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Volumn 112, Issue 1, 2015, Pages 112-117

Engineering an improved light-induced dimer (iLID) for controlling the localization and activity of signaling proteins

Author keywords

Computational library; Optogenetic tool; Per arnt sim domain; Phage display; Rosetta molecular modeling suite

Indexed keywords

DIMER; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; IMPROVED LIGHT INDUCED DIMER; UNCLASSIFIED DRUG; MUTANT PROTEIN; VEGETABLE PROTEIN;

EID: 84920409500     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1417910112     Document Type: Article
Times cited : (458)

References (29)
  • 1
    • 9544226448 scopus 로고    scopus 로고
    • A humanized system for pharmacologic control of gene expression
    • Rivera VM, et al. (1996) A humanized system for pharmacologic control of gene expression. Nat Med 2(9):1028-1032.
    • (1996) Nat Med , vol.2 , Issue.9 , pp. 1028-1032
    • Rivera, V.M.1
  • 2
    • 70349967637 scopus 로고    scopus 로고
    • Induction of protein-protein interactions in live cells using light
    • Yazawa M, Sadaghiani AM, Hsueh B, Dolmetsch RE (2009) Induction of protein-protein interactions in live cells using light. Nat Biotechnol 27(10):941-945.
    • (2009) Nat Biotechnol , vol.27 , Issue.10 , pp. 941-945
    • Yazawa, M.1    Sadaghiani, A.M.2    Hsueh, B.3    Dolmetsch, R.E.4
  • 3
    • 70350070364 scopus 로고    scopus 로고
    • Spatiotemporal control of cell signalling using a light-switchable protein interaction
    • Levskaya A, Weiner OD, Lim WA, Voigt CA (2009) Spatiotemporal control of cell signalling using a light-switchable protein interaction. Nature 461(7266):997-1001.
    • (2009) Nature , vol.461 , Issue.7266 , pp. 997-1001
    • Levskaya, A.1    Weiner, O.D.2    Lim, W.A.3    Voigt, C.A.4
  • 4
    • 78649714869 scopus 로고    scopus 로고
    • Rapid blue-light-mediated induction of protein interactions in living cells
    • Kennedy MJ, et al. (2010) Rapid blue-light-mediated induction of protein interactions in living cells. Nat Methods 7(12):973-975.
    • (2010) Nat Methods , vol.7 , Issue.12 , pp. 973-975
    • Kennedy, M.J.1
  • 5
    • 84882976110 scopus 로고    scopus 로고
    • Optical control of mammalian endogenous transcription and epigenetic states
    • Konermann S, et al. (2013) Optical control of mammalian endogenous transcription and epigenetic states. Nature 500(7463):472-476.
    • (2013) Nature , vol.500 , Issue.7463 , pp. 472-476
    • Konermann, S.1
  • 6
    • 84874656353 scopus 로고    scopus 로고
    • Optogenetic protein clustering and signaling activation in mammalian cells
    • Bugaj LJ, Choksi AT, Mesuda CK, Kane RS, Schaffer DV (2013) Optogenetic protein clustering and signaling activation in mammalian cells. Nat Methods 10(3):249-252.
    • (2013) Nat Methods , vol.10 , Issue.3 , pp. 249-252
    • Bugaj, L.J.1    Choksi, A.T.2    Mesuda, C.K.3    Kane, R.S.4    Schaffer, D.V.5
  • 7
    • 28544442417 scopus 로고    scopus 로고
    • Synthetic biology: Engineering Escherichia coli to see light
    • Levskaya A, et al. (2005) Synthetic biology: Engineering Escherichia coli to see light. Nature 438(7067):441-442.
    • (2005) Nature , vol.438 , Issue.7067 , pp. 441-442
    • Levskaya, A.1
  • 8
    • 78650896342 scopus 로고    scopus 로고
    • Multichromatic control of gene expression in Escherichia coli
    • Tabor JJ, Levskaya A, Voigt CA (2011) Multichromatic control of gene expression in Escherichia coli. J Mol Biol 405(2):315-324.
    • (2011) J Mol Biol , vol.405 , Issue.2 , pp. 315-324
    • Tabor, J.J.1    Levskaya, A.2    Voigt, C.A.3
  • 9
    • 84862777445 scopus 로고    scopus 로고
    • TULIPs: Tunable, light-controlled interacting protein tags for cell biology
    • Strickland D, et al. (2012) TULIPs: Tunable, light-controlled interacting protein tags for cell biology. Nat Methods 9(4):379-384.
    • (2012) Nat Methods , vol.9 , Issue.4 , pp. 379-384
    • Strickland, D.1
  • 10
    • 37049002915 scopus 로고    scopus 로고
    • N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa
    • Halavaty AS, Moffat K (2007) N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa. Biochemistry 46(49):14001-14009.
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 14001-14009
    • Halavaty, A.S.1    Moffat, K.2
  • 11
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper SM, Neil LC, Gardner KH (2003) Structural basis of a phototropin light switch. Science 301(5639):1541-1544.
    • (2003) Science , vol.301 , Issue.5639 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 12
    • 84860285055 scopus 로고    scopus 로고
    • The amino-terminal helix modulates light-activated conformational changes in AsLOV2
    • Zayner JP, Antoniou C, Sosnick TR (2012) The amino-terminal helix modulates light-activated conformational changes in AsLOV2. J Mol Biol 419(1-2):61-74.
    • (2012) J Mol Biol , vol.419 , Issue.1-2 , pp. 61-74
    • Zayner, J.P.1    Antoniou, C.2    Sosnick, T.R.3
  • 13
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon M, Christie JM, Knieb E, Lempert U, Briggs WR (2000) Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin. Biochemistry 39(31):9401-9410.
    • (2000) Biochemistry , vol.39 , Issue.31 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 14
    • 0035965307 scopus 로고    scopus 로고
    • The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin
    • Swartz TE, et al. (2001) The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin. J Biol Chem 276(39):36493-36500.
    • (2001) J Biol Chem , vol.276 , Issue.39 , pp. 36493-36500
    • Swartz, T.E.1
  • 15
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • Wah DA, Levchenko I, Baker TA, Sauer RT (2002) Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem Biol 9(11):1237-1245.
    • (2002) Chem Biol , vol.9 , Issue.11 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 16
    • 0035845498 scopus 로고    scopus 로고
    • Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis
    • Flynn JM, et al. (2001) Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis. Proc Natl Acad Sci USA 98(19):10584-10589.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.19 , pp. 10584-10589
    • Flynn, J.M.1
  • 17
    • 0141992126 scopus 로고    scopus 로고
    • Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag
    • Levchenko I, Grant RA, Wah DA, Sauer RT, Baker TA (2003) Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. Mol Cell 12(2):365-372.
    • (2003) Mol Cell , vol.12 , Issue.2 , pp. 365-372
    • Levchenko, I.1    Grant, R.A.2    Wah, D.A.3    Sauer, R.T.4    Baker, T.A.5
  • 18
    • 84860133612 scopus 로고    scopus 로고
    • Designing photoswitchable peptides using the AsLOV2 domain
    • Lungu OI, et al. (2012) Designing photoswitchable peptides using the AsLOV2 domain. Chem Biol 19(4):507-517.
    • (2012) Chem Biol , vol.19 , Issue.4 , pp. 507-517
    • Lungu, O.I.1
  • 19
    • 77955170460 scopus 로고    scopus 로고
    • Rationally improving LOV domain-based photoswitches
    • Strickland D, et al. (2010) Rationally improving LOV domain-based photoswitches. Nat Methods 7(8):623-626.
    • (2010) Nat Methods , vol.7 , Issue.8 , pp. 623-626
    • Strickland, D.1
  • 20
    • 78650905964 scopus 로고    scopus 로고
    • ROSETTA3: An object-oriented software suite for the simulation and design of macromolecules
    • Leaver-Fay A, et al. (2011) ROSETTA3: An object-oriented software suite for the simulation and design of macromolecules. Methods Enzymol 487:545-574.
    • (2011) Methods Enzymol , vol.487 , pp. 545-574
    • Leaver-Fay, A.1
  • 21
    • 79956126348 scopus 로고    scopus 로고
    • Efficient phage display of intracellularly folded proteins mediated by the TAT pathway
    • Speck J, Arndt KM, Müller KM (2011) Efficient phage display of intracellularly folded proteins mediated by the TAT pathway. Protein Eng Des Sel 24(6):473-484.
    • (2011) Protein Eng des Sel , vol.24 , Issue.6 , pp. 473-484
    • Speck, J.1    Arndt, K.M.2    Müller, K.M.3
  • 22
    • 44449109239 scopus 로고    scopus 로고
    • Improving the photostability of bright monomeric orange and red fluorescent proteins
    • Shaner NC, et al. (2008) Improving the photostability of bright monomeric orange and red fluorescent proteins. Nat Methods 5(6):545-551.
    • (2008) Nat Methods , vol.5 , Issue.6 , pp. 545-551
    • Shaner, N.C.1
  • 23
    • 52649120304 scopus 로고    scopus 로고
    • Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia
    • Cai L, Makhov AM, Schafer DA, Bear JE (2008) Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia. Cell 134(5):828-842.
    • (2008) Cell , vol.134 , Issue.5 , pp. 828-842
    • Cai, L.1    Makhov, A.M.2    Schafer, D.A.3    Bear, J.E.4
  • 24
    • 21444442055 scopus 로고    scopus 로고
    • An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways
    • Inoue T, Heo WD, Grimley JS, Wandless TJ, Meyer T (2005) An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways. Nat Methods 2(6):415-418.
    • (2005) Nat Methods , vol.2 , Issue.6 , pp. 415-418
    • Inoue, T.1    Heo, W.D.2    Grimley, J.S.3    Wandless, T.J.4    Meyer, T.5
  • 25
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A (1995) Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81(1):53-62.
    • (1995) Cell , vol.81 , Issue.1 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 26
    • 84873676027 scopus 로고    scopus 로고
    • Deciphering the molecular and functional basis of Dbl family proteins: A novel systematic approach toward classification of selective activation of the Rho family proteins
    • Jaiswal M, Dvorsky R, Ahmadian MR (2013) Deciphering the molecular and functional basis of Dbl family proteins: A novel systematic approach toward classification of selective activation of the Rho family proteins. J Biol Chem 288(6):4486-4500.
    • (2013) J Biol Chem , vol.288 , Issue.6 , pp. 4486-4500
    • Jaiswal, M.1    Dvorsky, R.2    Ahmadian, M.R.3
  • 27
    • 84871288267 scopus 로고    scopus 로고
    • PFunkel: Efficient, expansive, user-defined mutagenesis
    • Firnberg E, Ostermeier M (2012) PFunkel: Efficient, expansive, user-defined mutagenesis. PLoS ONE 7(12):e52031.
    • (2012) PLoS ONE , vol.7 , Issue.12 , pp. e52031
    • Firnberg, E.1    Ostermeier, M.2
  • 28
    • 34250748507 scopus 로고    scopus 로고
    • Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries
    • Tonikian R, Zhang Y, Boone C, Sidhu SS (2007) Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries. Nat Protoc 2(6):1368-1386.
    • (2007) Nat Protoc , vol.2 , Issue.6 , pp. 1368-1386
    • Tonikian, R.1    Zhang, Y.2    Boone, C.3    Sidhu, S.S.4
  • 29
    • 84862520770 scopus 로고    scopus 로고
    • Fiji: An open-source platform for biological-image analysis
    • Schindelin J, et al. (2012) Fiji: An open-source platform for biological-image analysis. Nat Methods 9(7):676-682.
    • (2012) Nat Methods , vol.9 , Issue.7 , pp. 676-682
    • Schindelin, J.1


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