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Volumn 11, Issue 10, 2003, Pages 1207-1217

Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain

Author keywords

[No Author keywords available]

Indexed keywords

PAXILLIN; VINCULIN;

EID: 0141483200     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.08.010     Document Type: Article
Times cited : (88)

References (41)
  • 1
    • 0036118284 scopus 로고    scopus 로고
    • The structural basis of localization and signaling by the focal adhesion targeting domain
    • Arold S.T., Hoellerer M.K., Noble M.E. The structural basis of localization and signaling by the focal adhesion targeting domain. Structure (Camb.). 10:2002;319-327.
    • (2002) Structure (Camb.) , vol.10 , pp. 319-327
    • Arold, S.T.1    Hoellerer, M.K.2    Noble, M.E.3
  • 3
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G., Ruben D.J. Natural Abundance Nitrogen-15 NMR by Enhanced Heteronuclear Spectroscopy. Chem. Phys. Lett. 69:1980;185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 5
    • 0028103275 scopus 로고
    • Collaborative computational project number 4) The CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project Number 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 6
    • 0029048405 scopus 로고
    • Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein
    • Chen J.J., Reid C.E., Band V., Androphy E.J. Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein. Science. 269:1995;529-531.
    • (1995) Science , vol.269 , pp. 529-531
    • Chen, J.J.1    Reid, C.E.2    Band, V.3    Androphy, E.J.4
  • 7
    • 0034490676 scopus 로고    scopus 로고
    • Paxillin binding is not the sole determinant of focal adhesion localization or dominant-negative activity of focal adhesion kinase/focal adhesion kinase-related nonkinase
    • Cooley M.A., Broome J.M., Ohngemach C., Romer L.H., Schaller M.D. Paxillin binding is not the sole determinant of focal adhesion localization or dominant-negative activity of focal adhesion kinase/focal adhesion kinase-related nonkinase. Mol. Biol. Cell. 11:2000;3247-3263.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3247-3263
    • Cooley, M.A.1    Broome, J.M.2    Ohngemach, C.3    Romer, L.H.4    Schaller, M.D.5
  • 8
    • 0034843745 scopus 로고    scopus 로고
    • Easier threading through web-based comparisons and cross-validations
    • Douguet D., Labesse G. Easier threading through web-based comparisons and cross-validations. Bioinformatics. 17:2001;752-753.
    • (2001) Bioinformatics , vol.17 , pp. 752-753
    • Douguet, D.1    Labesse, G.2
  • 9
    • 0025210153 scopus 로고
    • Complete resonance assignment for the polypeptide backbone of interleukin-1-Beta using 3-dimensional heteronuclear Nmr-spectroscopy
    • Driscoll P.C., Clore G.M., Marion D., Wingfield P.T., Gronenborn A.M. Complete Resonance Assignment For the Polypeptide Backbone Of Interleukin-1-Beta Using 3-Dimensional Heteronuclear Nmr-Spectroscopy. Biochemistry. 29:1990;3542-3556.
    • (1990) Biochemistry , vol.29 , pp. 3542-3556
    • Driscoll, P.C.1    Clore, G.M.2    Marion, D.3    Wingfield, P.T.4    Gronenborn, A.M.5
  • 10
    • 0028503463 scopus 로고
    • A heteronuclear correlation experiment for simultaneous determination of N-15 longitudinal decay and chemical-exchange rates of systems in slow equilibrium
    • Farrow N.A., Zhang O.W., Formankay J.D., Kay L.E. A Heteronuclear Correlation Experiment For Simultaneous Determination Of N-15 Longitudinal Decay and Chemical-Exchange Rates Of Systems In Slow Equilibrium. J. Biomol. NMR. 4:1994;727-734.
    • (1994) J. Biomol. NMR , vol.4 , pp. 727-734
    • Farrow, N.A.1    Zhang, O.W.2    Formankay, J.D.3    Kay, L.E.4
  • 11
    • 9444245493 scopus 로고
    • Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance Nmr
    • a
    • Grzesiek S., Bax A. Correlating Backbone Amide and Side-Chain Resonances In Larger Proteins By Multiple Relayed Triple Resonance Nmr. J. Am. Chem. Soc. 114:1992;6291-6293. a.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 12
    • 44049117010 scopus 로고
    • Improved 3d triple-resonance nmr techniques applied to a 31-Kda protein
    • b
    • Grzesiek S., Bax A. Improved 3d Triple-Resonance Nmr Techniques Applied to a 31-Kda Protein. J. Magn. Reson. 96:1992;432-440. b.
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 13
    • 0027569483 scopus 로고
    • Amino-acid type determination in the sequential assignment procedure of uniformly C-13/N-15-enriched proteins
    • a
    • Grzesiek S., Bax A. Amino-Acid Type Determination In the Sequential Assignment Procedure Of Uniformly C-13/N-15-Enriched Proteins. J. Biomol. NMR. 3:1993;185-204. a.
    • (1993) J. Biomol. NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 14
    • 0027787894 scopus 로고
    • The importance of not saturating H2o in protein nmr - Application to sensitivity enhancement and noe measurements
    • b
    • Grzesiek S., Bax A. The Importance Of Not Saturating H2o In Protein Nmr - Application to Sensitivity Enhancement and Noe Measurements. J. Am. Chem. Soc. 115:1993;12593-12594. b.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 15
    • 0036172186 scopus 로고    scopus 로고
    • The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
    • Hayashi I., Vuori K., Liddington R.C. The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nat. Struct. Biol. 9:2002;101-106.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 16
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand J.D., Schaller M.D., Parsons J.T. Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell. 6:1995;637-647.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 17
    • 34249765651 scopus 로고
    • NMR view - A computer-program for the visualization and analysis of Nmr data
    • Johnson B.A., Blevins R.A. NMR View - a Computer-Program For the Visualization and Analysis Of Nmr Data. J. Biomol. NMR. 4:1994;603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and trhe location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and trhe location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0003026536 scopus 로고
    • Practical aspects of 3d heteronuclear nmr of proteins
    • a
    • Kay L.E., Marion D., Bax A. Practical Aspects Of 3d Heteronuclear Nmr Of Proteins. J. Magn. Reson. 84:1989;72-84. a.
    • (1989) J. Magn. Reson. , vol.84 , pp. 72-84
    • Kay, L.E.1    Marion, D.2    Bax, A.3
  • 20
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by N-15 inverse detected heteronuclear Nmr-spectroscopy - Application to staphylococcal nuclease
    • b
    • Kay L.E., Torchia D.A., Bax A. Backbone Dynamics Of Proteins As Studied By N-15 Inverse Detected Heteronuclear Nmr-Spectroscopy - Application to Staphylococcal Nuclease. Biochemistry. 28:1989;8972-8979. b.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 21
    • 44949291986 scopus 로고
    • 3-Dimensional triple-resonance Nmr-spectroscopy of isotopically enriched proteins
    • Kay L.E., Ikura M., Tschudin R., Bax A. 3-Dimensional Triple-Resonance Nmr-Spectroscopy Of Isotopically Enriched Proteins. J. Magn. Reson. 89:1990;496-514.
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 22
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., Saarinen T. Pure Absorption Gradient Enhanced Heteronuclear Single Quantum Correlation Spectroscopy With Improved Sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 23
    • 0036197382 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase
    • Liu G., Guibao C.D., Zheng J. Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase. Mol. Cell. Biol. 22:2002;2751-2760.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2751-2760
    • Liu, G.1    Guibao, C.D.2    Zheng, J.3
  • 24
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J.U., Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature. 356:1992;83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 25
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Munoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. Nat. Struct. Biol. 1:1994;399-409.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 26
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos S.N., Turner C.E. Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J. Cell Biol. 151:2000;1435-1448.
    • (2000) J. Cell Biol. , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 27
    • 0002059999 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    • Nikolopoulos S.N., Turner C.E. Integrin-Linked Kinase (ILK) Binding to Paxillin LD1 Motif Regulates ILK Localization to Focal Adhesions. J. Biol. Chem. 2:2001;E231-E236.
    • (2001) J. Biol. Chem. , vol.2
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 28
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 29
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature. 372:1994;786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van der Geer, P.4
  • 31
    • 45449123980 scopus 로고
    • Iterative schemes for bilinear operators - Application to spin decoupling
    • Shaka A.J., Lee C.J., Pines A. Iterative Schemes for Bilinear Operators - Application to Spin Decoupling. J. Magn. Reson. 77:1988;274-293.
    • (1988) J. Magn. Reson. , vol.77 , pp. 274-293
    • Shaka, A.J.1    Lee, C.J.2    Pines, A.3
  • 32
    • 0035967880 scopus 로고    scopus 로고
    • Fugue: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J., Blundell T.L., Mizuguchi K. Fugue. sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties J. Mol. Biol. 310:2001;243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 33
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl M.J. Recognition of errors in three-dimensional structures of proteins. Proteins. 17:1993;355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 34
    • 0028980418 scopus 로고
    • Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK
    • Tachibana K., Sato T., D'Avirro N., Morimoto C. Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. J. Exp. Med. 182:1995;1089-1099.
    • (1995) J. Exp. Med. , vol.182 , pp. 1089-1099
    • Tachibana, K.1    Sato, T.2    D'Avirro, N.3    Morimoto, C.4
  • 36
    • 0031001560 scopus 로고    scopus 로고
    • The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton
    • Tong X., Howley P.M. The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton. Proc. Natl. Acad. Sci. USA. 94:1997;4412-4417.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4412-4417
    • Tong, X.1    Howley, P.M.2
  • 37
    • 0031439110 scopus 로고    scopus 로고
    • The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase
    • Tong X., Salgia R., Li J.L., Griffin J.D., Howley P.M. The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase. J. Biol. Chem. 272:1997;33373-33376.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33373-33376
    • Tong, X.1    Salgia, R.2    Li, J.L.3    Griffin, J.D.4    Howley, P.M.5
  • 39
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner C.E., Kramarcy N., Sealock R., Burridge K. Paxillin. a new vinculin-binding protein present in focal adhesions Exp. Cell Res. 111:1990;1059-1068.
    • (1990) Exp. Cell Res. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Kramarcy, N.2    Sealock, R.3    Burridge, K.4
  • 41
    • 0028324634 scopus 로고
    • Characterisation of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin
    • Wood C.K., Turner C.E., Jackson P., Critchley D.R. Characterisation of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin. J. Cell Sci. 107:1994;709-717.
    • (1994) J. Cell Sci. , vol.107 , pp. 709-717
    • Wood, C.K.1    Turner, C.E.2    Jackson, P.3    Critchley, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.