PKA and GSK3beta regulates its stability and localization in the primary cilium
    • Y. Chen, S. Yue, L. Xie, X. H. Pu, T. Jin, S. Y. Cheng, Dual Phosphorylation of suppressor of fused (Sufu) by PKA and GSK3beta regulates its stability and localization in the primary cilium. J. Biol. Chem. 286, 13502-13511 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 13502-13511
    • Chen, Y.1    Yue, S.2    Xie, L.3    Pu, X.H.4    Jin, T.5    Cheng, S.Y.6
  • 195
    • 76049114315 scopus 로고    scopus 로고
    • Gli2 trafficking links Hedgehog-dependent activation of Smoothened in the primary cilium to transcriptional activation in the nucleus
    • J. Kim, M. Kato, P. A. Beachy, Gli2 trafficking links Hedgehog-dependent activation of Smoothened in the primary cilium to transcriptional activation in the nucleus. Proc. Natl. Acad. Sci. U.S.A. 106, 21666-21671 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21666-21671
    • Kim, J.1    Kato, M.2    Beachy, P.A.3
  • 196
    • 40749144679 scopus 로고    scopus 로고
    • Gli2 and Gli3 localize to cilia and require the intraflagellar transport protein polaris for processing and function
    • C. J. Haycraft, B. Banizs, Y. Aydin-Son, Q. Zhang, E. J. Michaud, B. K. Yoder, Gli2 and Gli3 localize to cilia and require the intraflagellar transport protein polaris for processing and function. PLoS Genet. 1, e53 (2005).
    • (2005) PLoS Genet. , vol.1
    • Haycraft, C.J.1    Banizs, B.2    Aydin-Son, Y.3    Zhang, Q.4    Michaud, E.J.5    Yoder, B.K.6
  • 197
    • 27744484694 scopus 로고    scopus 로고
    • Loss of the retrograde motor for IFT disrupts localization of Smo to cilia and prevents the expression of both activator and repressor functions of Gli
    • S. R. May, A. M. Ashique, M. Karlen, B. Wang, Y. Shen, K. Zarbalis, J. Reiter, J. Ericson, A. S. Peterson, Loss of the retrograde motor for IFT disrupts localization of Smo to cilia and prevents the expression of both activator and repressor functions of Gli. Dev. Biol. 287, 378-389 (2005).
    • (2005) Dev. Biol. , vol.287 , pp. 378-389
    • May, S.R.1    Ashique, A.M.2    Karlen, M.3    Wang, B.4    Shen, Y.5    Zarbalis, K.6    Reiter, J.7    Ericson, J.8    Peterson, A.S.9
  • 198
    • 77950671813 scopus 로고    scopus 로고
    • Kinetics of hedgehog-dependent full-length Gli3 accumulation in primary cilia and subsequent degradation
    • X. Wen, C. K. Lai, M. Evangelista, J. A. Hongo, F. J. de Sauvage, S. J. Scales, Kinetics of hedgehog-dependent full-length Gli3 accumulation in primary cilia and subsequent degradation. Mol. Cell. Biol. 30, 1910-1922 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1910-1922
    • Wen, X.1    Lai, C.K.2    Evangelista, M.3    Hongo, J.A.4    De Sauvage, F.J.5    Scales, S.J.6
  • 200
    • 69449099121 scopus 로고    scopus 로고
    • Mouse Kif7/Costal2 is a cilia-associated protein that regulates Sonic hedgehog signaling
    • K. F. Liem, Jr, M. He, P. J. Ocbina, K. V. Anderson, Mouse Kif7/Costal2 is a cilia-associated 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
  • 201
    • 67349198593 scopus 로고    scopus 로고
    • Suppressor of Fused inhibits mammalian Hedgehog signaling in the absence of cilia
    • J. Jia, A. Kolterud, H. Zeng, A. Hoover, S. Teglund, R. Toftgård, A. Liu, Suppressor of Fused inhibits mammalian Hedgehog signaling in the absence of cilia. Dev. Biol. 330, 452-460 (2009).
    • (2009) Dev. Biol. , vol.330 , pp. 452-460
    • Jia, J.1    Kolterud, A.2    Zeng, H.3    Hoover, A.4    Teglund, S.5    Toftgård, R.6    Liu, A.7
  • 202
    • 49449086772 scopus 로고    scopus 로고
    • Intraflagellar transport, cilia, and mammalian Hedgehog signaling: Analysis in mouse embryonic fibroblasts
    • P. J. Ocbina, K. V. Anderson, Intraflagellar transport, cilia, and mammalian Hedgehog signaling: analysis in mouse embryonic fibroblasts. Dev. Dyn. 237, 2030-2038 (2008).
    • (2008) Dev. Dyn. , vol.237 , pp. 2030-2038
    • Ocbina, P.J.1    Anderson, K.V.2
  • 203
    • 1442295841 scopus 로고    scopus 로고
    • Apoptosis and dependence receptors: A molecular basis for cellular addiction
    • D. E. Bredesen, P. Mehlen, S. Rabizadeh, Apoptosis and dependence receptors: A molecular basis for cellular addiction. Physiol. Rev. 84, 411-430 (2004).
    • (2004) Physiol. Rev. , vol.84 , pp. 411-430
    • Bredesen, D.E.1    Mehlen, P.2    Rabizadeh, S.3
  • 205
    • 79954989679 scopus 로고    scopus 로고
    • A novel signaling pathway mediated by the nuclear targeting of C-terminal fragments of mammalian Patched 1
    • H. Kagawa, Y. Shino, D. Kobayashi, S. Demizu, M. Shimada, H. Ariga, H. Kawahara, A novel signaling pathway mediated by the nuclear targeting of C-terminal fragments of mammalian Patched 1. PLoS ONE 6, e18638 (2011).
    • (2011) PLoS ONE , vol.6
    • Kagawa, H.1    Shino, Y.2    Kobayashi, D.3    Demizu, S.4    Shimada, M.5    Ariga, H.6    Kawahara, H.7
  • 207
    • 77951932085 scopus 로고    scopus 로고
    • Hedgehog proteins activate pro-angiogenic responses in endothelial cells through non-canonical signaling pathways
    • P. Chinchilla, L. Xiao, M. G. Kazanietz, N. A. Riobo, Hedgehog proteins activate pro-angiogenic responses in endothelial cells through non-canonical signaling pathways. Cell Cycle 9, 570-579 (2010).
    • (2010) Cell Cycle , vol.9 , pp. 570-579
    • Chinchilla, P.1    Xiao, L.2    Kazanietz, M.G.3    Riobo, N.A.4
  • 208
    • 0032796826 scopus 로고    scopus 로고
    • Sonic hedgehog regulates the growth and patterning of the cerebellum
    • N. Dahmane, A. Ruiz i Altaba, Sonic hedgehog regulates the growth and patterning of the cerebellum. Development 126, 3089-3100 (1999).
    • (1999) Development , vol.126 , pp. 3089-3100
    • Dahmane, N.1    Ruiz I Altaba, A.2
  • 209
    • 0033594537 scopus 로고    scopus 로고
    • Purkinje-cell-derived Sonic hedgehog regulates granule neuron precursor cell proliferation in the developing mouse cerebellum
    • V. A. Wallace, Purkinje-cell-derived Sonic hedgehog regulates granule neuron precursor cell proliferation in the developing mouse cerebellum. Curr. Biol. 9, 445-448 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 445-448
    • Wallace, V.A.1
  • 210
    • 0032959871 scopus 로고    scopus 로고
    • Control of neuronal precursor proliferation in the cerebellum by Sonic Hedgehog
    • R. J. Wechsler-Reya, M. P. Scott, Control of neuronal precursor proliferation in the cerebellum by Sonic Hedgehog. Neuron 22, 103-114 (1999).
    • (1999) Neuron , vol.22 , pp. 103-114
    • Wechsler-Reya, R.J.1    Scott, M.P.2
  • 211
    • 0035341310 scopus 로고    scopus 로고
    • Patched1 interacts with cyclin B1 to regulate cell cycle progression
    • E. A. Barnes, M. Kong, V. Ollendorff, D. J. Donoghue, Patched1 interacts with cyclin B1 to regulate cell cycle progression. EMBO J. 20, 2214-2223 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2214-2223
    • Barnes, E.A.1    Kong, M.2    Ollendorff, V.3    Donoghue, D.J.4
  • 212
    • 0033695002 scopus 로고    scopus 로고
    • Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C
    • C. G. Takizawa, D. O. Morgan, Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C. Curr. Opin. Cell Biol. 12, 658-665 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 658-665
    • Takizawa, C.G.1    Morgan, D.O.2
  • 213
    • 13444251046 scopus 로고    scopus 로고
    • Constitutive activation of the shh-ptc1 pathway by a patched1 mutation identified in BCC
    • E. A. Barnes, K. J. Heidtman, D. J. Donoghue, Constitutive activation of the shh-ptc1 pathway by a patched1 mutation identified in BCC. Oncogene 24, 902-915 (2005).
    • (2005) Oncogene , vol.24 , pp. 902-915
    • Barnes, E.A.1    Heidtman, K.J.2    Donoghue, D.J.3
  • 214
    • 67649836304 scopus 로고    scopus 로고
    • Kinase activity-independent regulation of cyclin pathway by GRK2 is essential for zebrafish early development
    • X. Jiang, P. Yang, L. Ma, Kinase activity-independent regulation of cyclin pathway by GRK2 is essential for zebrafish early development. Proc. Natl. Acad. Sci. U.S.A. 106, 10183-10188 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10183-10188
    • Jiang, X.1    Yang, P.2    Ma, L.3
  • 216
    • 79957613017 scopus 로고    scopus 로고
    • Heterotrimeric Gi proteins link Hedgehog signaling to activation of Rho small GTPases to promote fibroblast migration
    • A. H. Polizio, P. Chinchilla, X. Chen, S. Kim, D. R. Manning, N. A. Riobo, Heterotrimeric Gi proteins link Hedgehog signaling to activation of Rho small GTPases to promote fibroblast migration. J. Biol. Chem. 286, 19589-19596 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 19589-19596
    • Polizio, A.H.1    Chinchilla, P.2    Chen, X.3    Kim, S.4    Manning, D.R.5    Riobo, N.A.6
  • 217
    • 77957966730 scopus 로고    scopus 로고
    • Sonic hedgehog signaling regulates actin cytoskeleton via Tiam1- Rac1 cascade during spine formation
    • N. Sasaki, J. Kurisu, M. Kengaku, Sonic hedgehog signaling regulates actin cytoskeleton via Tiam1- Rac1 cascade during spine formation. Mol. Cell. Neurosci. 45, 335-344 (2010).
    • (2010) Mol. Cell. Neurosci. , vol.45 , pp. 335-344
    • Sasaki, N.1    Kurisu, J.2    Kengaku, M.3
  • 218
    • 21044450377 scopus 로고    scopus 로고
    • Novel brain wiring functions for classical morphogens: A role as graded positional cues in axon guidance
    • F. Charron, M. Tessier-Lavigne, Novel brain wiring functions for classical morphogens: A role as graded positional cues in axon guidance. Development 132, 2251-2262 (2005).
    • (2005) Development , vol.132 , pp. 2251-2262
    • Charron, F.1    Tessier-Lavigne, M.2
  • 220
    • 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
  • 221
  • 223
    • 23844492113 scopus 로고    scopus 로고
    • Src-dependent tyrosine phosphorylation at the tips of growth cone filopodia promotes extension
    • E. Robles, S. Woo, T. M. Gomez, Src-dependent tyrosine phosphorylation at the tips of growth cone filopodia promotes extension. J. Neurosci. 25, 7669-7681 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 7669-7681
    • Robles, E.1    Woo, S.2    Gomez, T.M.3
  • 224
    • 0035851919 scopus 로고    scopus 로고
    • Transmission of growth cone traction force through apCAM-cytoskeletal linkages is regulated by Src family tyrosine kinase activity
    • D. M. Suter, P. Forscher, Transmission of growth cone traction force through apCAM-cytoskeletal linkages is regulated by Src family tyrosine kinase activity. J. Cell Biol. 155, 427-438 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 427-438
    • Suter, D.M.1    Forscher, P.2
  • 225
    • 0029953417 scopus 로고    scopus 로고
    • Pax2 contributes to inner ear patterning and optic nerve trajectory
    • M. Torres, E. Gómez-Pardo, P. Gruss, Pax2 contributes to inner ear patterning and optic nerve trajectory. Development 122, 3381-3391 (1996).
    • (1996) Development , vol.122 , pp. 3381-3391
    • Torres, M.1    Gómez-Pardo, E.2    Gruss, P.3
  • 226
    • 0034755395 scopus 로고    scopus 로고
    • Control of retinal ganglion cell axon growth: A new role for Sonic hedgehog
    • F. Trousse, E. Martí, P. Gruss, M. Torres, P. Bovolenta, Control of retinal ganglion cell axon growth: A new role for Sonic hedgehog. Development 128, 3927-3936 (2001).
    • (2001) Development , vol.128 , pp. 3927-3936
    • Trousse, F.1    Martí, E.2    Gruss, P.3    Torres, M.4    Bovolenta, P.5
  • 227
    • 0033152924 scopus 로고    scopus 로고
    • Signal transduction underlying growth cone guidance by diffusible factors
    • H. J. Song, M. M. Poo, Signal transduction underlying growth cone guidance by diffusible factors. Curr. Opin. Neurobiol. 9, 355-363 (1999).
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 355-363
    • Song, H.J.1    Poo, M.M.2
  • 228
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • M. J. Berridge, Neuronal calcium signaling. Neuron 21, 13-26 (1998).
    • (1998) Neuron , vol.21 , pp. 13-26
    • Berridge, M.J.1
  • 229
    • 0030201466 scopus 로고    scopus 로고
    • 2+ fluctuations modulate the rate of neuronal migration
    • 2+ fluctuations modulate the rate of neuronal migration. Neuron 17, 275-285 (1996).
    • (1996) Neuron , vol.17 , pp. 275-285
    • Komuro, H.1    Rakic, P.2
  • 230
    • 79952733097 scopus 로고    scopus 로고
    • Sonic hedgehog signaling is decoded by calcium spike activity in the developing spinal cord
    • Y. H. Belgacem, L. N. Borodinsky, Sonic hedgehog signaling is decoded by calcium spike activity in the developing spinal cord. Proc. Natl. Acad. Sci. U.S.A. 108, 4482-4487 (2011).
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 4482-4487
    • Belgacem, Y.H.1    Borodinsky, L.N.2
  • 231
    • 77953943126 scopus 로고    scopus 로고
    • Not lost in space: Traffi cking in the hedgehog signaling pathway
    • L. Milenkovic, M. P. Scott, Not lost in space: Traffi cking in the hedgehog signaling pathway. Sci. Signal. 3, pe14 (2010).
    • (2010) Sci. Signal. , vol.3
    • Milenkovic, L.1    Scott, M.P.2
  • 232
    • 80555135917 scopus 로고    scopus 로고
    • Regulation of primary response genes
    • T. Fowler, R. Sen, A. L. Roy, Regulation of primary response genes. Mol. Cell 44, 348-360 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 348-360
    • Fowler, T.1    Sen, R.2    Roy, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.