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Volumn 51, Issue 8, 2012, Pages 1638-1647

Assembly of membrane-bound protein complexes: Detection and analysis by single molecule diffusion

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE MEMBRANES; ASSEMBLY REACTIONS; BI-LAYER; BINDING CURVES; BIOLOGY AND MEDICINE; CELL PROCESS; COMPLEX ASSEMBLY; COMPLEX DISSOCIATION; COMPLEX FORMATIONS; CRITICAL SIGNALING PATHWAYS; FUSION PROTEINS; HETERODIMERIC COMPLEXES; HETERODIMERS; MEMBRANE SURFACE; MEMBRANE SYSTEM; MEMBRANE-BOUND; MEMBRANE-BOUND PROTEINS; MOLECULAR UNDERSTANDING; MYOSIN LIGHT CHAIN KINASE; PLECKSTRIN HOMOLOGY DOMAINS; PROTEIN COMPLEXES; SIGNALING PATHWAYS; SINGLE-MOLECULE DIFFUSION; SUPPORTED LIPID BILAYERS;

EID: 84857597124     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201743a     Document Type: Article
Times cited : (30)

References (44)
  • 1
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M. A. and Ferguson, K. M. (2000) Signal-dependent membrane targeting by pleckstrin homology (PH) domains Biochem. J. 350 (Pt. 1) 1-18
    • (2000) Biochem. J. , vol.350 , Issue.PART 1 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 2
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: Complex roles at the cell surface
    • Czech, M. P. (2000) PIP2 and PIP3: complex roles at the cell surface Cell 100, 603-606
    • (2000) Cell , vol.100 , pp. 603-606
    • Czech, M.P.1
  • 3
    • 0035656919 scopus 로고    scopus 로고
    • PIP3, PIP2, and cell movement - Similar messages, different meanings?
    • Insall, R. H. and Weiner, O. D. (2001) PIP3, PIP2, and cell movement - similar messages, different meanings? Dev. Cell 1, 743-747
    • (2001) Dev. Cell , vol.1 , pp. 743-747
    • Insall, R.H.1    Weiner, O.D.2
  • 5
    • 0036308458 scopus 로고    scopus 로고
    • Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils
    • Wang, F., Herzmark, P., Weiner, O. D., Srinivasan, S., Servant, G., and Bourne, H. R. (2002) Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils Nat. Cell Biol. 4, 513-518
    • (2002) Nat. Cell Biol. , vol.4 , pp. 513-518
    • Wang, F.1    Herzmark, P.2    Weiner, O.D.3    Srinivasan, S.4    Servant, G.5    Bourne, H.R.6
  • 6
    • 0038650888 scopus 로고    scopus 로고
    • Dynamics of phosphoinositides in membrane retrieval and insertion
    • Czech, M. P. (2003) Dynamics of phosphoinositides in membrane retrieval and insertion Annu. Rev. Physiol. 65, 791-815
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 791-815
    • Czech, M.P.1
  • 7
    • 1542569606 scopus 로고    scopus 로고
    • Membrane recognition and targeting by lipid-binding domains
    • DiNitto, J. P., Cronin, T. C., and Lambright, D. G. (2003) Membrane recognition and targeting by lipid-binding domains Sci. STKE re16
    • (2003) Sci. STKE , pp. 16
    • Dinitto, J.P.1    Cronin, T.C.2    Lambright, D.G.3
  • 8
    • 11144292734 scopus 로고    scopus 로고
    • GRP1 pleckstrin homology domain: Activation parameters and novel search mechanism for rare target lipid
    • Corbin, J. A., Dirkx, R. A., and Falke, J. J. (2004) GRP1 pleckstrin homology domain: activation parameters and novel search mechanism for rare target lipid Biochemistry 43, 16161-16173
    • (2004) Biochemistry , vol.43 , pp. 16161-16173
    • Corbin, J.A.1    Dirkx, R.A.2    Falke, J.J.3
  • 10
    • 33748462297 scopus 로고    scopus 로고
    • Membrane binding domains
    • Hurley, J. H. (2006) Membrane binding domains Biochim. Biophys. Acta 1761, 805-811
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 805-811
    • Hurley, J.H.1
  • 12
    • 66349096059 scopus 로고    scopus 로고
    • Lipid activation of protein kinases
    • Newton, A. C. (2009) Lipid activation of protein kinases J. Lipid Res. 50, xxxx
    • (2009) J. Lipid Res. , vol.50
    • Newton, A.C.1
  • 14
    • 80054736907 scopus 로고    scopus 로고
    • Structural basis for activation and inhibition of class I phosphoinositide 3-kinases
    • Vadas, O., Burke, J. E., Zhang, X., Berndt, A., and Williams, R. L. (2011) Structural basis for activation and inhibition of class I phosphoinositide 3-kinases Sci. Signaling 4, xxxx
    • (2011) Sci. Signaling , vol.4
    • Vadas, O.1    Burke, J.E.2    Zhang, X.3    Berndt, A.4    Williams, R.L.5
  • 15
    • 67349094328 scopus 로고    scopus 로고
    • 3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase
    • Calleja, V., Laguerre, M., and Larijani, B. (2009) 3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase J. Chem. Biol. 2, 11-25
    • (2009) J. Chem. Biol. , vol.2 , pp. 11-25
    • Calleja, V.1    Laguerre, M.2    Larijani, B.3
  • 18
    • 77958576132 scopus 로고    scopus 로고
    • Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition
    • Wu, W. I., Voegtli, W. C., Sturgis, H. L., Dizon, F. P., Vigers, G. P., and Brandhuber, B. J. (2010) Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition PLoS One 5, e12913
    • (2010) PLoS One , vol.5 , pp. 12913
    • Wu, W.I.1    Voegtli, W.C.2    Sturgis, H.L.3    Dizon, F.P.4    Vigers, G.P.5    Brandhuber, B.J.6
  • 21
    • 79952213088 scopus 로고    scopus 로고
    • How to quantify protein diffusion in the bacterial membrane
    • van den Wildenberg, S. M., Bollen, Y. J., and Peterman, E. J. (2011) How to quantify protein diffusion in the bacterial membrane Biopolymers 95, 312-321
    • (2011) Biopolymers , vol.95 , pp. 312-321
    • Van Den Wildenberg, S.M.1    Bollen, Y.J.2    Peterman, E.J.3
  • 22
    • 58149456901 scopus 로고    scopus 로고
    • Synaptic receptor trafficking: The lateral point of view
    • Jaskolski, F. and Henley, J. M. (2009) Synaptic receptor trafficking: the lateral point of view Neuroscience 158, 19-24
    • (2009) Neuroscience , vol.158 , pp. 19-24
    • Jaskolski, F.1    Henley, J.M.2
  • 23
    • 47349120744 scopus 로고    scopus 로고
    • Double cushions preserve transmembrane protein mobility in supported bilayer systems
    • Diaz, A. J., Albertorio, F., Daniel, S., and Cremer, P. S. (2008) Double cushions preserve transmembrane protein mobility in supported bilayer systems Langmuir 24, 6820-6826
    • (2008) Langmuir , vol.24 , pp. 6820-6826
    • Diaz, A.J.1    Albertorio, F.2    Daniel, S.3    Cremer, P.S.4
  • 24
    • 48749105304 scopus 로고    scopus 로고
    • Abundance and stability of complexes containing inactive G protein-coupled receptors and G proteins
    • Qin, K., Sethi, P. R., and Lambert, N. A. (2008) Abundance and stability of complexes containing inactive G protein-coupled receptors and G proteins FASEB J. 22, 2920-2927
    • (2008) FASEB J. , vol.22 , pp. 2920-2927
    • Qin, K.1    Sethi, P.R.2    Lambert, N.A.3
  • 25
    • 33748969315 scopus 로고    scopus 로고
    • Fluorescence-based methods to image palmitoylated proteins
    • Kenworthy, A. K. (2006) Fluorescence-based methods to image palmitoylated proteins Methods 40, 198-205
    • (2006) Methods , vol.40 , pp. 198-205
    • Kenworthy, A.K.1
  • 26
    • 33746303104 scopus 로고    scopus 로고
    • Methods to measure the lateral diffusion of membrane lipids and proteins
    • Chen, Y., Lagerholm, B. C., Yang, B., and Jacobson, K. (2006) Methods to measure the lateral diffusion of membrane lipids and proteins Methods 39, 147-153
    • (2006) Methods , vol.39 , pp. 147-153
    • Chen, Y.1    Lagerholm, B.C.2    Yang, B.3    Jacobson, K.4
  • 27
    • 0038959242 scopus 로고    scopus 로고
    • Organization and dynamics of the proteolipid complexes formed by annexin v and lipids in planar supported lipid bilayers
    • Cezanne, L., Lopez, A., Loste, F., Parnaud, G., Saurel, O., Demange, P., and Tocanne, J. F. (1999) Organization and dynamics of the proteolipid complexes formed by annexin V and lipids in planar supported lipid bilayers Biochemistry 38, 2779-2786
    • (1999) Biochemistry , vol.38 , pp. 2779-2786
    • Cezanne, L.1    Lopez, A.2    Loste, F.3    Parnaud, G.4    Saurel, O.5    Demange, P.6    Tocanne, J.F.7
  • 28
    • 0023873084 scopus 로고
    • Lateral diffusion and fluorescence microscope studies on a monoclonal antibody specifically bound to supported phospholipid bilayers
    • Tamm, L. K. (1988) Lateral diffusion and fluorescence microscope studies on a monoclonal antibody specifically bound to supported phospholipid bilayers Biochemistry 27, 1450-1457
    • (1988) Biochemistry , vol.27 , pp. 1450-1457
    • Tamm, L.K.1
  • 29
    • 78249261241 scopus 로고    scopus 로고
    • Single molecule diffusion of membrane-bound proteins: Window into lipid contacts and bilayer dynamics
    • Knight, J. D., Lerner, M. G., Marcano-Velazquez, J. G., Pastor, R. W., and Falke, J. J. (2010) Single molecule diffusion of membrane-bound proteins: window into lipid contacts and bilayer dynamics Biophys. J. 99, 2879-2887
    • (2010) Biophys. J. , vol.99 , pp. 2879-2887
    • Knight, J.D.1    Lerner, M.G.2    Marcano-Velazquez, J.G.3    Pastor, R.W.4    Falke, J.J.5
  • 30
    • 0031893953 scopus 로고    scopus 로고
    • Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence
    • Barth, A., Martin, S. R., and Bayley, P. M. (1998) Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence J. Biol. Chem. 273, 2174-2183
    • (1998) J. Biol. Chem. , vol.273 , pp. 2174-2183
    • Barth, A.1    Martin, S.R.2    Bayley, P.M.3
  • 32
    • 58849094579 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of a PH domain: New insights into the membrane docking reaction
    • Knight, J. D. and Falke, J. J. (2009) Single-molecule fluorescence studies of a PH domain: new insights into the membrane docking reaction Biophys. J. 96, 566-582
    • (2009) Biophys. J. , vol.96 , pp. 566-582
    • Knight, J.D.1    Falke, J.J.2
  • 33
    • 23044515069 scopus 로고    scopus 로고
    • Feature point tracking and trajectory analysis for video imaging in cell biology
    • Sbalzarini, I. F. and Koumoutsakos, P. (2005) Feature point tracking and trajectory analysis for video imaging in cell biology J. Struct. Biol. 151, 182-195
    • (2005) J. Struct. Biol. , vol.151 , pp. 182-195
    • Sbalzarini, I.F.1    Koumoutsakos, P.2
  • 34
    • 0039587949 scopus 로고    scopus 로고
    • Single-molecule microscopy on model membranes reveals anomalous diffusion
    • Schutz, G. J., Schindler, H., and Schmidt, T. (1997) Single-molecule microscopy on model membranes reveals anomalous diffusion Biophys. J. 73, 1073-1080
    • (1997) Biophys. J. , vol.73 , pp. 1073-1080
    • Schutz, G.J.1    Schindler, H.2    Schmidt, T.3
  • 35
    • 0033804075 scopus 로고    scopus 로고
    • Tracking single proteins within cells
    • Goulian, M. and Simon, S. M. (2000) Tracking single proteins within cells Biophys. J. 79, 2188-2198
    • (2000) Biophys. J. , vol.79 , pp. 2188-2198
    • Goulian, M.1    Simon, S.M.2
  • 36
    • 0027340011 scopus 로고
    • Ca2+, caldesmon, and myosin light chain kinase exchange with calmodulin
    • Kasturi, R., Vasulka, C., and Johnson, J. D. (1993) Ca2+, caldesmon, and myosin light chain kinase exchange with calmodulin J. Biol. Chem. 268, 7958-7964
    • (1993) J. Biol. Chem. , vol.268 , pp. 7958-7964
    • Kasturi, R.1    Vasulka, C.2    Johnson, J.D.3
  • 37
    • 77954811524 scopus 로고    scopus 로고
    • Recent Applications of Fluorescence Recovery after Photobleaching (FRAP) to Membrane Bio-Macromolecules
    • Rayan, G., Guet, J. E., Taulier, N., Pincet, F., and Urbach, W. (2010) Recent Applications of Fluorescence Recovery after Photobleaching (FRAP) to Membrane Bio-Macromolecules Sensors (Basel) 10, 5927-5948
    • (2010) Sensors (Basel) , vol.10 , pp. 5927-5948
    • Rayan, G.1    Guet, J.E.2    Taulier, N.3    Pincet, F.4    Urbach, W.5
  • 38
    • 0000291826 scopus 로고
    • Rates of diffusion controlled reactions in one, two and three dimensions
    • Hardt, S. L. (1979) Rates of diffusion controlled reactions in one, two and three dimensions Biophys. Chem. 10, 239-243
    • (1979) Biophys. Chem. , vol.10 , pp. 239-243
    • Hardt, S.L.1
  • 39
    • 0037307080 scopus 로고    scopus 로고
    • Protein conformational changes studied by diffusion NMR spectroscopy: Application to helix-loop-helix calcium binding proteins
    • Weljie, A. M., Yamniuk, A. P., Yoshino, H., Izumi, Y., and Vogel, H. J. (2003) Protein conformational changes studied by diffusion NMR spectroscopy: application to helix-loop-helix calcium binding proteins Protein Sci. 12, 228-236
    • (2003) Protein Sci. , vol.12 , pp. 228-236
    • Weljie, A.M.1    Yamniuk, A.P.2    Yoshino, H.3    Izumi, Y.4    Vogel, H.J.5
  • 40
    • 66349132474 scopus 로고    scopus 로고
    • Lipid binding domains: More than simple lipid effectors
    • Stahelin, R. V. (2009) Lipid binding domains: more than simple lipid effectors, J. Lipid Res. 50 Suppl, S299-304.
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Stahelin, R.V.1
  • 42
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T., and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin Nat. Struct. Biol. 2, 758-767
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 44
    • 0001018554 scopus 로고
    • Calcineurin: A calcium- and calmodulin-binding protein of the nervous system
    • Klee, C. B., Crouch, T. H., and Krinks, M. H. (1979) Calcineurin: a calcium- and calmodulin-binding protein of the nervous system Proc. Natl. Acad. Sci. U. S. A. 76, 6270-6273
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 6270-6273
    • Klee, C.B.1    Crouch, T.H.2    Krinks, M.H.3


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