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Volumn 50, Issue 4, 2011, Pages 566-573

Molecular and structural insight into the role of key residues of thrombospondin-1 and calreticulin in thrombospondin-1-calreticulin binding

Author keywords

[No Author keywords available]

Indexed keywords

ANOIKIS; CALRETICULIN; CELL MIGRATION; CELL SURFACES; CELL-BASED; CELLULAR ACTIVITIES; COMPLEX STRUCTURE; CONFORMATIONAL AND STRUCTURAL CHANGES; CONFORMATIONAL FLEXIBILITY; CORRELATED MOTIONS; EXPERIMENTAL OBSERVATION; FOCAL ADHESIONS; MOLECULAR DYNAMICS SIMULATIONS; SIMULATION RESULT; STEERED MOLECULAR DYNAMICS SIMULATIONS; STRUCTURAL BASIS; STRUCTURAL INSIGHTS; THROMBOSPONDIN; WILD TYPES;

EID: 79952077436     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101639y     Document Type: Article
Times cited : (16)

References (32)
  • 1
    • 0035058769 scopus 로고    scopus 로고
    • The de-adhesive activity of matricellular proteins: Is intermediate cell adhesion an adaptive state?
    • Murphy-Ullrich, J. E. (2001) The de-adhesive activity of matricellular proteins: Is intermediate cell adhesion an adaptive state? J. Clin. Invest. 107, 785-790. (Pubitemid 32274027)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.7 , pp. 785-790
    • Murphy-Ullrich, J.E.1
  • 2
    • 0032374079 scopus 로고    scopus 로고
    • Signaling of de-adhesion in cellular regulation and motility
    • DOI 10.1002/(SICI)1097-0029(19981201)43:5<420::AID-JEMT8>3.0.CO;2-B
    • Greenwood, J. A., and Murphy-Ullrich, J. E. (1998) Signaling of deadhesion in cellular regulation and motility. Microsc. Res. Tech. 43, 420-432. (Pubitemid 28565789)
    • (1998) Microscopy Research and Technique , vol.43 , Issue.5 , pp. 420-432
    • Greenwood, J.A.1    Murphy-Ullrich, J.E.2
  • 3
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea, S., Orr, A. W., Pallero, M. A., Eggleton, P., and Murphy- Ullrich, J. E. (2000) Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J. Biol. Chem. 275, 36358-36368.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy- Ullrich, J.E.5
  • 4
    • 0037020093 scopus 로고    scopus 로고
    • The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin
    • Goicoechea, S., Pallero, M. A., Eggleton, P., Michalak, M., and Murphy-Ullrich, J. E. (2002) The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin. J. Biol. Chem. 277, 37219-37228.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37219-37228
    • Goicoechea, S.1    Pallero, M.A.2    Eggleton, P.3    Michalak, M.4    Murphy-Ullrich, J.E.5
  • 5
    • 0042170209 scopus 로고    scopus 로고
    • Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration
    • DOI 10.1242/jcs.00600
    • Orr, A. W., Elzie, C. A., Kucik, D. F., and Murphy-Ullrich, J. E. (2003) Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration. J. Cell Sci. 116, 2917-2927. (Pubitemid 36926981)
    • (2003) Journal of Cell Science , vol.116 , Issue.14 , pp. 2917-2927
    • Orr, A.W.1    Elzie, C.A.2    Kucik, D.F.3    Murphy-Ullrich, J.E.4
  • 6
    • 0037477628 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly
    • DOI 10.1083/jcb.200302069
    • Orr, A. W., Pedraza, C. E., Pallero, M. A., Elzie, C. A., Goicoechea, S., Strickland, D. K., and Murphy-Ullrich, J. E. (2003) Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly. J. Cell Biol. 161, 1179-1189. (Pubitemid 36870178)
    • (2003) Journal of Cell Biology , vol.161 , Issue.6 , pp. 1179-1189
    • Orr, A.W.1    Pedraza, C.E.2    Pallero, M.A.3    Elzie, C.A.4    Goicoechea, S.5    Strickland, D.K.6    Murphy-Ullrich, J.E.7
  • 7
    • 55549142180 scopus 로고    scopus 로고
    • Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis
    • Pallero, M. A., Elzie, C. A., Chen, J., Mosher, D. F., and Murphy- Ullrich, J. E. (2008) Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis. FASEB J. 22, 3968-3979.
    • (2008) FASEB J. , vol.22 , pp. 3968-3979
    • Pallero, M.A.1    Elzie, C.A.2    Chen, J.3    Mosher, D.F.4    Murphy- Ullrich, J.E.5
  • 9
    • 77957357565 scopus 로고    scopus 로고
    • The calreticulin-binding sequence of thrombospondin 1 regulates collagen expression and organization during tissue remodeling
    • Sweetwyne, M. T., Pallero, M. A., Lu, A., Van Duyn Graham, L., and Murphy-Ullrich, J. E. (2010) The calreticulin-binding sequence of thrombospondin 1 regulates collagen expression and organization during tissue remodeling. Am. J. Pathol. 177, 1710-1724.
    • (2010) Am. J. Pathol. , vol.177 , pp. 1710-1724
    • Sweetwyne, M.T.1    Pallero, M.A.2    Lu, A.3    Van Duyn Graham, L.4    Murphy-Ullrich, J.E.5
  • 10
    • 0035049231 scopus 로고    scopus 로고
    • Thrombospondins as matricellular modulators of cell function
    • Bornstein, P. (2001) Thrombospondins as matricellular modulators of cell function. J. Clin. Invest. 107, 929-934. (Pubitemid 32323400)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.8 , pp. 929-934
    • Bornstein, P.1
  • 11
    • 0029347102 scopus 로고
    • Diversity of function is inherent in matricellular proteins: An appraisal of thrombospondin 1
    • Bornstein, P. (1995) Diversity of function is inherent in matricellular proteins: An appraisal of thrombospondin 1. J. Cell Biol. 130, 503-506.
    • (1995) J. Cell Biol. , vol.130 , pp. 503-506
    • Bornstein, P.1
  • 14
    • 0035846853 scopus 로고    scopus 로고
    • Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment
    • DOI 10.1016/S0014-5793(00)02382-6, PII S0014579300023826
    • Ellgaard, L., Riek, R., Braun, D., Herrmann, T., Helenius, A., and Wuthrich, K. (2001) Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment. FEBS Lett. 488, 69-73. (Pubitemid 32332809)
    • (2001) FEBS Letters , vol.488 , Issue.1-2 , pp. 69-73
    • Ellgaard, L.1    Riek, R.2    Braun, D.3    Herrmann, T.4    Helenius, A.5    Wuthrich, K.6
  • 15
    • 33646091537 scopus 로고    scopus 로고
    • The calcium- and zinc-responsive regions of calreticulin reside strictly in the N-/C-domain
    • Tan, Y., Chen, M., Li, Z., Mabuchi, K., and Bouvier, M. (2006) The calcium- and zinc-responsive regions of calreticulin reside strictly in the N-/C-domain. Biochim. Biophys. Acta 1760, 745-753.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 745-753
    • Tan, Y.1    Chen, M.2    Li, Z.3    Mabuchi, K.4    Bouvier, M.5
  • 16
    • 0027377783 scopus 로고
    • Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity
    • Murphy-Ullrich, J. E., Gurusiddappa, S., Frazier, W. A., and Hook, M. (1993) Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity. J. Biol. Chem. 268, 26784-26789. (Pubitemid 23361768)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.35 , pp. 26784-26789
    • Murphy-Ullrich, J.E.1    Gurusiddappa, S.2    Frazier, W.A.3    Hook, M.4
  • 17
    • 33644807623 scopus 로고    scopus 로고
    • The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin
    • DOI 10.1016/j.str.2005.09.017, PII S0969212605003977
    • Tan, K., Duquette, M., Liu, J. H., Zhang, R., Joachimiak, A., Wang, J. H., and Lawler, J. (2006) The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin. Structure 14, 33-42. (Pubitemid 43350071)
    • (2006) Structure , vol.14 , Issue.1 , pp. 33-42
    • Tan, K.1    Duquette, M.2    Liu, J.-H.3    Zhang, R.4    Joachimiak, A.5    Wang, J.-H.6    Lawler, J.7
  • 18
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • DOI 10.1016/S1097-2765(01)00318-5
    • Schrag, J. D., Bergeron, J. J., Li, Y., Borisova, S., Hahn, M., Thomas, D. Y., and Cygler, M. (2001) The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8, 633-644. (Pubitemid 32946940)
    • (2001) Molecular Cell , vol.8 , Issue.3 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.M.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6    Cygler, M.7
  • 20
    • 77951681940 scopus 로고    scopus 로고
    • Structural insight into the role of thrombospondin-1 binding to calreticulin in calreticulin- induced focal adhesion disassembly
    • Yan, Q., Murphy-Ullrich, J. E., and Song, Y. (2010) Structural insight into the role of thrombospondin-1 binding to calreticulin in calreticulin- induced focal adhesion disassembly. Biochemistry 49, 3685-3694.
    • (2010) Biochemistry , vol.49 , pp. 3685-3694
    • Yan, Q.1    Murphy-Ullrich, J.E.2    Song, Y.3
  • 23
    • 77954377943 scopus 로고    scopus 로고
    • Role of altered sialylation of the i-like domain of β1 integrin in the binding of fibronectin to β1 integrin: Thermodynamics and conformational analyses
    • Pan, D., and Song, Y. (2010) Role of Altered Sialylation of the I-like Domain of β1 Integrin in the Binding of Fibronectin to β1 Integrin: Thermodynamics and Conformational Analyses. Biophys. J. 99, 208-217.
    • (2010) Biophys. J. , vol.99 , pp. 208-217
    • Pan, D.1    Song, Y.2
  • 24
    • 58749083051 scopus 로고    scopus 로고
    • Conformation and free energy analyses of the complex of calciumbound calmodulin and the Fas death domain
    • Suever, J. D., Chen, Y., McDonald, J. M., and Song, Y. (2008) Conformation and free energy analyses of the complex of calciumbound calmodulin and the Fas death domain. Biophys. J. 95, 5913-5921.
    • (2008) Biophys. J. , vol.95 , pp. 5913-5921
    • Suever, J.D.1    Chen, Y.2    McDonald, J.M.3    Song, Y.4
  • 25
    • 58149308800 scopus 로고    scopus 로고
    • Effect of altered glycosylation on the structure of the I-like domain of β1 integrin: A molecular dynamics study
    • Liu, Y., Pan, D., Bellis, S. L., and Song, Y. (2008) Effect of altered glycosylation on the structure of the I-like domain of β1 integrin: A molecular dynamics study. Proteins 73, 989-1000.
    • (2008) Proteins , vol.73 , pp. 989-1000
    • Liu, Y.1    Pan, D.2    Bellis, S.L.3    Song, Y.4
  • 26
    • 26644433416 scopus 로고    scopus 로고
    • Molecular dynamics simulations of salicylate effects on the micro- and mesoscopic properties of a dipalmitoylphosphatidylcholine bilayer
    • DOI 10.1021/bi0506829
    • Song, Y., Guallar, V., and Baker, N. A. (2005) Molecular dynamics simulations of salicylate effects on the micro- and mesoscopic properties of a dipalmitoylphosphatidylcholine bilayer. Biochemistry 44, 13425-13438. (Pubitemid 41443670)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13425-13438
    • Song, Y.1    Guallar, V.2    Baker, N.A.3
  • 27
    • 0030987036 scopus 로고    scopus 로고
    • Molecular dynamics study of unbinding of the avidin-biotin complex
    • Izrailev, S., Stepaniants, S., Balsera, M., Oono, Y., and Schulten, K. (1997) Molecular dynamics study of unbinding of the avidin-biotin complex. Biophys. J. 72, 1568-1581. (Pubitemid 27133097)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1568-1581
    • Izrailev, S.1    Stepaniants, S.2    Balsera, M.3    Oono, Y.4    Schulten, K.5
  • 28
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu, H., Isralewitz, B., Krammer, A., Vogel, V., and Schulten, K. (1998) Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75, 662-671. (Pubitemid 28357508)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 29
    • 0036428792 scopus 로고    scopus 로고
    • 10 by steered molecular dynamics
    • DOI 10.1016/S0022-2836(02)01001-X
    • Gao, M., Craig, D., Vogel, V., and Schulten, K. (2002) Identifying unfolding intermediates of FN-III(10) by steered molecular dynamics. J. Mol. Biol. 323, 939-950. (Pubitemid 35341066)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.5 , pp. 939-950
    • Gao, M.1    Craig, D.2    Vogel, V.3    Schulten, K.4
  • 30
    • 40149107045 scopus 로고    scopus 로고
    • How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism
    • Hytonen, V. P., and Vogel, V. (2008) How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism. PLoS Comput. Biol. 4, No. e24.
    • (2008) PLoS Comput. Biol. , vol.4 , Issue.E24
    • Hytonen, V.P.1    Vogel, V.2
  • 32
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. G. (1993) Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.G.3


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