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Volumn 406, Issue 2, 2011, Pages 343-353

Genetic incorporation of a photo-crosslinkable amino acid reveals novel protein complexes with GRB2 in mammalian cells

Author keywords

cell signaling; genetic code expansion; mass spectrometry; nonnatural amino acid; Src homology 2 domain

Indexed keywords

ALPHA TUBULIN; DYNAMIN I; DYNAMIN II; DYNAMIN III; EPIDERMAL GROWTH FACTOR; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; PROTEIN SH2; PROTEIN SH3; SYNAPTOJANIN;

EID: 79251597864     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.12.022     Document Type: Article
Times cited : (46)

References (45)
  • 1
    • 3242675407 scopus 로고    scopus 로고
    • Glutathione-S-transferase-fusion based assays for studying protein-protein interactions
    • Vikis H.G., and Guan K.L. Glutathione-S-transferase-fusion based assays for studying protein-protein interactions Methods Mol. Biol. 261 2004 175 186
    • (2004) Methods Mol. Biol. , vol.261 , pp. 175-186
    • Vikis, H.G.1    Guan, K.L.2
  • 2
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B., Kratchmarova I., Ong S.E., Nielsen M., Foster L.J., and Mann M. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling Nat. Biotechnol. 21 2003 315 318
    • (2003) Nat. Biotechnol. , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 3
  • 4
    • 18744389180 scopus 로고    scopus 로고
    • Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells
    • Suchanek M., Radzikowska A., and Thiele C. Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells Nat. Methods 2 2005 261 267
    • (2005) Nat. Methods , vol.2 , pp. 261-267
    • Suchanek, M.1    Radzikowska, A.2    Thiele, C.3
  • 5
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli
    • Chin J.W., Martin A.B., King D.S., Wang L., and Schultz P.G. Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli Proc. Natl Acad. Sci. USA 99 2002 11020 11024
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 6
    • 38849085321 scopus 로고    scopus 로고
    • A genetically encoded diazirine photocrosslinker in Escherichia coli
    • Tippmann E.M., Liu W., Summerer D., Mack A.V., and Schultz P.G. A genetically encoded diazirine photocrosslinker in Escherichia coli ChemBioChem 8 2007 2210 2214
    • (2007) ChemBioChem , vol.8 , pp. 2210-2214
    • Tippmann, E.M.1    Liu, W.2    Summerer, D.3    MacK, A.V.4    Schultz, P.G.5
  • 8
    • 18744396951 scopus 로고    scopus 로고
    • Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid
    • Hino N., Okazaki Y., Kobayashi T., Hayashi A., Sakamoto K., and Yokoyama S. Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid Nat. Methods 2 2005 201 206
    • (2005) Nat. Methods , vol.2 , pp. 201-206
    • Hino, N.1    Okazaki, Y.2    Kobayashi, T.3    Hayashi, A.4    Sakamoto, K.5    Yokoyama, S.6
  • 9
    • 38349107042 scopus 로고    scopus 로고
    • Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis
    • Ye S., Köhrer C., Huber T., Kazmi M., Sachdev P., and Yan E.C. Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis J. Biol. Chem. 285 2008 1525 1533
    • (2008) J. Biol. Chem. , vol.285 , pp. 1525-1533
    • Ye, S.1    Köhrer, C.2    Huber, T.3    Kazmi, M.4    Sachdev, P.5    Yan, E.C.6
  • 10
    • 0036849244 scopus 로고    scopus 로고
    • Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells
    • Sakamoto K., Hayashi A., Sakamoto A., Kiga D., Nakayama H., and Soma A. Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells Nucleic Acids Res. 30 2002 4692 4699
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4692-4699
    • Sakamoto, K.1    Hayashi, A.2    Sakamoto, A.3    Kiga, D.4    Nakayama, H.5    Soma, A.6
  • 11
    • 18144435747 scopus 로고    scopus 로고
    • A possible approach to site-specific insertion of two different unnatural amino acids into proteins in mammalian cells via nonsense suppression
    • Köhrer C., Yoo J.H., Bennett M., Schaack J., and RajBhandary U.L. A possible approach to site-specific insertion of two different unnatural amino acids into proteins in mammalian cells via nonsense suppression Chem. Biol. 10 2003 1095 1102
    • (2003) Chem. Biol. , vol.10 , pp. 1095-1102
    • Köhrer, C.1    Yoo, J.H.2    Bennett, M.3    Schaack, J.4    Rajbhandary, U.L.5
  • 13
    • 33847648384 scopus 로고    scopus 로고
    • Genetic incorporation of unnatural amino acids into proteins in mammalian cells
    • Liu W., Brock A., Chen S., Chen S., and Schultz P.G. Genetic incorporation of unnatural amino acids into proteins in mammalian cells Nat. Methods 4 2007 239 244
    • (2007) Nat. Methods , vol.4 , pp. 239-244
    • Liu, W.1    Brock, A.2    Chen, S.3    Chen, S.4    Schultz, P.G.5
  • 14
    • 33645658328 scopus 로고    scopus 로고
    • Stereospecific synthesis of a carbene-generating angiotensin II analogue for comparative photoaffinity labeling: Improved incorporation and absence of methionine selectivity
    • Fillion D., Deraët M., Holleran B.J., and Escher E. Stereospecific synthesis of a carbene-generating angiotensin II analogue for comparative photoaffinity labeling: improved incorporation and absence of methionine selectivity J. Med. Chem. 49 2006 2200 2209
    • (2006) J. Med. Chem. , vol.49 , pp. 2200-2209
    • Fillion, D.1    Deraët, M.2    Holleran, B.J.3    Escher, E.4
  • 15
    • 0025216163 scopus 로고
    • A bacterial amber suppressor in Saccharomyces cerevisiae is selectively recognized by a bacterial aminoacyl-tRNA synthetase
    • Edwards H., and Schimmel P. A bacterial amber suppressor in Saccharomyces cerevisiae is selectively recognized by a bacterial aminoacyl-tRNA synthetase Mol. Cell. Biol. 10 1990 1633 1641
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1633-1641
    • Edwards, H.1    Schimmel, P.2
  • 16
    • 0030029337 scopus 로고    scopus 로고
    • Amber suppression in mammalian cells dependent upon expression of an Escherichia coli aminoacyl-tRNA synthetase gene
    • Drabkin H.J., Park H.J., and RajBhandary U.L. Amber suppression in mammalian cells dependent upon expression of an Escherichia coli aminoacyl-tRNA synthetase gene Mol. Cell. Biol. 16 1996 907 913
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 907-913
    • Drabkin, H.J.1    Park, H.J.2    Rajbhandary, U.L.3
  • 17
    • 0037162453 scopus 로고    scopus 로고
    • An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system
    • Kiga D., Sakamoto K., Kodama K., Kigawa T., Matsuda T., and Yabuki T. An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system Proc. Natl Acad. Sci. USA 99 2002 9715 9720
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9715-9720
    • Kiga, D.1    Sakamoto, K.2    Kodama, K.3    Kigawa, T.4    Matsuda, T.5    Yabuki, T.6
  • 18
    • 34548813605 scopus 로고    scopus 로고
    • Site-specific incorporation of non-natural amino acids into proteins in mammalian cells with an expanded genetic code
    • Hino N., Hayashi A., Sakamoto K., and Yokoyama S. Site-specific incorporation of non-natural amino acids into proteins in mammalian cells with an expanded genetic code Nat. Protoc. 1 2007 2957 2962
    • (2007) Nat. Protoc. , vol.1 , pp. 2957-2962
    • Hino, N.1    Hayashi, A.2    Sakamoto, K.3    Yokoyama, S.4
  • 20
    • 0026678172 scopus 로고
    • Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • Rozakis-Adcock M., McGlade J., Mbamalu G., Pelicci G., Daly R., and Li W. Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases Nature 360 1992 689 692
    • (1992) Nature , vol.360 , pp. 689-692
    • Rozakis-Adcock, M.1    McGlade, J.2    Mbamalu, G.3    Pelicci, G.4    Daly, R.5    Li, W.6
  • 21
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., and Pandey A. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 1 2002 376 386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 22
    • 61649097515 scopus 로고    scopus 로고
    • Temporal perturbation of tyrosine phosphoproteome dynamics reveals the system-wide regulatory networks
    • Oyama M., Kozuka-Hata H., Tasaki S., Semba K., Hattori S., and Sugano S. Temporal perturbation of tyrosine phosphoproteome dynamics reveals the system-wide regulatory networks Mol. Cell. Proteomics 8 2009 226 231
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 226-231
    • Oyama, M.1    Kozuka-Hata, H.2    Tasaki, S.3    Semba, K.4    Hattori, S.5    Sugano, S.6
  • 23
    • 0029844431 scopus 로고    scopus 로고
    • Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584
    • Vogel W., and Ullrich A. Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584 Cell Growth Differ. 7 1996 1589 1597
    • (1996) Cell Growth Differ. , vol.7 , pp. 1589-1597
    • Vogel, W.1    Ullrich, A.2
  • 24
    • 0031033105 scopus 로고    scopus 로고
    • Multiple Grb2-protein complexes in human cancer cells
    • Sastry L., Cao T., and King C.R. Multiple Grb2-protein complexes in human cancer cells Int. J. Cancer 70 1997 208 213
    • (1997) Int. J. Cancer , vol.70 , pp. 208-213
    • Sastry, L.1    Cao, T.2    King, C.R.3
  • 25
    • 0032571273 scopus 로고    scopus 로고
    • Grb2 and its apoptotic isoform Grb3-3 associate with heterogeneous nuclear ribonucleoprotein C, and these interactions are modulated by poly(U) RNA
    • Romero F., Ramos-Morales F., Domínguez A., Rios R.M., Schweighoffer F., and Tocqué B. Grb2 and its apoptotic isoform Grb3-3 associate with heterogeneous nuclear ribonucleoprotein C, and these interactions are modulated by poly(U) RNA J. Biol. Chem. 273 1998 7776 7781
    • (1998) J. Biol. Chem. , vol.273 , pp. 7776-7781
    • Romero, F.1    Ramos-Morales, F.2    Domínguez, A.3    Rios, R.M.4    Schweighoffer, F.5    Tocqué, B.6
  • 26
    • 0028811668 scopus 로고
    • Heterogeneous nuclear ribonucleoproteins H, H′, and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes
    • Honoré B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., and Gromov P. Heterogeneous nuclear ribonucleoproteins H, H′, and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes J. Biol. Chem. 270 1995 28780 28789
    • (1995) J. Biol. Chem. , vol.270 , pp. 28780-28789
    • Honoré, B.1    Rasmussen, H.H.2    Vorum, H.3    Dejgaard, K.4    Liu, X.5    Gromov, P.6
  • 28
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee B.J., Cansizoglu A.E., Süel K.E., Louis T.H., Zhang Z., and Chook Y.M. Rules for nuclear localization sequence recognition by karyopherin beta 2 Cell 126 2006 543 558
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Süel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 29
    • 77951990307 scopus 로고    scopus 로고
    • A glycine-rich domain of hnRNP H/F promotes nucleocytoplasmic shuttling and nuclear import through an interaction with transportin 1
    • Van Dusen C.M., Yee L., McNally L.M., and McNally M.T. A glycine-rich domain of hnRNP H/F promotes nucleocytoplasmic shuttling and nuclear import through an interaction with transportin 1 Mol. Cell. Biol. 30 2010 2552 2562
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2552-2562
    • Van Dusen, C.M.1    Yee, L.2    McNally, L.M.3    McNally, M.T.4
  • 30
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase
    • Schlaepfer D.D., Hanks S.K., Hunter T., and van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase Nature 372 1994 786 791
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 31
    • 0028000009 scopus 로고
    • Activation of the Ras signalling pathway in human breast cancer cells overexpressing erbB-2
    • Janes P.W., Daly R.J., deFazio A., and Sutherland R.L. Activation of the Ras signalling pathway in human breast cancer cells overexpressing erbB-2 Oncogene 9 1994 3601 3608
    • (1994) Oncogene , vol.9 , pp. 3601-3608
    • Janes, P.W.1    Daly, R.J.2    Defazio, A.3    Sutherland, R.L.4
  • 32
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
    • Lowenstein E.J., Daly R.J., Batzer A.G., Li W., Margolis B., and Lammers R. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling Cell 70 1992 431 442
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1    Daly, R.J.2    Batzer, A.G.3    Li, W.4    Margolis, B.5    Lammers, R.6
  • 33
    • 10744226991 scopus 로고    scopus 로고
    • GIT1 mediates Src-dependent activation of phospholipase C gamma by angiotensin II and epidermal growth factor
    • Haendeler J., Yin G., Hojo Y., Saito Y., Melaragno M., and Yan C. GIT1 mediates Src-dependent activation of phospholipase C gamma by angiotensin II and epidermal growth factor J. Biol. Chem. 278 2003 49936 49944
    • (2003) J. Biol. Chem. , vol.278 , pp. 49936-49944
    • Haendeler, J.1    Yin, G.2    Hojo, Y.3    Saito, Y.4    Melaragno, M.5    Yan, C.6
  • 36
    • 33646705915 scopus 로고    scopus 로고
    • The multifunctional GIT family of proteins
    • Hoefen R.J., and Berk B.C. The multifunctional GIT family of proteins J. Cell Sci. 119 2006 1469 1475
    • (2006) J. Cell Sci. , vol.119 , pp. 1469-1475
    • Hoefen, R.J.1    Berk, B.C.2
  • 37
    • 20744450092 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein F/H proteins modulate the alternative splicing of the apoptotic mediator Bcl-x
    • Garneau D., Revil T., Fisette J.F., and Chabot B. Heterogeneous nuclear ribonucleoprotein F/H proteins modulate the alternative splicing of the apoptotic mediator Bcl-x J. Biol. Chem. 280 2005 22641 22650
    • (2005) J. Biol. Chem. , vol.280 , pp. 22641-22650
    • Garneau, D.1    Revil, T.2    Fisette, J.F.3    Chabot, B.4
  • 38
    • 69249087295 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-xS splice isoform
    • Revil T., Pelletier J., Toutant J., Cloutier A., and Chabot B. Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-xS splice isoform J. Biol. Chem. 284 2009 21458 21467
    • (2009) J. Biol. Chem. , vol.284 , pp. 21458-21467
    • Revil, T.1    Pelletier, J.2    Toutant, J.3    Cloutier, A.4    Chabot, B.5
  • 39
    • 2442435550 scopus 로고    scopus 로고
    • P54(nrb) associates with the 5′ splice site within large transcription/splicing complexes
    • Kameoka S., Duque P., and Konarska M.M. p54(nrb) associates with the 5′ splice site within large transcription/splicing complexes EMBO J. 23 2004 1782 1791
    • (2004) EMBO J. , vol.23 , pp. 1782-1791
    • Kameoka, S.1    Duque, P.2    Konarska, M.M.3
  • 40
    • 0031032041 scopus 로고    scopus 로고
    • The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68
    • Lawe D.C., Hahn C., and Wong A.J. The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68 Oncogene 14 1997 223 231
    • (1997) Oncogene , vol.14 , pp. 223-231
    • Lawe, D.C.1    Hahn, C.2    Wong, A.J.3
  • 41
    • 35148833199 scopus 로고    scopus 로고
    • The association of Sam68 with Vav1 contributes to tumorigenesis
    • Lazer G., Pe'er L., Schapira V., Richard S., and Katzav S. The association of Sam68 with Vav1 contributes to tumorigenesis Cell. Signalling 19 2007 2479 2486
    • (2007) Cell. Signalling , vol.19 , pp. 2479-2486
    • Lazer, G.1    Pe'Er, L.2    Schapira, V.3    Richard, S.4    Katzav, S.5
  • 42
    • 0032489365 scopus 로고    scopus 로고
    • Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C. Evidence for Vav-hnRNP interactions in an RNA-dependent manner
    • Romero F., Germani A., Puvion E., Camonis J., Varin-Blank N., and Gisselbrecht S. Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C. Evidence for Vav-hnRNP interactions in an RNA-dependent manner J. Biol. Chem. 273 1998 5923 5931
    • (1998) J. Biol. Chem. , vol.273 , pp. 5923-5931
    • Romero, F.1    Germani, A.2    Puvion, E.3    Camonis, J.4    Varin-Blank, N.5    Gisselbrecht, S.6
  • 43
    • 0030867556 scopus 로고    scopus 로고
    • Grb2 overexpression in nuclei and cytoplasm of human breast cells: A histochemical and biochemical study of normal and neoplastic mammary tissue specimens
    • Verbeek B.S., Adriaansen-Slot S.S., Rijksen G., and Vroom T.M. Grb2 overexpression in nuclei and cytoplasm of human breast cells: a histochemical and biochemical study of normal and neoplastic mammary tissue specimens J. Pathol. 183 1997 195 203
    • (1997) J. Pathol. , vol.183 , pp. 195-203
    • Verbeek, B.S.1    Adriaansen-Slot, S.S.2    Rijksen, G.3    Vroom, T.M.4
  • 44
    • 68049110634 scopus 로고    scopus 로고
    • The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site
    • Bae J.H., Lew E.D., Yuzawa S., Tomé F., Lax I., and Schlessinger J. The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site Cell 138 2009 514 524
    • (2009) Cell , vol.138 , pp. 514-524
    • Bae, J.H.1    Lew, E.D.2    Yuzawa, S.3    Tomé, F.4    Lax, I.5    Schlessinger, J.6
  • 45
    • 44149083513 scopus 로고    scopus 로고
    • Adding l-lysine derivatives to the genetic code of mammalian cells with engineered pyrrolysyl-tRNA synthetases
    • Mukai T., Kobayashi T., Hino N., Yanagisawa T., Sakamoto K., and Yokoyama S. Adding l-lysine derivatives to the genetic code of mammalian cells with engineered pyrrolysyl-tRNA synthetases Biochem. Biophys. Res. Commun. 371 2008 818 822
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 818-822
    • Mukai, T.1    Kobayashi, T.2    Hino, N.3    Yanagisawa, T.4    Sakamoto, K.5    Yokoyama, S.6


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