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Volumn 6, Issue , 2015, Pages

Regulation of endogenous transmembrane receptors through optogenetic Cry2 clustering

Author keywords

[No Author keywords available]

Indexed keywords

CRYPTOCHROME 2; FIBROBLAST GROWTH FACTOR RECEPTOR; INTEGRIN RECEPTOR; MEMBRANE RECEPTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE; ARABIDOPSIS PROTEIN; CRY2 PROTEIN, ARABIDOPSIS; CRYPTOCHROME;

EID: 84928807371     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7898     Document Type: Article
Times cited : (75)

References (54)
  • 1
    • 0031940393 scopus 로고    scopus 로고
    • Controlling signaling with a specifically designed Gi-coupled receptor
    • Coward, P. et al. Controlling signaling with a specifically designed Gi-coupled receptor. Proc. Natl Acad. Sci. USA 95, 352-357 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 352-357
    • Coward, P.1
  • 2
    • 0027756895 scopus 로고
    • Controlling signal transduction with synthetic ligands
    • Spencer, D., Wandless, T., Schreiber, S. & Crabtree, G. Controlling signal transduction with synthetic ligands. Science 262, 1019-1024 (1993).
    • (1993) Science , vol.262 , pp. 1019-1024
    • Spencer, D.1    Wandless, T.2    Schreiber, S.3    Crabtree, G.4
  • 3
    • 0028485768 scopus 로고
    • PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation
    • Dikic, I., Schlessinger, J. & Lax, I. PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation. Curr. Biol. 4, 702-708 (1994).
    • (1994) Curr. Biol. , vol.4 , pp. 702-708
    • Dikic, I.1    Schlessinger, J.2    Lax, I.3
  • 4
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang, Y., Woronicz, J. D., Liu, W. & Goeddel, D. V. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 283, 543-546 (1999).
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 5
    • 0028483678 scopus 로고
    • EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor
    • Traverse, S. et al. EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr. Biol. 4, 694-701 (1994).
    • (1994) Curr. Biol. , vol.4 , pp. 694-701
    • Traverse, S.1
  • 6
    • 83455176258 scopus 로고    scopus 로고
    • Mosaic amplification of multiple receptor tyrosine kinase genes in glioblastoma
    • Snuderl, M. et al. Mosaic amplification of multiple receptor tyrosine kinase genes in glioblastoma. Cancer Cell 20, 810-817 (2011).
    • (2011) Cancer Cell , vol.20 , pp. 810-817
    • Snuderl, M.1
  • 7
    • 84858239977 scopus 로고    scopus 로고
    • Gene overexpression: Uses, mechanisms, and interpretation
    • Prelich, G. Gene overexpression: uses, mechanisms, and interpretation. Genetics 190, 841-854 (2012).
    • (2012) Genetics , vol.190 , pp. 841-854
    • Prelich, G.1
  • 8
    • 79959873914 scopus 로고    scopus 로고
    • The development and application of optogenetics
    • Fenno, L., Yizhar, O. & Deisseroth, K. The development and application of optogenetics. Annu. Rev. Neurosci. 34, 389-412 (2011).
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 389-412
    • Fenno, L.1    Yizhar, O.2    Deisseroth, K.3
  • 9
    • 65549086510 scopus 로고    scopus 로고
    • Temporally precise in vivo control of intracellular signalling
    • Airan, R. D., Thompson, K. R., Fenno, L. E., Bernstein, H. & Deisseroth, K. Temporally precise in vivo control of intracellular signalling. Nature 458, 1025-1029 (2009).
    • (2009) Nature , vol.458 , pp. 1025-1029
    • Airan, R.D.1    Thompson, K.R.2    Fenno, L.E.3    Bernstein, H.4    Deisseroth, K.5
  • 10
    • 69949104482 scopus 로고    scopus 로고
    • A genetically encoded photoactivatable Rac controls the motility of living cells
    • Wu, Y. I. et al. A genetically encoded photoactivatable Rac controls the motility of living cells. Nature 461, 104-108 (2009).
    • (2009) Nature , vol.461 , pp. 104-108
    • Wu, Y.I.1
  • 11
    • 70350070364 scopus 로고    scopus 로고
    • Spatiotemporal control of cell signalling using a light-switchable protein interaction
    • Levskaya, A., Weiner, O. D., Lim, W. A. & Voigt, C. A. Spatiotemporal control of cell signalling using a light-switchable protein interaction. Nature 461, 997-1001 (2009).
    • (2009) Nature , vol.461 , pp. 997-1001
    • Levskaya, A.1    Weiner, O.D.2    Lim, W.A.3    Voigt, C.A.4
  • 12
    • 70349967637 scopus 로고    scopus 로고
    • Induction of protein-protein interactions in live cells using light
    • Yazawa, M., Sadaghiani, A. M., Hsueh, B. & Dolmetsch, R. E. Induction of protein-protein interactions in live cells using light. Nat. Biotechnol. 27, 941-945 (2009).
    • (2009) Nat. Biotechnol. , vol.27 , pp. 941-945
    • Yazawa, M.1    Sadaghiani, A.M.2    Hsueh, B.3    Dolmetsch, R.E.4
  • 13
    • 78649714869 scopus 로고    scopus 로고
    • Rapid blue-light-mediated induction of protein interactions in living cells
    • Kennedy, M. J. et al. Rapid blue-light-mediated induction of protein interactions in living cells. Nat. Method 7, 973-975 (2010).
    • (2010) Nat. Method , vol.7 , pp. 973-975
    • Kennedy, M.J.1
  • 14
    • 84862777445 scopus 로고    scopus 로고
    • TULIPs: Tunable, light-controlled interacting protein tags for cell biology
    • Strickland, D. et al. TULIPs: tunable, light-controlled interacting protein tags for cell biology. Nat. Method 9, 379-384 (2012).
    • (2012) Nat. Method , vol.9 , pp. 379-384
    • Strickland, D.1
  • 15
    • 84868556564 scopus 로고    scopus 로고
    • Optical control of protein activity by fluorescent protein domains
    • Zhou, X. X., Chung, H. K., Lam, A. J. & Lin, M. Z. Optical control of protein activity by fluorescent protein domains. Science 338, 810-814 (2012).
    • (2012) Science , vol.338 , pp. 810-814
    • Zhou, X.X.1    Chung, H.K.2    Lam, A.J.3    Lin, M.Z.4
  • 16
    • 84874656353 scopus 로고    scopus 로고
    • Optogenetic protein clustering and signaling activation in mammalian cells
    • Bugaj, L. J., Choksi, A. T., Mesuda, C. K., Kane, R. S. & Schaffer, D. V. Optogenetic protein clustering and signaling activation in mammalian cells. Nat. Methods 10, 249-252 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 249-252
    • Bugaj, L.J.1    Choksi, A.T.2    Mesuda, C.K.3    Kane, R.S.4    Schaffer, D.V.5
  • 17
    • 84883212789 scopus 로고    scopus 로고
    • Light-inducible activation of target mRNA translation in mammalian cells
    • Cao, J. et al. Light-inducible activation of target mRNA translation in mammalian cells. Chem. Commun. 49, 8338-8340 (2013).
    • (2013) Chem. Commun. , vol.49 , pp. 8338-8340
    • Cao, J.1
  • 18
    • 0028110068 scopus 로고
    • Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity
    • Davis, S. et al. Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. Science 266, 816-819 (1994).
    • (1994) Science , vol.266 , pp. 816-819
    • Davis, S.1
  • 19
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C.-H. Dimerization of cell surface receptors in signal transduction. Cell 80, 213-223 (1995).
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.-H.1
  • 20
    • 0025998529 scopus 로고
    • T-cell and basophil activation through the cytoplasmic tail of T-cell-receptor zeta family proteins
    • Letourneur, F. & Klausner, R. D. T-cell and basophil activation through the cytoplasmic tail of T-cell-receptor zeta family proteins. Proc. Natl Acad. Sci. USA 88, 8905-8909 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8905-8909
    • Letourneur, F.1    Klausner, R.D.2
  • 22
    • 0026083035 scopus 로고
    • Cellular immunity to HIV activated by CD4 fused to T cell or Fc receptor polypeptides
    • Romeo, C. & Seed, B. Cellular immunity to HIV activated by CD4 fused to T cell or Fc receptor polypeptides. Cell 64, 1037-1046 (1991).
    • (1991) Cell , vol.64 , pp. 1037-1046
    • Romeo, C.1    Seed, B.2
  • 23
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000).
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 24
    • 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, 252-258 (2007).
    • (2007) Nature , vol.450 , pp. 252-258
    • Zhao, Y.1    Tong, C.2    Jiang, J.3
  • 25
    • 8444223093 scopus 로고    scopus 로고
    • Wnt signals across the plasma membrane to activate the b-catenin pathway by forming oligomers containing its receptors, Frizzled and LRP
    • Cong, F., Schweizer, L. & Varmus, H. Wnt signals across the plasma membrane to activate the b-catenin pathway by forming oligomers containing its receptors, Frizzled and LRP. Development 131, 5103-5115 (2004).
    • (2004) Development , vol.131 , pp. 5103-5115
    • Cong, F.1    Schweizer, L.2    Varmus, H.3
  • 26
    • 0028239074 scopus 로고
    • Clustering of the high affinity Fc receptor for immunoglobulin G (Fc gamma RI) results in phosphorylation of its associated gamma-chain
    • Duchemin, A. M., Ernst, L. K. & Anderson, C. L. Clustering of the high affinity Fc receptor for immunoglobulin G (Fc gamma RI) results in phosphorylation of its associated gamma-chain. J. Biol. Chem. 269, 12111-12117 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12111-12117
    • Duchemin, A.M.1    Ernst, L.K.2    Anderson, C.L.3
  • 27
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • Havranek, J. J. & Harbury, P. B. Automated design of specificity in molecular recognition. Nat. Struct. Mol. Biol. 10, 45-52 (2003).
    • (2003) Nat. Struct. Mol. Biol. , vol.10 , pp. 45-52
    • Havranek, J.J.1    Harbury, P.B.2
  • 28
    • 77951719842 scopus 로고    scopus 로고
    • Stability elements in the LRP6 cytoplasmic tail confer efficient signalling upon DIXdependent polymerization
    • Metcalfe, C., Mendoza-Topaz, C., Mieszczanek, J. & Bienz, M. Stability elements in the LRP6 cytoplasmic tail confer efficient signalling upon DIXdependent polymerization. J. Cell Sci. 123, 1588-1599 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 1588-1599
    • Metcalfe, C.1    Mendoza-Topaz, C.2    Mieszczanek, J.3    Bienz, M.4
  • 29
    • 77949587674 scopus 로고    scopus 로고
    • Lentiviral vectors to probe and manipulate the Wnt signaling pathway
    • Fuerer, C. & Nusse, R. Lentiviral vectors to probe and manipulate the Wnt signaling pathway. PLoS ONE 5, e9370 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e9370
    • Fuerer, C.1    Nusse, R.2
  • 30
    • 0024797725 scopus 로고
    • Inhibition of phosphotyrosine phosphatases reveals candidate substrates of the PDGF receptor kinase
    • Zippel, R. et al. Inhibition of phosphotyrosine phosphatases reveals candidate substrates of the PDGF receptor kinase. Eur. J. Cell Biol. 50, 428-434 (1989).
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 428-434
    • Zippel, R.1
  • 31
    • 0025941527 scopus 로고
    • A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1
    • Mohammadi, M. et al. A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1. Mol. Cell Biol. 11, 5068-5078 (1991).
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5068-5078
    • Mohammadi, M.1
  • 32
    • 0025681492 scopus 로고
    • Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors
    • Anderson, D. et al. Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. Science 250, 979-982 (1990).
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1
  • 33
    • 0033772308 scopus 로고    scopus 로고
    • FAK integrates growth-factor and integrin signals to promote cell migration
    • Sieg, D. J. et al. FAK integrates growth-factor and integrin signals to promote cell migration. Nat. Cell Biol. 2, 249-256 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 249-256
    • Sieg, D.J.1
  • 34
    • 0035196711 scopus 로고    scopus 로고
    • EDG-1 links the PDGF receptor to Src and focal adhesion kinase activation leading to lamellipodia formation and cell migration
    • Rosenfeldt, H. M. et al. EDG-1 links the PDGF receptor to Src and focal adhesion kinase activation leading to lamellipodia formation and cell migration. FASEB J. 15, 2649-2659 (2001).
    • (2001) FASEB J. , vol.15 , pp. 2649-2659
    • Rosenfeldt, H.M.1
  • 35
    • 0028055272 scopus 로고
    • Regulation of chemotaxis by the platelet-derived growth factor receptor-[beta]
    • Kundra, V. et al. Regulation of chemotaxis by the platelet-derived growth factor receptor-[beta]. Nature 367, 474-476 (1994).
    • (1994) Nature , vol.367 , pp. 474-476
    • Kundra, V.1
  • 36
    • 0032875460 scopus 로고    scopus 로고
    • Mechanism of action and in vivo role of platelet-derived growth factor
    • Heldin, C.-H. & Westermark, B. Mechanism of action and in vivo role of platelet-derived growth factor. Physiol. Rev. 79, 1283-1316 (1999).
    • (1999) Physiol. Rev. , vol.79 , pp. 1283-1316
    • Heldin, C.-H.1    Westermark, B.2
  • 37
    • 0033594403 scopus 로고    scopus 로고
    • Akt/PKB localisation and 30 phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction
    • Watton, S. J. & Downward, J. Akt/PKB localisation and 30 phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction. Curr. Biol. 9, 433-436 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 433-436
    • Watton, S.J.1    Downward, J.2
  • 39
    • 0038644597 scopus 로고    scopus 로고
    • Activation of integrin aIIb-3 by modulation of transmembrane helix associations
    • Li, R. et al. Activation of integrin aIIb-3 by modulation of transmembrane helix associations. Science 300, 795-798 (2003).
    • (2003) Science , vol.300 , pp. 795-798
    • Li, R.1
  • 40
    • 0037674763 scopus 로고    scopus 로고
    • Detection of integrin aIIbb3clustering in living cells
    • Buensuceso, C., de Virgilio, M. & Shattil, S. J. Detection of integrin aIIbb3clustering in living cells. J. Biol. Chem. 278, 15217-15224 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 15217-15224
    • Buensuceso, C.1    De Virgilio, M.2    Shattil, S.J.3
  • 41
    • 73649106911 scopus 로고    scopus 로고
    • B integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation
    • Anthis, N. J. et al. b integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation. J. Biol. Chem. 284, 36700-36710 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 36700-36710
    • Anthis, N.J.1
  • 42
  • 43
    • 0034644603 scopus 로고    scopus 로고
    • Localized Rac activation dynamics visualized in living cells
    • Kraynov, V. S. et al. Localized Rac activation dynamics visualized in living cells. Science 290, 333-337 (2000).
    • (2000) Science , vol.290 , pp. 333-337
    • Kraynov, V.S.1
  • 44
    • 84875456720 scopus 로고    scopus 로고
    • A localized Wnt signal orients asymmetric stem cell division in vitro
    • Habib, S. J. et al. A localized Wnt signal orients asymmetric stem cell division in vitro. Science 339, 1445-1448 (2013).
    • (2013) Science , vol.339 , pp. 1445-1448
    • Habib, S.J.1
  • 45
    • 84862270480 scopus 로고    scopus 로고
    • P53 dynamics control cell fate
    • Purvis, J. E. et al. p53 dynamics control cell fate. Science 336, 1440-1444 (2012).
    • (2012) Science , vol.336 , pp. 1440-1444
    • Purvis, J.E.1
  • 46
    • 84862776564 scopus 로고    scopus 로고
    • Spatiotemporal control of gene expression by a light-switchable transgene system
    • Wang, X., Chen, X. & Yang, Y. Spatiotemporal control of gene expression by a light-switchable transgene system. Nat. Method 9, 266-269 (2012).
    • (2012) Nat. Method , vol.9 , pp. 266-269
    • Wang, X.1    Chen, X.2    Yang, Y.3
  • 47
    • 84901992638 scopus 로고    scopus 로고
    • Light-inducible receptor tyrosine kinases that regulate neurotrophin signalling
    • Chang, K.-Y. et al. Light-inducible receptor tyrosine kinases that regulate neurotrophin signalling. Nat. Commun. 5, 4057 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4057
    • Chang, K.-Y.1
  • 48
    • 84904568275 scopus 로고    scopus 로고
    • Spatiotemporal control of fibroblast growth factor receptor signals by blue light
    • Kim, N. et al. Spatiotemporal control of fibroblast growth factor receptor signals by blue light. Chem. Biol. 21, 903-912 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 903-912
    • Kim, N.1
  • 49
    • 0037434983 scopus 로고    scopus 로고
    • Generation and functional characterization of intracellular antibodies interacting with the kinase domain of human EGF receptor
    • Hyland, S., Beerli, R. R., Barbas, III C. F., Hynes, N. E. & Wels, W. Generation and functional characterization of intracellular antibodies interacting with the kinase domain of human EGF receptor. Oncogene 22, 1557-1567 (2003).
    • (2003) Oncogene , vol.22 , pp. 1557-1567
    • Hyland, S.1    Beerli, R.R.2    Barbas, C.F.3    Hynes, N.E.4    Wels, W.5
  • 50
    • 84881409937 scopus 로고    scopus 로고
    • Formation of Arabidopsis Cryptochrome 2 photobodies in mammalian nuclei: Application as an optogenetic DNA damage checkpoint switch
    • Ozkan-Dagliyan, I. et al. Formation of Arabidopsis Cryptochrome 2 photobodies in mammalian nuclei: application as an optogenetic DNA damage checkpoint switch. J. Biol. Chem. 288, 23244-23251 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 23244-23251
    • Ozkan-Dagliyan, I.1
  • 51
    • 84908520377 scopus 로고    scopus 로고
    • An optimized optogenetic clustering tool for probing protein interaction and function
    • Taslimi, A. et al. An optimized optogenetic clustering tool for probing protein interaction and function. Nat. Commun. 5, 4925 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4925
    • Taslimi, A.1
  • 52
    • 68149136937 scopus 로고    scopus 로고
    • Circular polymerase extension cloning of complex gene libraries and pathways
    • Quan, J. & Tian, J. Circular polymerase extension cloning of complex gene libraries and pathways. PLoS ONE 4, e6441 (2009).
    • (2009) PLoS ONE , vol.4 , pp. e6441
    • Quan, J.1    Tian, J.2
  • 53
    • 0029610078 scopus 로고
    • Survival and differentiation of adult neuronal progenitor cells transplanted to the adult brain
    • Gage, F. H. et al. Survival and differentiation of adult neuronal progenitor cells transplanted to the adult brain. Proc. Natl Acad. Sci. USA 92, 11879-11883 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11879-11883
    • Gage, F.H.1
  • 54
    • 33645217805 scopus 로고    scopus 로고
    • Selection of novel vesicular stomatitis virus glycoprotein variants from a peptide insertion library for enhanced purification of retroviral and lentiviral vectors
    • Yu, J. H. & Schaffer, D. V. Selection of novel vesicular stomatitis virus glycoprotein variants from a peptide insertion library for enhanced purification of retroviral and lentiviral vectors. J. Virol. 80, 3285-3292 (2006).
    • (2006) J. Virol. , vol.80 , pp. 3285-3292
    • Yu, J.H.1    Schaffer, D.V.2


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