메뉴 건너뛰기




Volumn 17, Issue 4, 2005, Pages 513-523

Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility

Author keywords

[No Author keywords available]

Indexed keywords

LIM PROTEIN; PROTEIN DERIVATIVE;

EID: 13944249955     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.12.031     Document Type: Article
Times cited : (110)

References (54)
  • 1
    • 0034383397 scopus 로고    scopus 로고
    • The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction
    • Barnett P., Bottger G., Klein A.T., Tabak H.F., Distel B. The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction. EMBO J. 19:2000;6382-6391
    • (2000) EMBO J. , vol.19 , pp. 6382-6391
    • Barnett, P.1    Bottger, G.2    Klein, A.T.3    Tabak, H.F.4    Distel, B.5
  • 2
    • 0031281898 scopus 로고    scopus 로고
    • Zyxin: Zinc fingers at sites of cell adhesion
    • Beckerle M. Zyxin. zinc fingers at sites of cell adhesion Bioessays. 19:1997;949-957
    • (1997) Bioessays , vol.19 , pp. 949-957
    • Beckerle, M.1
  • 3
    • 0038383014 scopus 로고    scopus 로고
    • The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network
    • Bladt F., Aippersbach E., Gelkop S., Strasser G.A., Nash P., Tafuri A., Gertler F.B., Pawson T. The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network. Mol. Cell. Biol. 23:2003;4586-4597
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4586-4597
    • Bladt, F.1    Aippersbach, E.2    Gelkop, S.3    Strasser, G.A.4    Nash, P.5    Tafuri, A.6    Gertler, F.B.7    Pawson, T.8
  • 4
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch C., Fassler R. The integrin-actin connection, an eternal love affair. EMBO J. 22:2003;2324-2333
    • (2003) EMBO J. , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fassler, R.2
  • 5
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: Regulators of actin cytoskeleton
    • Buday L., Wunderlich L., Tamas P. The Nck family of adapter proteins. Regulators of actin cytoskeleton Cell. Signal. 14:2002;723-731
    • (2002) Cell. Signal. , vol.14 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 6
    • 0842309767 scopus 로고    scopus 로고
    • Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly
    • Campellone K.G., Rankin S., Pawson T., Kirschner M.W., Tipper D.J., Leong J.M. Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly. J. Cell Biol. 64:2004;407-416
    • (2004) J. Cell Biol. , vol.64 , pp. 407-416
    • Campellone, K.G.1    Rankin, S.2    Pawson, T.3    Kirschner, M.W.4    Tipper, D.J.5    Leong, J.M.6
  • 7
    • 0037138380 scopus 로고    scopus 로고
    • Can we infer peptide recognition specificity mediated by SH3 domains?
    • Cesareni G., Panni S., Nardelli G., Castagnoli L. Can we infer peptide recognition specificity mediated by SH3 domains? FEBS Lett. 513:2002;38-44
    • (2002) FEBS Lett. , vol.513 , pp. 38-44
    • Cesareni, G.1    Panni, S.2    Nardelli, G.3    Castagnoli, L.4
  • 8
    • 0033623198 scopus 로고    scopus 로고
    • Nckbeta adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bb
    • Chen M., She H., Kim A., Woodley D.T., Li W. Nckbeta adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bb. Mol. Cell. Biol. 20:2000;7867-7880
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7867-7880
    • Chen, M.1    She, H.2    Kim, A.3    Woodley, D.T.4    Li, W.5
  • 9
    • 0038409304 scopus 로고    scopus 로고
    • Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes
    • Clark K.A., McGrail M., Beckerle M.C. Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes. Development. 130:2003;2611-2621
    • (2003) Development , vol.130 , pp. 2611-2621
    • Clark, K.A.1    McGrail, M.2    Beckerle, M.C.3
  • 10
    • 0037433504 scopus 로고    scopus 로고
    • 1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
    • 1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics. J. Am. Chem. Soc. 125:2003;2902-2912
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2902-2912
    • Clore, G.M.1    Schwieters, C.D.2
  • 11
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR. 13:1999;289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 12
    • 0035855819 scopus 로고    scopus 로고
    • The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
    • Cowan C.A., Henkemeyer M. The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals. Nature. 413:2001;174-179
    • (2001) Nature , vol.413 , pp. 174-179
    • Cowan, C.A.1    Henkemeyer, M.2
  • 13
    • 0037543995 scopus 로고    scopus 로고
    • Structural basis for the recognition of Idb1 by the N-terminal LIM domains of LMO2 and LMO4
    • Deane J.E., Mackay J.P., Kwan A.H.Y., Sum E.Y.M., Visvader J.E., Matthews J.M. Structural basis for the recognition of Idb1 by the N-terminal LIM domains of LMO2 and LMO4. EMBO J. 22:2003;2224-2233
    • (2003) EMBO J. , vol.22 , pp. 2224-2233
    • Deane, J.E.1    MacKay, J.P.2    Kwan, A.H.Y.3    Sum, E.Y.M.4    Visvader, J.E.5    Matthews, J.M.6
  • 15
    • 0035957958 scopus 로고    scopus 로고
    • Yes-associated protein and p53-binding protein-2 interact through their WW and SH3 domains
    • Espanel X., Sudol M. Yes-associated protein and p53-binding protein-2 interact through their WW and SH3 domains. J. Biol. Chem. 276:2001;14514-14523
    • (2001) J. Biol. Chem. , vol.276 , pp. 14514-14523
    • Espanel, X.1    Sudol, M.2
  • 16
    • 0345803932 scopus 로고    scopus 로고
    • PINCH-1 is an obligate partner of ILK functioning in cell shape modulation, motility and survival
    • Fukuda T., Chen K., Shi X., Wu C. PINCH-1 is an obligate partner of ILK functioning in cell shape modulation, motility and survival. J. Biol. Chem. 278:2003;51324-51333
    • (2003) J. Biol. Chem. , vol.278 , pp. 51324-51333
    • Fukuda, T.1    Chen, K.2    Shi, X.3    Wu, C.4
  • 17
    • 0000041361 scopus 로고
    • A common-sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett D.S., Powers R., Gronenborn A.M., Clore G.M. A common-sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95:1991;214-220
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 20
    • 0034753803 scopus 로고    scopus 로고
    • A novel, specific interaction involving the Csk SH3 domain and its natural ligand
    • Ghose R., Shehtman A., Goger M.J., Ji H., Cowburn D. A novel, specific interaction involving the Csk SH3 domain and its natural ligand. Nat. Struct. Biol. 8:2001;998-1004
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 998-1004
    • Ghose, R.1    Shehtman, A.2    Goger, M.J.3    Ji, H.4    Cowburn, D.5
  • 23
    • 0033545214 scopus 로고    scopus 로고
    • A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans
    • Hobert O., Moerman D.G., Clark K.A., Beckerle M.C., Ruvkun G. A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans. J. Cell Biol. 144:1999;45-57
    • (1999) J. Cell Biol. , vol.144 , pp. 45-57
    • Hobert, O.1    Moerman, D.G.2    Clark, K.A.3    Beckerle, M.C.4    Ruvkun, G.5
  • 26
    • 0035900669 scopus 로고    scopus 로고
    • Grb4/Nckbeta acts as a nuclear repressor of v-Abl-induced transcription from c-jun/c-fos promoter elements
    • Jahn T., Seipel P., Coutinho S., Miething C., Peschel C., Duyster J. Grb4/Nckbeta acts as a nuclear repressor of v-Abl-induced transcription from c-jun/c-fos promoter elements. J. Biol. Chem. 276:2001;43419-43427
    • (2001) J. Biol. Chem. , vol.276 , pp. 43419-43427
    • Jahn, T.1    Seipel, P.2    Coutinho, S.3    Miething, C.4    Peschel, C.5    Duyster, J.6
  • 28
    • 0034659759 scopus 로고    scopus 로고
    • SH3 domain recognition of a proline-independent tyrosine-based RkxxYxY motif in immune cell adapter SKAP55
    • Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., Rudd C.E. SH3 domain recognition of a proline-independent tyrosine-based RkxxYxY motif in immune cell adapter SKAP55. EMBO J. 19:2000;2889-2899
    • (2000) EMBO J. , vol.19 , pp. 2889-2899
    • Kang, H.1    Freund, C.2    Duke-Cohan, J.S.3    Musacchio, A.4    Wagner, G.5    Rudd, C.E.6
  • 30
    • 0034535340 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
    • Kato M., Miyazawa K., Kitamura N. A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J. Biol. Chem. 275:2000;37481-37487
    • (2000) J. Biol. Chem. , vol.275 , pp. 37481-37487
    • Kato, M.1    Miyazawa, K.2    Kitamura, N.3
  • 31
    • 0029881007 scopus 로고    scopus 로고
    • Molmol: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. Molmol. a program for display and analysis of macromolecular structures J. Mol. Graph. 14:1996;51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 32
  • 33
    • 0035280175 scopus 로고    scopus 로고
    • The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif
    • Lewitzky M., Kardinal C., Gehring N.H., Schmidt E.K., Konkol B., Eulitz M., Birchmeier W., Schaeper U., Feller S.M. The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif. Oncogene. 20:2001;1052-1062
    • (2001) Oncogene , vol.20 , pp. 1052-1062
    • Lewitzky, M.1    Kardinal, C.2    Gehring, N.H.3    Schmidt, E.K.4    Konkol, B.5    Eulitz, M.6    Birchmeier, W.7    Schaeper, U.8    Feller, S.M.9
  • 34
    • 0037291960 scopus 로고    scopus 로고
    • Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide: A novel mode of peptide recognition
    • Liu Q., Berry D., Nash P., Pawson T., McGlade C.J., Li S.S. Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide. a novel mode of peptide recognition Mol. Cell. 11:2003;471-481
    • (2003) Mol. Cell , vol.11 , pp. 471-481
    • Liu, Q.1    Berry, D.2    Nash, P.3    Pawson, T.4    McGlade, C.J.5    Li, S.S.6
  • 36
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer B.J. SH3 domains. complexity in moderation J. Cell Sci. 114:2001;1253-1263
    • (2001) J. Cell Sci. , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 38
    • 0026319199 scopus 로고
    • Protein folding and association - Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 39
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren I.M., Thornton J.M. Diversity of protein-protein interactions. EMBO J. 22:2003;3486-3492
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 41
    • 0034919312 scopus 로고    scopus 로고
    • Protein-protein interactions probed by NMR spectroscopy
    • Qin J., Vinogradova O., Gronenborn A. Protein-protein interactions probed by NMR spectroscopy. Methods Enzymol. 339:2001;377-389
    • (2001) Methods Enzymol. , vol.339 , pp. 377-389
    • Qin, J.1    Vinogradova, O.2    Gronenborn, A.3
  • 42
    • 0346965734 scopus 로고    scopus 로고
    • Inducible clustering of membrane-targeted SH3 domains of the adaptor protein Nck triggers localized actin polymerization
    • Rivera G.M., Briceno C.A., Takeshima F., Snapper S.B., Mayer B.J. Inducible clustering of membrane-targeted SH3 domains of the adaptor protein Nck triggers localized actin polymerization. Curr. Biol. 14:2004;11-22
    • (2004) Curr. Biol. , vol.14 , pp. 11-22
    • Rivera, G.M.1    Briceno, C.A.2    Takeshima, F.3    Snapper, S.B.4    Mayer, B.J.5
  • 45
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways
    • Tu Y., Li F., Wu C. Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways. Mol. Biol. Cell. 9:1998;3367-3382
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 46
    • 0035793946 scopus 로고    scopus 로고
    • Identification and kinetic analysis of the interaction between Nck-2 and DOCK180
    • Tu Y., Kucik D.F., Wu C. Identification and kinetic analysis of the interaction between Nck-2 and DOCK180. FEBS Lett. 491:2001;193-199
    • (2001) FEBS Lett. , vol.491 , pp. 193-199
    • Tu, Y.1    Kucik, D.F.2    Wu, C.3
  • 47
    • 0042971650 scopus 로고    scopus 로고
    • Molecular interactions mediating T cell antigen recognition
    • van der Merwe P.A., Davis S.J. Molecular interactions mediating T cell antigen recognition. Annu. Rev. Immunol. 21:2003;659-684
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 659-684
    • Van Der Merwe, P.A.1    Davis, S.J.2
  • 48
    • 0035895898 scopus 로고    scopus 로고
    • Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain
    • Velyvis A., Yang Y., Wu C., Qin J. Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain. J. Biol. Chem. 276:2001;4932-4939
    • (2001) J. Biol. Chem. , vol.276 , pp. 4932-4939
    • Velyvis, A.1    Yang, Y.2    Wu, C.3    Qin, J.4
  • 49
    • 0037743516 scopus 로고    scopus 로고
    • Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling
    • Velyvis A., Vinogradova O., Wu C., Qin J. Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling. Nat. Struct. Biol. 10:2003;558-564
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 558-564
    • Velyvis, A.1    Vinogradova, O.2    Wu, C.3    Qin, J.4
  • 51
    • 0033379103 scopus 로고    scopus 로고
    • Integrin-linked kinase and PINCH: Partners in regulation of cell-extracellular matrix interaction and signal transduction
    • Wu C. Integrin-linked kinase and PINCH. partners in regulation of cell-extracellular matrix interaction and signal transduction J. Cell Sci. 112:1999;4485-4489
    • (1999) J. Cell Sci. , vol.112 , pp. 4485-4489
    • Wu, C.1
  • 52
    • 0035969233 scopus 로고    scopus 로고
    • Integrin linked kinase (ILK) and its interactors: A new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
    • Wu C., Dedhar S. Integrin linked kinase (ILK) and its interactors. a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes J. Cell Biol. 155:2001;505-510
    • (2001) J. Cell Biol. , vol.155 , pp. 505-510
    • Wu, C.1    Dedhar, S.2
  • 53
    • 0037016703 scopus 로고    scopus 로고
    • A critical role of the PINCH-integrin-linked kinase interaction in the regulation of cell shape change and migration
    • Zhang Y., Guo L., Chen K., Wu C. A critical role of the PINCH-integrin-linked kinase interaction in the regulation of cell shape change and migration. J. Biol. Chem. 277:2002;318-326
    • (2002) J. Biol. Chem. , vol.277 , pp. 318-326
    • Zhang, Y.1    Guo, L.2    Chen, K.3    Wu, C.4
  • 54
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage λ N-peptide/boxB RNA complex
    • Zwahlen C., Legault P., Vincent S.J.F., Greenblatt J., Konrat R., Kay L.E. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy. application to a bacteriophage λ N-peptide/boxB RNA complex J. Am. Chem. Soc. 119:1997;711-721
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 711-721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.