메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages 2479-2484

Rapid transfer of transmembrane proteins for single molecule dimerization assays in polymer-supported membranes

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; MEMBRANE PROTEIN; POLYMER;

EID: 84914118707     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb5005806     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 84862670921 scopus 로고    scopus 로고
    • Strategies for membrane interaction proteomics: No mass spectrometry required
    • Lam, M. H. and Stagljar, I. (2012) Strategies for membrane interaction proteomics: No mass spectrometry required Proteomics 12, 1519-1526
    • (2012) Proteomics , vol.12 , pp. 1519-1526
    • Lam, M.H.1    Stagljar, I.2
  • 2
    • 78650147139 scopus 로고    scopus 로고
    • Allostery at G protein-coupled receptor homo- and heteromers: Uncharted pharmacological landscapes
    • Smith, N. J. and Milligan, G. (2010) Allostery at G protein-coupled receptor homo- and heteromers: Uncharted pharmacological landscapes Pharmacol Rev. 62, 701-725
    • (2010) Pharmacol Rev. , vol.62 , pp. 701-725
    • Smith, N.J.1    Milligan, G.2
  • 3
    • 84879882018 scopus 로고    scopus 로고
    • Allosteric modulation and functional selectivity of G protein-coupled receptors
    • Gao, Z. G. and Jacobson, K. A. (2013) Allosteric modulation and functional selectivity of G protein-coupled receptors Drug Discov. Today Technol. 10, e237-e243
    • (2013) Drug Discov. Today Technol. , vol.10 , pp. 237-e243
    • Gao, Z.G.1    Jacobson, K.A.2
  • 4
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M. A. and Schlessinger, J. (2010) Cell signaling by receptor tyrosine kinases Cell 141, 1117-1134
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 9
    • 80855133525 scopus 로고    scopus 로고
    • Cell membranes: The lipid perspective
    • Coskun, U. and Simons, K. (2011) Cell membranes: the lipid perspective Structure 19, 1543-1548
    • (2011) Structure , vol.19 , pp. 1543-1548
    • Coskun, U.1    Simons, K.2
  • 10
    • 84856153687 scopus 로고    scopus 로고
    • Nanoscale membrane organization: Where biochemistry meets advanced microscopy
    • Cambi, A. and Lidke, D. S. (2012) Nanoscale membrane organization: Where biochemistry meets advanced microscopy ACS Chem. Biol. 7, 139-149
    • (2012) ACS Chem. Biol. , vol.7 , pp. 139-149
    • Cambi, A.1    Lidke, D.S.2
  • 11
    • 77951923713 scopus 로고    scopus 로고
    • Hierarchical organization of the plasma membrane: Investigations by single-molecule tracking vs. Fluorescence correlation spectroscopy
    • Kusumi, A., Shirai, Y. M., Koyama-Honda, I., Suzuki, K. G., and Fujiwara, T. K. (2010) Hierarchical organization of the plasma membrane: investigations by single-molecule tracking vs. fluorescence correlation spectroscopy FEBS Lett. 584, 1814-1823
    • (2010) FEBS Lett. , vol.584 , pp. 1814-1823
    • Kusumi, A.1    Shirai, Y.M.2    Koyama-Honda, I.3    Suzuki, K.G.4    Fujiwara, T.K.5
  • 12
    • 36549043460 scopus 로고    scopus 로고
    • Model membrane systems and their applications
    • Chan, Y. H. and Boxer, S. G. (2007) Model membrane systems and their applications Curr. Opin Chem. Biol. 11, 581-587
    • (2007) Curr. Opin Chem. Biol. , vol.11 , pp. 581-587
    • Chan, Y.H.1    Boxer, S.G.2
  • 14
    • 0033860735 scopus 로고    scopus 로고
    • Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: Silane-polyethyleneglycol-lipid as a cushion and covalent linker
    • Wagner, M. L. and Tamm, L. K. (2000) Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: Silane-polyethyleneglycol-lipid as a cushion and covalent linker Biophys. J. 79, 1400-1414
    • (2000) Biophys. J. , vol.79 , pp. 1400-1414
    • Wagner, M.L.1    Tamm, L.K.2
  • 15
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • Tanaka, M. and Sackmann, E. (2005) Polymer-supported membranes as models of the cell surface Nature 437, 656-663
    • (2005) Nature , vol.437 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 17
    • 71549144739 scopus 로고    scopus 로고
    • Purification of membrane proteins
    • Lin, S. H. and Guidotti, G. (2009) Purification of membrane proteins Methods Enzymol. 463, 619-629
    • (2009) Methods Enzymol. , vol.463 , pp. 619-629
    • Lin, S.H.1    Guidotti, G.2
  • 18
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids, and detergents: Not just a soap opera
    • Seddon, A. M., Curnow, P., and Booth, P. J. (2004) Membrane proteins, lipids, and detergents: Not just a soap opera Biochim. Biophys. Acta 1666, 105-117
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 20
    • 0029618097 scopus 로고
    • Differential recognition of the type i interferon receptor by interferons τ and α is responsible for their disparate cytotoxicities
    • Subramaniam, P. S., Khan, S. A., Pontzer, C. H., and Johnson, H. M. (1995) Differential recognition of the type I interferon receptor by interferons τ and α is responsible for their disparate cytotoxicities Proc. Natl. Acad. Sci. U.S.A. 92, 12270-12274
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 12270-12274
    • Subramaniam, P.S.1    Khan, S.A.2    Pontzer, C.H.3    Johnson, H.M.4
  • 21
    • 33644522358 scopus 로고    scopus 로고
    • Inquiring into the differential action of interferons (IFNs): An IFN-α2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-β
    • Jaitin, D. A., Roisman, L. C., Jaks, E., Gavutis, M., Piehler, J., Van der Heyden, J., Uze, G., and Schreiber, G. (2006) Inquiring into the differential action of interferons (IFNs): An IFN-α2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-β Mol. Cell. Biol. 26, 1888-1897
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1888-1897
    • Jaitin, D.A.1    Roisman, L.C.2    Jaks, E.3    Gavutis, M.4    Piehler, J.5    Van Der Heyden, J.6    Uze, G.7    Schreiber, G.8
  • 22
    • 33846345778 scopus 로고    scopus 로고
    • Differential receptor subunit affinities of type i interferons govern differential signal activation
    • Jaks, E., Gavutis, M., Uzé, G., Martal, J., and Piehler, J. (2007) Differential receptor subunit affinities of type I interferons govern differential signal activation J. Mol. Biol. 366, 525-539
    • (2007) J. Mol. Biol. , vol.366 , pp. 525-539
    • Jaks, E.1    Gavutis, M.2    Uzé, G.3    Martal, J.4    Piehler, J.5
  • 23
    • 84867411811 scopus 로고    scopus 로고
    • Structural and dynamic determinants of type i interferon receptor assembly and their functional interpretation
    • Piehler, J., Thomas, C., Christopher Garcia, K., and Schreiber, G. (2012) Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation Immunol Rev. 250, 317-334
    • (2012) Immunol Rev. , vol.250 , pp. 317-334
    • Piehler, J.1    Thomas, C.2    Christopher Garcia, K.3    Schreiber, G.4
  • 24
    • 34249687020 scopus 로고    scopus 로고
    • An interferon α2 mutant optimized by phage display for IFNAR1 binding confers specifically enhanced antitumor activities
    • Kalie, E., Jaitin, D. A., Abramovich, R., and Schreiber, G. (2007) An interferon α2 mutant optimized by phage display for IFNAR1 binding confers specifically enhanced antitumor activities J. Biol. Chem. 282, 11602-11611
    • (2007) J. Biol. Chem. , vol.282 , pp. 11602-11611
    • Kalie, E.1    Jaitin, D.A.2    Abramovich, R.3    Schreiber, G.4
  • 25
    • 0032032913 scopus 로고    scopus 로고
    • Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes
    • Degrip, W. J., Vanoostrum, J., and Bovee-Geurts, P. H. (1998) Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes Biochem. J. 330 (Pt 2) 667-674
    • (1998) Biochem. J. , vol.330 , Issue.PART 2 , pp. 667-674
    • Degrip, W.J.1    Vanoostrum, J.2    Bovee-Geurts, P.H.3
  • 26
    • 80052314755 scopus 로고    scopus 로고
    • Reconstitution of membrane proteins into polymer-supported membranes for probing diffusion and interactions by single molecule techniques
    • Roder, F., Waichman, S., Paterok, D., Schubert, R., Richter, C., Liedberg, B., and Piehler, J. (2011) Reconstitution of membrane proteins into polymer-supported membranes for probing diffusion and interactions by single molecule techniques Anal. Chem. 83, 6792-6799
    • (2011) Anal. Chem. , vol.83 , pp. 6792-6799
    • Roder, F.1    Waichman, S.2    Paterok, D.3    Schubert, R.4    Richter, C.5    Liedberg, B.6    Piehler, J.7
  • 27
    • 84874039926 scopus 로고    scopus 로고
    • Diffusion and interaction dynamics of individual membrane protein complexes confined in micropatterned polymer-supported membranes
    • Waichman, S., Roder, F., Richter, C. P., Birkholz, O., and Piehler, J. (2013) Diffusion and interaction dynamics of individual membrane protein complexes confined in micropatterned polymer-supported membranes Small 9, 570-577
    • (2013) Small , vol.9 , pp. 570-577
    • Waichman, S.1    Roder, F.2    Richter, C.P.3    Birkholz, O.4    Piehler, J.5
  • 28
    • 0029052176 scopus 로고
    • Ligand-induced association of the type i interferon receptor components
    • Cohen, B., Novick, D., Barak, S., and Rubinstein, M. (1995) Ligand-induced association of the type I interferon receptor components Mol. Cell. Biol. 15, 4208-4214
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4208-4214
    • Cohen, B.1    Novick, D.2    Barak, S.3    Rubinstein, M.4
  • 29
    • 77958138174 scopus 로고    scopus 로고
    • Measuring colocalization by dual color single molecule imaging: Thresholds, error rates, and sensitivity
    • (Iglic, A. Ed.), Academic Press, Oxford.
    • Ruprecht, V., Weghuber, J., Wieser, S., and Schütz, G. J. (2010) Measuring colocalization by dual color single molecule imaging: Thresholds, error rates, and sensitivity. In Advances in Planar Lipid Bilayers and Liposomes (Iglic, A., Ed.), pp 21-40, Academic Press, Oxford.
    • (2010) Advances in Planar Lipid Bilayers and Liposomes , pp. 21-40
    • Ruprecht, V.1    Weghuber, J.2    Wieser, S.3    Schütz, G.J.4
  • 30
    • 0035836645 scopus 로고    scopus 로고
    • Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain
    • Constantinescu, S. N., Keren, T., Socolovsky, M., Nam, H., Henis, Y. I., and Lodish, H. F. (2001) Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain Proc. Natl. Acad. Sci. U.S.A. 98, 4379-4384
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4379-4384
    • Constantinescu, S.N.1    Keren, T.2    Socolovsky, M.3    Nam, H.4    Henis, Y.I.5    Lodish, H.F.6
  • 32
    • 31144451979 scopus 로고    scopus 로고
    • Preassembly and ligand-induced restructuring of the chains of the IFN-γ receptor complex: The roles of Jak kinases, Stat1, and the receptor chains
    • Krause, C. D., Lavnikova, N., Xie, J., Mei, E., Mirochnitchenko, O. V., Jia, Y., Hochstrasser, R. M., and Pestka, S. (2006) Preassembly and ligand-induced restructuring of the chains of the IFN-γ receptor complex: The roles of Jak kinases, Stat1, and the receptor chains Cell Res. 16, 55-69
    • (2006) Cell Res. , vol.16 , pp. 55-69
    • Krause, C.D.1    Lavnikova, N.2    Xie, J.3    Mei, E.4    Mirochnitchenko, O.V.5    Jia, Y.6    Hochstrasser, R.M.7    Pestka, S.8
  • 34
    • 84883559027 scopus 로고    scopus 로고
    • Ligand-independent interaction of the type i interferon receptor complex is necessary to observe its biological activity
    • Krause, C. D., Digioia, G., Izotova, L. S., Xie, J., Kim, Y., Schwartz, B. J., Mirochnitchenko, O. V., and Pestka, S. (2013) Ligand-independent interaction of the type I interferon receptor complex is necessary to observe its biological activity Cytokine 64, 286-297
    • (2013) Cytokine , vol.64 , pp. 286-297
    • Krause, C.D.1    Digioia, G.2    Izotova, L.S.3    Xie, J.4    Kim, Y.5    Schwartz, B.J.6    Mirochnitchenko, O.V.7    Pestka, S.8
  • 35
    • 0033117570 scopus 로고    scopus 로고
    • Small molecule cytokine mimetics
    • Whitty, A. and Borysenko, C. W. (1999) Small molecule cytokine mimetics Chem. Biol. 6, R107-118
    • (1999) Chem. Biol. , vol.6 , pp. 107-118
    • Whitty, A.1    Borysenko, C.W.2
  • 36
    • 4143062575 scopus 로고    scopus 로고
    • Ligand-induced assembling of the type i interferon receptor on supported lipid bilayers
    • Lamken, P., Lata, S., Gavutis, M., and Piehler, J. (2004) Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers J. Mol. Biol. 341, 303-318
    • (2004) J. Mol. Biol. , vol.341 , pp. 303-318
    • Lamken, P.1    Lata, S.2    Gavutis, M.3    Piehler, J.4
  • 37
    • 25144452720 scopus 로고    scopus 로고
    • Mutational analysis of the IFNAR1 binding site on IFNα2 reveals the architecture of a weak ligand-receptor binding-site
    • Roisman, L. C., Jaitin, D., Baker, D. P., and Schreiber, G. (2005) Mutational analysis of the IFNAR1 binding site on IFNα2 reveals the architecture of a weak ligand-receptor binding-site J. Mol. Biol. 353, 271-281
    • (2005) J. Mol. Biol. , vol.353 , pp. 271-281
    • Roisman, L.C.1    Jaitin, D.2    Baker, D.P.3    Schreiber, G.4
  • 38
    • 78751524974 scopus 로고    scopus 로고
    • Maleimide photolithography for single-molecule protein-protein interaction analysis in micropatterns
    • Waichman, S., You, C., Beutel, O., Bhagawati, M., and Piehler, J. (2011) Maleimide photolithography for single-molecule protein-protein interaction analysis in micropatterns Anal. Chem. 83, 501-508
    • (2011) Anal. Chem. , vol.83 , pp. 501-508
    • Waichman, S.1    You, C.2    Beutel, O.3    Bhagawati, M.4    Piehler, J.5
  • 39
    • 0033612226 scopus 로고    scopus 로고
    • Biophysical analysis of the interaction of human ifnar2 expressed in E. Coli with IFN α2
    • Piehler, J. and Schreiber, G. (1999) Biophysical analysis of the interaction of human ifnar2 expressed in E. coli with IFN α2 J. Mol. Biol. 289, 57-67
    • (1999) J. Mol. Biol. , vol.289 , pp. 57-67
    • Piehler, J.1    Schreiber, G.2
  • 40
    • 84881272936 scopus 로고    scopus 로고
    • Kinetic analysis of cytokine-mediated receptor assembly using engineered FC heterodimers
    • Deshpande, A., Putcha, B. D., Kuruganti, S., and Walter, M. R. (2013) Kinetic analysis of cytokine-mediated receptor assembly using engineered FC heterodimers Protein Sci. 22, 1100-1108
    • (2013) Protein Sci. , vol.22 , pp. 1100-1108
    • Deshpande, A.1    Putcha, B.D.2    Kuruganti, S.3    Walter, M.R.4
  • 41
    • 20444452736 scopus 로고    scopus 로고
    • Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection
    • Gavutis, M., Lata, S., Lamken, P., Müller, P., and Piehler, J. (2005) Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection Biophys. J. 88, 4289-4302
    • (2005) Biophys. J. , vol.88 , pp. 4289-4302
    • Gavutis, M.1    Lata, S.2    Lamken, P.3    Müller, P.4    Piehler, J.5
  • 42
    • 33646147372 scopus 로고    scopus 로고
    • Determination of the 2-dimensional interaction rate constants of a cytokine receptor complex
    • Gavutis, M., Jaks, E., Lamken, P., and Piehler, J. (2006) Determination of the 2-dimensional interaction rate constants of a cytokine receptor complex Biophys. J. 90, 3345-3355
    • (2006) Biophys. J. , vol.90 , pp. 3345-3355
    • Gavutis, M.1    Jaks, E.2    Lamken, P.3    Piehler, J.4
  • 43
    • 78650708712 scopus 로고    scopus 로고
    • Single particle tracking reveals corralling of a transmembrane protein in a double-cushioned lipid bilayer assembly
    • Poudel, K. R., Keller, D. J., and Brozik, J. A. (2011) Single particle tracking reveals corralling of a transmembrane protein in a double-cushioned lipid bilayer assembly Langmuir 27, 320-327
    • (2011) Langmuir , vol.27 , pp. 320-327
    • Poudel, K.R.1    Keller, D.J.2    Brozik, J.A.3
  • 46
    • 33846786770 scopus 로고    scopus 로고
    • Domain registration in raft-mimicking lipid mixtures studied using polymer-tethered lipid bilayers
    • Garg, S., Ruhe, J., Ludtke, K., Jordan, R., and Naumann, C. A. (2007) Domain registration in raft-mimicking lipid mixtures studied using polymer-tethered lipid bilayers Biophys. J. 92, 1263-1270
    • (2007) Biophys. J. , vol.92 , pp. 1263-1270
    • Garg, S.1    Ruhe, J.2    Ludtke, K.3    Jordan, R.4    Naumann, C.A.5
  • 47
    • 84873844278 scopus 로고    scopus 로고
    • Spatial organization of lipid phases in micropatterned polymer-supported membranes
    • Roder, F., Birkholz, O., Beutel, O., Paterok, D., and Piehler, J. (2013) Spatial organization of lipid phases in micropatterned polymer-supported membranes J. Am. Chem. Soc. 135, 1189-1192
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1189-1192
    • Roder, F.1    Birkholz, O.2    Beutel, O.3    Paterok, D.4    Piehler, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.