메뉴 건너뛰기




Volumn 5, Issue 12, 2008, Pages 1053-1060

Micropatterning for quantitative analysis of protein-protein interactions in living cells

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIBODY; CYAN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; PROTEIN KINASE LCK; YELLOW FLUORESCENT PROTEIN; ZINC;

EID: 57049187658     PISSN: 15487091     EISSN: 15491676     Source Type: Journal    
DOI: 10.1038/nmeth.1268     Document Type: Article
Times cited : (92)

References (30)
  • 1
    • 13444278821 scopus 로고    scopus 로고
    • Reconstruction of cellular signalling networks and analysis of their properties
    • Papin, J.A., Hunter, T., Palsson B.O. & Subramaniam, S. Reconstruction of cellular signalling networks and analysis of their properties. Nat. Rev. Mol. Cell Biol. 6, 99-111 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 99-111
    • Papin, J.A.1    Hunter, T.2    Palsson, B.O.3    Subramaniam, S.4
  • 2
    • 20144372620 scopus 로고    scopus 로고
    • High-throughput mapping of a dynamic signaling network in mammalian cells
    • Barrios-Rodites, M. et al. High-throughput mapping of a dynamic signaling network in mammalian cells. Science 307, 1621-1625 (2005).
    • (2005) Science , vol.307 , pp. 1621-1625
    • Barrios-Rodites, M.1
  • 3
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig, O. et al. The tandem affinity purification (TAP) method: A general procedure of protein complex purification. Methods 24 218-229 (2001).
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1
  • 4
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. & Song, O. A novel genetic system to detect protein-protein interactions. Nature 340, 245-246 (1989).
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 5
    • 0032497564 scopus 로고    scopus 로고
    • The ras recruitment system, a novel approach to the study of protein-protein interactions
    • Broder, Y.C., Katz, S. & Aronheim, A. The ras recruitment system, a novel approach to the study of protein-protein interactions. Curr. Biol. 8, 1121-1124 (1998).
    • (1998) Curr. Biol , vol.8 , pp. 1121-1124
    • Broder, Y.C.1    Katz, S.2    Aronheim, A.3
  • 6
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar, I., Korostensky, C., Johnsson, N. & te Heesen, S. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc. Natl. Acad. Sci. USA 95, 5187-5192 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    te Heesen, S.4
  • 7
    • 24144454858 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with GFP-fragment reassembly
    • Wilson, C.G., Magliery, T.J. & Regan, L. Detecting protein-protein interactions with GFP-fragment reassembly. Nat. Methods 1, 255-262 (2004).
    • (2004) Nat. Methods , vol.1 , pp. 255-262
    • Wilson, C.G.1    Magliery, T.J.2    Regan, L.3
  • 8
    • 0036849482 scopus 로고    scopus 로고
    • Analysis of membrane protein interactions using yeast-based technologies
    • Stagljar, I. & Fields, S. Analysis of membrane protein interactions using yeast-based technologies. Trends Biochem. Sci. 27, 559-563 (2002).
    • (2002) Trends Biochem. Sci , vol.27 , pp. 559-563
    • Stagljar, I.1    Fields, S.2
  • 9
    • 44449096254 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: Application to GPCR oligomerization
    • Maurel, D. et al. Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: Application to GPCR oligomerization. Nat. Methods 5, 561-567 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 561-567
    • Maurel, D.1
  • 10
    • 28544448884 scopus 로고    scopus 로고
    • Photoconversion of YFP into a CFP-Like species during acceptor photobleaching FRET experiments
    • Valentin, G. et al. Photoconversion of YFP into a CFP-Like species during acceptor photobleaching FRET experiments. Nat. Methods 2 801 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 801
    • Valentin, G.1
  • 11
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P. & Simons, K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141, 929-942 (1998).
    • (1998) J. Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 12
    • 33845219419 scopus 로고    scopus 로고
    • Some G protein heterotrimers physically dissociate in living cells
    • Digby, G.J., Lober, R.M., Sethi, P.R. & Lambert, N.A. Some G protein heterotrimers physically dissociate in living cells. Proc. Natl. Acad Sci. USA 103, 17789-17794 (2006).
    • (2006) Proc. Natl. Acad Sci. USA , vol.103 , pp. 17789-17794
    • Digby, G.J.1    Lober, R.M.2    Sethi, P.R.3    Lambert, N.A.4
  • 13
    • 34447508103 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals heterogeneous dynamics of Lipid raft components upon TCR engagement
    • Drbal, K. et al. Single-molecule microscopy reveals heterogeneous dynamics of Lipid raft components upon TCR engagement. Int. Immunol. 19, 675-684 (2007).
    • (2007) Int. Immunol , vol.19 , pp. 675-684
    • Drbal, K.1
  • 14
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and G\{aLpha, for temporary cluster immobilization and Lyn activation: Single-molecule tracking study 1
    • Suzuki, K.G. et al. GPI-anchored receptor clusters transiently recruit Lyn and G\{aLpha\} for temporary cluster immobilization and Lyn activation: Single-molecule tracking study 1. J. Cell Biol. 177 717-730 (2007).
    • (2007) J. Cell Biol , vol.177 , pp. 717-730
    • Suzuki, K.G.1
  • 15
    • 0344519526 scopus 로고    scopus 로고
    • Mast cell activation on patterned lipid bilayers of subcellular dimensions
    • Orth, R.N. et al. Mast cell activation on patterned lipid bilayers of subcellular dimensions. Langmuir 19, 1599-1605 (2003).
    • (2003) Langmuir , vol.19 , pp. 1599-1605
    • Orth, R.N.1
  • 16
    • 4644364556 scopus 로고    scopus 로고
    • Visualization of plasma membrane compartmentalization with patterned Lipid biLayers
    • Wu, M., Holowka, D., Craighead, H.G. & Baird, B. Visualization of plasma membrane compartmentalization with patterned Lipid biLayers. Proc. Natl. Acad. Sci. USA 101, 13798-13803 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13798-13803
    • Wu, M.1    Holowka, D.2    Craighead, H.G.3    Baird, B.4
  • 17
    • 27944442353 scopus 로고    scopus 로고
    • Altered TCR signaling from geometrically repatterned immunological synapses
    • Mossman, K.D., Campi, G., Groves, J.T. & Dustin, M.L. Altered TCR signaling from geometrically repatterned immunological synapses. Science 310, 1191-1193 (2005).
    • (2005) Science , vol.310 , pp. 1191-1193
    • Mossman, K.D.1    Campi, G.2    Groves, J.T.3    Dustin, M.L.4
  • 18
    • 33644932947 scopus 로고    scopus 로고
    • Lateral spacing of integrin Ligands influences cell spreading and focal adhesion assembly
    • Cavalcanti-Adam, E.A. et al. Lateral spacing of integrin Ligands influences cell spreading and focal adhesion assembly. Eur. J. Cell Biol. 85, 219-224 (2006).
    • (2006) Eur. J. Cell Biol , vol.85 , pp. 219-224
    • Cavalcanti-Adam, E.A.1
  • 19
    • 0025303702 scopus 로고
    • Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56Lck tyrosine protein kinase
    • Shaw, A.S. et al. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56Lck tyrosine protein kinase. Mol. Cell. Biol. 10, 1853-1862 (1990).
    • (1990) Mol. Cell. Biol , vol.10 , pp. 1853-1862
    • Shaw, A.S.1
  • 20
    • 0025237554 scopus 로고
    • Interaction of the unique N-terminal region of tyrosine kinase p56Lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs
    • Turner, J.M. et al. Interaction of the unique N-terminal region of tyrosine kinase p56Lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs. Cell 60, 755-765 (1990).
    • (1990) Cell , vol.60 , pp. 755-765
    • Turner, J.M.1
  • 21
    • 4444298148 scopus 로고    scopus 로고
    • CD4 enhances T cell sensitivity to antigen by coordinating Lck accumulation at the immunological synapse
    • Li, O.J. et al. CD4 enhances T cell sensitivity to antigen by coordinating Lck accumulation at the immunological synapse. Nat. Immunol. 5, 791-799 (2004).
    • (2004) Nat. Immunol , vol.5 , pp. 791-799
    • Li, O.J.1
  • 22
    • 1642282774 scopus 로고    scopus 로고
    • Enrichment of Lck in lipid rafts regulates colocalized fyn activation and the initiation of proximal signals through TCR alpha beta
    • FiLipp, D. et al. Enrichment of Lck in lipid rafts regulates colocalized fyn activation and the initiation of proximal signals through TCR alpha beta. J. Immunol. 172, 4266-4274 (2004).
    • (2004) J. Immunol , vol.172 , pp. 4266-4274
    • FiLipp, D.1
  • 23
    • 0141654999 scopus 로고    scopus 로고
    • A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8
    • Kim, P.W. et al. A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8. Science 301, 1725-1728 (2003).
    • (2003) Science , vol.301 , pp. 1725-1728
    • Kim, P.W.1
  • 24
    • 2442494090 scopus 로고    scopus 로고
    • Balamuth, F., Brogdon, J.L. & Bottomly, K. CD4 raft association and signaling regulate molecular clustering at the immunological synapse site. J. Immunol. 172, 5887-5892 (2004).
    • Balamuth, F., Brogdon, J.L. & Bottomly, K. CD4 raft association and signaling regulate molecular clustering at the immunological synapse site. J. Immunol. 172, 5887-5892 (2004).
  • 25
    • 0037438349 scopus 로고    scopus 로고
    • Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling
    • Fragoso, R. et al. Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling. J. Immunol. 170, 913-921 (2003).
    • (2003) J. Immunol , vol.170 , pp. 913-921
    • Fragoso, R.1
  • 26
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanova, I. et al. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 254, 1016-1019 (1991).
    • (1991) Science , vol.254 , pp. 1016-1019
    • Stefanova, I.1
  • 27
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • Kabouridis, P.S., Magee, A.I. & Ley, S.C. S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO J. 16, 4983-4998 (1997).
    • (1997) EMBO J , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 28
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., Violin, J.D., Newton, A.C. & Tsien, R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916 (2002).
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 29
    • 29744438833 scopus 로고    scopus 로고
    • Thinning out clusters white conserving stoichiometry of Labeling
    • Moertelmaier, M. et al. Thinning out clusters white conserving stoichiometry of Labeling. Appl. Phys. Lett. 87, 263903 (2005).
    • (2005) Appl. Phys. Lett , vol.87 , pp. 263903
    • Moertelmaier, M.1
  • 30
    • 34247843089 scopus 로고    scopus 로고
    • Subunit counting in membrane-bound proteins
    • Ulbrich, M.H. & Isacoff, E.Y. Subunit counting in membrane-bound proteins. Nat. Methods 4, 319-321 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 319-321
    • Ulbrich, M.H.1    Isacoff, E.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.