메뉴 건너뛰기




Volumn 287, Issue 37, 2012, Pages 31515-31526

Identifying key juxtamembrane interactions in cell membranes using AraC-based transcriptional reporter assay (AraTM)

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCTS; BACTERIAL MEMBRANES; CONSTITUTIVELY ACTIVES; EXTRACELLULAR; HEK293 CELLS; HOMODIMERIZATION; INTEGRINS; INTRACELLULAR SIGNALING; LIGAND BINDING; LIGAND RECOGNITION; MEMBRANE TRAFFICKING; REGULATORY MECHANISM; REPORTER ASSAY; REVERSE ORIENTATION; SPECIFIC INTERACTION; SPECIFIC INTERFACE; TRANSMEMBRANES; WILD TYPES;

EID: 84866076617     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.396895     Document Type: Article
Times cited : (22)

References (40)
  • 1
    • 0031892994 scopus 로고    scopus 로고
    • Dimerization as a regulatory mechanism in signal transduction
    • Klemm, J. D., Schreiber, S. L., and Crabtree, G. R. (1998) Dimerization as a regulatory mechanism in signal transduction. Annu. Rev. Immunol. 16, 569-592
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 569-592
    • Klemm, J.D.1    Schreiber, S.L.2    Crabtree, G.R.3
  • 2
    • 46049088691 scopus 로고    scopus 로고
    • Protein-protein interactions in the membrane: Sequence, structural, and biological motifs
    • Moore, D. T., Berger, B. W., and DeGrado, W. F. (2008) Protein-protein interactions in the membrane: sequence, structural, and biological motifs. Structure 16, 991-1001
    • (2008) Structure , vol.16 , pp. 991-1001
    • Moore, D.T.1    Berger, B.W.2    DeGrado, W.F.3
  • 3
    • 31044441154 scopus 로고    scopus 로고
    • Structure and function of the platelet integrin αIIbβ3
    • Bennett, J. S. (2005) Structure and function of the platelet integrin αIIbβ3. J. Clin. Investig. 115, 3363-3369
    • (2005) J. Clin. Investig. , vol.115 , pp. 3363-3369
    • Bennett, J.S.1
  • 5
    • 69749117731 scopus 로고    scopus 로고
    • Multiple approaches converge on the structure of the integrin αIIb/β3 transmembrane heterodimer
    • Metcalf, D. G., Kulp, D. W., Bennett, J. S., and DeGrado, W. F. (2009) Multiple approaches converge on the structure of the integrin αIIb/β3 transmembrane heterodimer. J. Mol. Biol. 392, 1087-1101
    • (2009) J. Mol. Biol. , vol.392 , pp. 1087-1101
    • Metcalf, D.G.1    Kulp, D.W.2    Bennett, J.S.3    DeGrado, W.F.4
  • 6
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin αIIbβ3: Roles of the transmembrane and cytoplasmic domains
    • Li, R., Babu, C. R., Lear, J. D., Wand, A. J., Bennett, J. S., and DeGrado, W. F. (2001) Oligomerization of the integrin αIIbβ3: roles of the transmembrane and cytoplasmic domains. Proc. Natl. Acad. Sci. U.S.A. 98, 12462-12467
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12462-12467
    • Li, R.1    Babu, C.R.2    Lear, J.D.3    Wand, A.J.4    Bennett, J.S.5    DeGrado, W.F.6
  • 8
    • 53049109463 scopus 로고    scopus 로고
    • Juxtamembrane basic residues in glycoprotein Ibβ cytoplasmic domain are required for assembly and surface expression of glycoprotein Ib-IX complex
    • Mo, X., Luo, S. Z., López, J. A., and Li, R. (2008) Juxtamembrane basic residues in glycoprotein Ibβ cytoplasmic domain are required for assembly and surface expression of glycoprotein Ib-IX complex. FEBS Lett. 582, 3270-3274
    • (2008) FEBS Lett. , vol.582 , pp. 3270-3274
    • Mo, X.1    Luo, S.Z.2    López, J.A.3    Li, R.4
  • 9
    • 52449117744 scopus 로고    scopus 로고
    • The membrane-proximal intermolecular disulfide bonds in glycoprotein Ib influence receptor binding to von Willebrand factor
    • Mo, X., Luo, S. Z., Munday, A. D., Sun, W., Berndt, M. C., López, J. A., Dong, J. F., and Li, R. (2008) The membrane-proximal intermolecular disulfide bonds in glycoprotein Ib influence receptor binding to von Willebrand factor. J. Thrombosis Haemostasis 6, 1789-1795
    • (2008) J. Thrombosis Haemostasis , vol.6 , pp. 1789-1795
    • Mo, X.1    Luo, S.Z.2    Munday, A.D.3    Sun, W.4    Berndt, M.C.5    López, J.A.6    Dong, J.F.7    Li, R.8
  • 10
    • 76749147499 scopus 로고    scopus 로고
    • Strong oligomerization behavior of PDGFβ receptor transmembrane domain and its regulation by the juxtamembrane regions
    • Oates, J., King, G., and Dixon, A. M. (2010) Strong oligomerization behavior of PDGFβ receptor transmembrane domain and its regulation by the juxtamembrane regions. Biochim. Biophys. Acta 1798, 605-615
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 605-615
    • Oates, J.1    King, G.2    Dixon, A.M.3
  • 11
    • 0037474296 scopus 로고    scopus 로고
    • GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane
    • Schneider, D., and Engelman, D. M. (2003) GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane. J. Biol. Chem. 278, 3105-3111
    • (2003) J. Biol. Chem. , vol.278 , pp. 3105-3111
    • Schneider, D.1    Engelman, D.M.2
  • 12
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ, W. P., and Engelman, D. M. (1999) TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl. Acad. Sci. U.S.A. 96, 863-868
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 13
    • 0035824509 scopus 로고    scopus 로고
    • In vitro selection of membrane-spanning leucine zipper protein-protein interaction motifs using POSSYCCAT
    • Gurezka, R., and Langosch, D. (2001) In vitro selection of membrane-spanning leucine zipper protein-protein interaction motifs using POSSYCCAT. J. Biol. Chem. 276, 45580-45587
    • (2001) J. Biol. Chem. , vol.276 , pp. 45580-45587
    • Gurezka, R.1    Langosch, D.2
  • 15
    • 0033710436 scopus 로고    scopus 로고
    • Genetic systems for analyzing protein-protein interactions in bacteria
    • Ladant, D., and Karimova, G. (2000) Genetic systems for analyzing protein-protein interactions in bacteria. Res. Microbiol. 151, 711-720
    • (2000) Res. Microbiol. , vol.151 , pp. 711-720
    • Ladant, D.1    Karimova, G.2
  • 16
    • 0026519517 scopus 로고
    • Co-ordinate expression of virulence genes by ToxR in V. cholerae
    • DiRita, V. J. (1992) Co-ordinate expression of virulence genes by ToxR in V. cholerae. Mol. Microbiol. 6, 451-458
    • (1992) Mol. Microbiol. , vol.6 , pp. 451-458
    • DiRita, V.J.1
  • 17
    • 0037092503 scopus 로고    scopus 로고
    • Integral membrane protein biosynthesis: Why topology is hard to predict
    • Ott, C. M., and Lingappa, V. R. (2002) Integral membrane protein biosynthesis: why topology is hard to predict. J. Cell Sci. 115, 2003-2009
    • (2002) J. Cell Sci. , vol.115 , pp. 2003-2009
    • Ott, C.M.1    Lingappa, V.R.2
  • 18
    • 0029115282 scopus 로고
    • Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures
    • Kolmar, H., Hennecke, F., Götze, K., Janzer, B., Vogt, B., Mayer, F., and Fritz, H. J. (1995) Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures. EMBO J. 14, 3895-3904
    • (1995) EMBO J. , vol.14 , pp. 3895-3904
    • Kolmar, H.1    Hennecke, F.2    Götze, K.3    Janzer, B.4    Vogt, B.5    Mayer, F.6    Fritz, H.J.7
  • 20
    • 0030759410 scopus 로고    scopus 로고
    • Gene expression from plasmids containing the araBAD promoter at subsaturating inducer concentrations represents mixed populations
    • Siegele, D. A., and Hu, J. C. (1997) Gene expression from plasmids containing the araBAD promoter at subsaturating inducer concentrations represents mixed populations. Proc. Natl. Acad. Sci. U.S.A. 94, 8168-8172
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8168-8172
    • Siegele, D.A.1    Hu, J.C.2
  • 21
    • 78649869175 scopus 로고    scopus 로고
    • Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms
    • Bonde, M. M., Hansen, J. T., Sanni, S. J., Hauns, S., Gammeltoft, S., Lyngs, C., and Hansen, J. L. (2010) Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms. PLoS ONE 5
    • (2010) PLoS ONE , vol.5
    • Bonde, M.M.1    Hansen, J.T.2    Sanni, S.J.3    Hauns, S.4    Gammeltoft, S.5    Lyngs, C.6    Hansen, J.L.7
  • 22
    • 0037337551 scopus 로고    scopus 로고
    • AraC protein: A love-hate relationship
    • Schleif, R. (2003) AraC protein: a love-hate relationship. BioEssays 25, 274-282
    • (2003) BioEssays , vol.25 , pp. 274-282
    • Schleif, R.1
  • 23
    • 33751540017 scopus 로고    scopus 로고
    • Specific interactions by the N-terminal arm inhibit self-association of the AraC dimerization domain
    • Weldon, J. E., and Schleif, R. F. (2006) Specific interactions by the N-terminal arm inhibit self-association of the AraC dimerization domain. Protein Science 15, 2828-2835
    • (2006) Protein Science , vol.15 , pp. 2828-2835
    • Weldon, J.E.1    Schleif, R.F.2
  • 25
    • 0028337332 scopus 로고
    • Maltose transport system of E. coli: An ABC-type transporter
    • Nikaido, H. (1994) Maltose transport system of E. coli: an ABC-type transporter. FEBS Lett. 346, 55-58
    • (1994) FEBS Lett. , vol.346 , pp. 55-58
    • Nikaido, H.1
  • 26
    • 2942700100 scopus 로고    scopus 로고
    • Dimerization of the transmembrane domain of Integrin αIIb subunit in cell membranes
    • Li, R., Gorelik, R., Nanda, V., Law, P. B., Lear, J. D., DeGrado, W. F., and Bennett, J. S. (2004) Dimerization of the transmembrane domain of Integrin αIIb subunit in cell membranes. J. Biol. Chem. 279, 26666-26673
    • (2004) J. Biol. Chem. , vol.279 , pp. 26666-26673
    • Li, R.1    Gorelik, R.2    Nanda, V.3    Law, P.B.4    Lear, J.D.5    DeGrado, W.F.6    Bennett, J.S.7
  • 27
    • 1642396353 scopus 로고    scopus 로고
    • Involvement of transmembrane domain interactions in signal transduction by α/β integrins
    • Schneider, D., and Engelman, D. (2004) Involvement of transmembrane domain interactions in signal transduction by α/β integrins. J. Biol. Chem. 279, 9840-9846
    • (2004) J. Biol. Chem. , vol.279 , pp. 9840-9846
    • Schneider, D.1    Engelman, D.2
  • 28
    • 0034795140 scopus 로고    scopus 로고
    • The multi-ligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
    • Schmidt, A. M., Yan, S. D., Yan, S. F., and Stern, D. M. (2001) The multi-ligand receptor RAGE as a progression factor amplifying immune and inflammatory responses. J. Clin. Investig. 108, 949-955
    • (2001) J. Clin. Investig. , vol.108 , pp. 949-955
    • Schmidt, A.M.1    Yan, S.D.2    Yan, S.F.3    Stern, D.M.4
  • 31
    • 77954891042 scopus 로고    scopus 로고
    • Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction
    • Zong, H., Madden, A., Ward, M., Mooney, M. H., Elliott, C. T., and Stitt, A. W. (2010) Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction. J. Biol. Chem. 285, 23137
    • (2010) J. Biol. Chem. , vol.285 , pp. 23137
    • Zong, H.1    Madden, A.2    Ward, M.3    Mooney, M.H.4    Elliott, C.T.5    Stitt, A.W.6
  • 32
    • 33947510205 scopus 로고    scopus 로고
    • Hexameric calgranulin C (S100A12) binds to the receptor for advanced glycated end products (RAGE) using symmetric hydrophobic target-binding patches
    • Xie, J., Burz, D. S., He, W., Bronstein, I. B., Lednev, I., and Shekhtman, A. (2007) Hexameric calgranulin C (S100A12) binds to the receptor for advanced glycated end products (RAGE) using symmetric hydrophobic target-binding patches. J. Biol. Chem. 282, 4218-4231
    • (2007) J. Biol. Chem. , vol.282 , pp. 4218-4231
    • Xie, J.1    Burz, D.S.2    He, W.3    Bronstein, I.B.4    Lednev, I.5    Shekhtman, A.6
  • 33
    • 0037101774 scopus 로고    scopus 로고
    • Homoand hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences
    • Ramsay, D., Kellett, E., McVey, M., Rees, S., and Milligan, G. (2002) Homoand hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences. Biochem. J. 365, 429-440
    • (2002) Biochem. J. , vol.365 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 34
    • 0037674763 scopus 로고    scopus 로고
    • Detection of integrin αIIbβ3 clustering in living cells
    • Buensuceso, C. (2003) Detection of integrin αIIbβ3 clustering in living cells. J Biol. Chem. 278, 15217-15224
    • (2003) J Biol. Chem. , vol.278 , pp. 15217-15224
    • Buensuceso, C.1
  • 35
    • 55249118389 scopus 로고    scopus 로고
    • Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE)
    • Xie, J., Reverdatto, S., Frolov, A., Hoffmann, R., Burz, D. S., and Shekhtman, A. (2008) Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE). J. Biol. Chem. 283, 27255-27269
    • (2008) J. Biol. Chem. , vol.283 , pp. 27255-27269
    • Xie, J.1    Reverdatto, S.2    Frolov, A.3    Hoffmann, R.4    Burz, D.S.5    Shekhtman, A.6
  • 36
    • 34447271539 scopus 로고    scopus 로고
    • Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations
    • Duong, M. T., Jaszewski, T. M., Fleming, K. G., and MacKenzie, K. R. (2007) Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations. J. Mol. Biol. 371, 422-434
    • (2007) J. Mol. Biol. , vol.371 , pp. 422-434
    • Duong, M.T.1    Jaszewski, T.M.2    Fleming, K.G.3    MacKenzie, K.R.4
  • 37
    • 84856873812 scopus 로고    scopus 로고
    • Signal transduction in receptor for advanced glycation end products (RAGE): Solution structure of C-terminal rage (ctRAGE) and its binding to mDia1
    • Rai, V., Maldonado, A. Y., Burz, D. S., Reverdatto, S., Yan, S. F., Schmidt, A. M., and Shekhtman, A. (2012) Signal transduction in receptor for advanced glycation end products (RAGE): solution structure of C-terminal rage (ctRAGE) and its binding to mDia1. J. Biol. Chem. 287, 5133-5144
    • (2012) J. Biol. Chem. , vol.287 , pp. 5133-5144
    • Rai, V.1    Maldonado, A.Y.2    Burz, D.S.3    Reverdatto, S.4    Yan, S.F.5    Schmidt, A.M.6    Shekhtman, A.7
  • 38
    • 0031053068 scopus 로고    scopus 로고
    • Cloning a new human gene from chromosome 21q22.3 encoding a glutamic acid-rich protein expressed in heart and skeletal muscle
    • Scartezzini, P., Egeo, A., Colella, S., Fumagalli, P., Arrigo, P., Nizetic, D., Taramelli, R., and Rasore-Quartino, A. (1997) Cloning a new human gene from chromosome 21q22.3 encoding a glutamic acid-rich protein expressed in heart and skeletal muscle. Human Genetics 99, 387-392
    • (1997) Human Genetics , vol.99 , pp. 387-392
    • Scartezzini, P.1    Egeo, A.2    Colella, S.3    Fumagalli, P.4    Arrigo, P.5    Nizetic, D.6    Taramelli, R.7    Rasore-Quartino, A.8
  • 40
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A., and Ladant, D. (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. U.S.A. 95, 5752-5756
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.