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Volumn 2, Issue 1, 2011, Pages

Detection of focal adhesion kinase activation at membrane microdomains by fluorescence resonance energy transfer

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; FOCAL ADHESION KINASE; PLATELET DERIVED GROWTH FACTOR; STEROID RECEPTOR COACTIVATOR 1;

EID: 79960903742     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1414     Document Type: Article
Times cited : (108)

References (38)
  • 1
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • DOI 10.1038/nrm1549
    • Mitra, S. K., Hanson, D. A. & Schlaepfer, D. D. Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6, 56-68 (2005). (Pubitemid 40064899)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 2
    • 35348847063 scopus 로고    scopus 로고
    • Cell mechanics: Integrating cell responses to mechanical stimuli
    • DOI 10.1146/annurev.bioeng.9.060906.151927
    • Janmey, P. A. & McCulloch, C. A. Cell mechanics: integrating cell responses to mechanical stimuli. Annu. Rev. Biomed. Eng. 9, 1-34 (2007). (Pubitemid 350252899)
    • (2007) Annual Review of Biomedical Engineering , vol.9 , pp. 1-34
    • Janmey, P.A.1    McCulloch, C.A.2
  • 4
    • 0033772308 scopus 로고    scopus 로고
    • FAK integrates growth-factor and integrin signals to promote cell migration
    • Sieg, D. J. et al. FAK integrates growth-factor and integrin signals to promote cell migration. Nat. Cell Biol. 2, 249-256 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 249-256
    • Sieg, D.J.1
  • 5
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • Simons, K. & Gerl, M. J. Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 11, 688-699.
    • Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 6
    • 33750130964 scopus 로고    scopus 로고
    • Lipid rafts: Now you see them, now you don't
    • DOI 10.1038/ni1405, PII NI1405
    • Shaw, A. S. Lipid rafts: now you seethem, now you don't. Nat. Immunol. 7, 1139-1142 (2006). (Pubitemid 44594308)
    • (2006) Nature Immunology , vol.7 , Issue.11 , pp. 1139-1142
    • Shaw, A.S.1
  • 7
    • 58849160148 scopus 로고    scopus 로고
    • Visualization of Src activity at different compartments of the plasma membrane by FRET imaging
    • Seong, J. et al. Visualization of Src activity at different compartments of the plasma membrane by FRET imaging. Chem. Biol. 16, 48-57 (2009).
    • (2009) Chem. Biol. , vol.16 , pp. 48-57
    • Seong, J.1
  • 8
    • 57349145336 scopus 로고    scopus 로고
    • Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains
    • Gao, X. & Zhang, J. Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains. Mol. Biol. Cell 19, 4366-4373 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4366-4373
    • Gao, X.1    Zhang, J.2
  • 9
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • DOI 10.1016/j.tibs.2005.06.004, PII S0968000405001830
    • Lichtenberg, D., Goni, F. M. & Heerklotz, H. Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem. Sci. 30, 430-436 (2005). (Pubitemid 41033238)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.8 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 10
    • 32944458874 scopus 로고    scopus 로고
    • Fluorescence (Förster) resonance energy transfer imaging of oncogene activity in living cells
    • DOI 10.1111/j.1349-7006.2006.00141.x
    • Kiyokawa, E., Hara, S., Nakamura, T. & Matsuda, M. Fluorescence (Forster) resonance energy transfer imaging of oncogene activity in living cells. Cancer Sci. 97, 8-15 (2006). (Pubitemid 43257021)
    • (2006) Cancer Science , vol.97 , Issue.1 , pp. 8-15
    • Kiyokawa, E.1    Hara, S.2    Nakamura, T.3    Matsuda, M.4
  • 11
    • 37549060016 scopus 로고    scopus 로고
    • Spatial and temporal regulation of focal adhesion kinase activity in living cells
    • Cai, X. et al. Spatial and temporal regulation of focal adhesion kinase activity in living cells. Mol. Cell. Biol. 28, 201-214 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 201-214
    • Cai, X.1
  • 12
    • 66149139873 scopus 로고    scopus 로고
    • Dynamic conformational changes in the FERM domain of FAK are involved in focal-adhesion behavior during cell spreading and motility
    • Papusheva, E. et al. Dynamic conformational changes in the FERM domain of FAK are involved in focal-adhesion behavior during cell spreading and motility. J. Cell Sci. 122, 656-666 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 656-666
    • Papusheva, E.1
  • 13
    • 34250026140 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of focal adhesion kinase
    • DOI 10.1016/j.cell.2007.05.041, PII S0092867407006800
    • Lietha, D. et al. Structural basis for the autoinhibition of focal adhesion kinase. Cell 129, 1177-1187 (2007). (Pubitemid 46891044)
    • (2007) Cell , vol.129 , Issue.6 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.J.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 14
    • 55749093427 scopus 로고    scopus 로고
    • Determination of hierarchical relationship of Src and Rac at subcellular locations with FRET biosensors
    • Ouyang, M., Sun, J., Chien, S. & Wang, Y. Determination of hierarchical relationship of Src and Rac at subcellular locations with FRET biosensors. Proc. Natl Acad. Sci. USA 105, 14353-14358 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 14353-14358
    • Ouyang, M.1    Sun, J.2    Chien, S.3    Wang, Y.4
  • 15
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • DOI 10.1126/science.1068539
    • 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). (Pubitemid 34464897)
    • (2002) Science , vol.296 , Issue.5569 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 17
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • DOI 10.1016/j.ceb.2006.08.011, PII S0955067406001220
    • Mitra, S. K. & Schlaepfer, D. D. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18, 516-523 (2006). (Pubitemid 44332916)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.5 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 18
    • 0242495710 scopus 로고    scopus 로고
    • Regulation of Focal Adhesion Kinase by Its Amino-Terminal Domain through an Autoinhibitory Interaction
    • DOI 10.1128/MCB.23.22.8030-8041.2003
    • Cooper, L. A., Shen, T. L. & Guan, J. L. Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction. Mol. Cell. Biol. 23, 8030-8041 (2003). (Pubitemid 37377496)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.22 , pp. 8030-8041
    • Cooper, L.A.1    Shen, T.-L.2    Guan, J.-L.3
  • 19
    • 67650097014 scopus 로고    scopus 로고
    • Cholesterol depletion induces anoikis-like apoptosis via FAK down-regulation and caveolae internalization
    • Park, E. K. et al. Cholesterol depletion induces anoikis-like apoptosis via FAK down-regulation and caveolae internalization. J. Pathol. 218, 337-349 (2009).
    • (2009) J. Pathol. , vol.218 , pp. 337-349
    • Park, E.K.1
  • 20
    • 0842331443 scopus 로고    scopus 로고
    • Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling
    • DOI 10.1126/science.1091325
    • Palazzo, A. F., Eng, C. H., Schlaepfer, D. D., Marcantonio, E. E. & Gundersen, G. G. Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling. Science 303, 836-839 (2004). (Pubitemid 38174661)
    • (2004) Science , vol.303 , Issue.5659 , pp. 836-839
    • Palazzo, A.F.1    Eng, C.H.2    Schlaepfer, D.D.3    Marcantonio, E.E.4    Gundersen, G.G.5
  • 21
    • 0027938974 scopus 로고
    • Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase
    • Chen, H. C. & Guan, J. L. Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc. Natl Acad. Sci. USA 91, 10148-10152 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10148-10152
    • Chen, H.C.1    Guan, J.L.2
  • 22
    • 0037177352 scopus 로고    scopus 로고
    • Visualizing cellular phosphoinositide pools with GFP-fused protein-modules
    • Balla, T. & Varnai, P. Visualizing cellular phosphoinositide pools with GFP-fused protein-modules. Sci. STKE 2002, PL3 (2002).
    • (2002) Sci. STKE , vol.2002
    • Balla, T.1    Varnai, P.2
  • 23
    • 0033572662 scopus 로고    scopus 로고
    • The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo
    • DOI 10.1042/0264-6021:3440929
    • Gray, A., Van Der Kaay, J. & Downes, C. P. The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo. Biochem. J. 344, 929-936 (1999). (Pubitemid 30032544)
    • (1999) Biochemical Journal , vol.344 , Issue.3 , pp. 929-936
    • Gray, A.1    Van Der Kaay, J.2    Downes, C.P.3
  • 28
    • 65349127021 scopus 로고    scopus 로고
    • FAK alters invadopodia and focal adhesion composition and dynamics to regulate breast cancer invasion
    • Chan, K. T., Cortesio, C. L. & Huttenlocher, A. FAK alters invadopodia and focal adhesion composition and dynamics to regulate breast cancer invasion. J. Cell Biol. 185, 357-370 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 357-370
    • Chan, K.T.1    Cortesio, C.L.2    Huttenlocher, A.3
  • 30
  • 31
    • 55049119303 scopus 로고    scopus 로고
    • Early adhesion induces interaction of FAK and Fyn in lipid domains and activates raft-dependent Akt signaling in SW480 colon cancer cells
    • Baillat, G., Siret, C., Delamarre, E. & Luis, J. Early adhesion induces interaction of FAK and Fyn in lipid domains and activates raft-dependent Akt signaling in SW480 colon cancer cells. Biochim. Biophys. Acta 1783, 2323-2331 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2323-2331
    • Baillat, G.1    Siret, C.2    Delamarre, E.3    Luis, J.4
  • 32
    • 0037152341 scopus 로고    scopus 로고
    • Direct transmembrane clustering and cytoplasmic dimerization of focal adhesion kinase initiates its tyrosine phosphorylation
    • Katz, B. Z. et al. Direct transmembrane clustering and cytoplasmic dimerization of focal adhesion kinase initiates its tyrosine phosphorylation. Biochim. Biophys. Acta 1592, 141-152 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 141-152
    • Katz, B.Z.1
  • 33
    • 0344507516 scopus 로고    scopus 로고
    • A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling
    • DOI 10.1083/jcb.144.6.1285
    • Wei, Y., Yang, X., Liu, Q., Wilkins, J. A. & Chapman, H. A. A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling. J. Cell Biol. 144, 1285-1294 (1999). (Pubitemid 29157305)
    • (1999) Journal of Cell Biology , vol.144 , Issue.6 , pp. 1285-1294
    • Ying, W.1    Yang, X.2    Qiumei, L.3    Wilkins, J.A.4    Chapman, H.A.5
  • 34
    • 33748099759 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates membrane order
    • DOI 10.1083/jcb.200603034
    • Gaus, K., Le Lay, S., Balasubramanian, N. & Schwartz, M. A. Integrin-mediated adhesion regulates membrane order. J. Cell Biol. 174, 725-734 (2006). (Pubitemid 44306728)
    • (2006) Journal of Cell Biology , vol.174 , Issue.5 , pp. 725-734
    • Gaus, K.1    Le Lay, S.2    Balasubramanian, N.3    Schwartz, M.A.4
  • 35
    • 0036205320 scopus 로고    scopus 로고
    • Src catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • DOI 10.1128/MCB.22.8.2427-2440.2002
    • Cary, L. A., Klinghoffer, R. A., Sachsenmaier, C. & Cooper, J. A. SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading. Mol. Cell. Biol. 22, 2427-2440 (2002). (Pubitemid 34262966)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.8 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 36
    • 0035947577 scopus 로고    scopus 로고
    • Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397
    • Salazar, E. P. & Rozengurt, E. Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397. J. Biol. Chem. 276, 17788-17795 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 17788-17795
    • Salazar, E.P.1    Rozengurt, E.2
  • 37
    • 0025172811 scopus 로고
    • Association between the PDGF receptor and members of the src family of tyrosine kinases
    • Kypta, R. M., Goldberg, Y., Ulug, E. T. & Courtneidge, S. A. Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell 62, 481-492 (1990).
    • (1990) Cell , vol.62 , pp. 481-492
    • Kypta, R.M.1    Goldberg, Y.2    Ulug, E.T.3    Courtneidge, S.A.4


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