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Volumn 45, Issue 7, 2006, Pages 2042-2052

Binding of laminin α1-chain LG4-5 domain to α-dystroglycan causes tyrosine phosphorylation of syntrophin to initiate Rac1 signaling

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BINDING ENERGY; BIOCHEMISTRY; PHOSPHATES;

EID: 33144482572     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0519957     Document Type: Article
Times cited : (33)

References (44)
  • 1
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman, E. P., Brown, R. H., and Kunkel, L. M. (1987) Dystrophin: the protein product of the Duchenne muscular dystrophy locus, Cell 51, 919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.H.2    Kunkel, L.M.3
  • 2
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti, J. M., and Campbell, K. P. (1991) Membrane organization of the dystrophin-glycoprotein complex, Cell 66, 1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 3
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J. M., and Campbell, K. P. (1993) A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin, J. Cell Biol. 122, 809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 4
    • 0029149757 scopus 로고
    • Interactions between dystrophin glycoprotein complex proteins
    • Madhavan, R., and Jarrett, H. W. (1995) Interactions between dystrophin glycoprotein complex proteins, Biochemistry 34, 12204-12209.
    • (1995) Biochemistry , vol.34 , pp. 12204-12209
    • Madhavan, R.1    Jarrett, H.W.2
  • 5
    • 0028928013 scopus 로고
    • Alternate binding of actin and calmodulin to multiple sites on dystrophin
    • Jarrett, H. W., and Foster, J. L. (1995) Alternate binding of actin and calmodulin to multiple sites on dystrophin, J. Biol. Chem. 270, 5578-5586.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5578-5586
    • Jarrett, H.W.1    Foster, J.L.2
  • 6
    • 0036842214 scopus 로고    scopus 로고
    • Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells
    • Langenbach, K. J., and Rando, T. A. (2002) Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells, Muscle Nerve 26, 644-653.
    • (2002) Muscle Nerve , vol.26 , pp. 644-653
    • Langenbach, K.J.1    Rando, T.A.2
  • 7
    • 12144255586 scopus 로고    scopus 로고
    • Laminin-α1 globular domains three and four induce heterotrimeric G-protein binding to α-syntrophin's PDZ domain
    • Zhou, Y. W., Oak, S. A., Senogles, S. E., and Jarrett, H. W. (2005) Laminin-α1 globular domains three and four induce heterotrimeric G-protein binding to α-syntrophin's PDZ domain, Am. J. Physiol. Cell Physiol. 288, C377-88.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Zhou, Y.W.1    Oak, S.A.2    Senogles, S.E.3    Jarrett, H.W.4
  • 8
    • 0141960276 scopus 로고    scopus 로고
    • Skeletal muscle signaling pathway through the dystrophin glycoprotein complex and Rac1
    • Oak, S. A., Zhou, Y. W., and Jarrett, H. W. (2003) Skeletal muscle signaling pathway through the dystrophin glycoprotein complex and Rac1, J. Biol. Chem. 278, 39287-39295.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39287-39295
    • Oak, S.A.1    Zhou, Y.W.2    Jarrett, H.W.3
  • 9
    • 0030909575 scopus 로고    scopus 로고
    • Muscular dystrophies and the dystrophin-glycoprotein complex
    • Straub, V., and Campbell, K. P. (1997) Muscular dystrophies and the dystrophin-glycoprotein complex, Curr. Opin. Neurol. 10, 168-175.
    • (1997) Curr. Opin. Neurol. , vol.10 , pp. 168-175
    • Straub, V.1    Campbell, K.P.2
  • 10
    • 4444234437 scopus 로고    scopus 로고
    • The congenital muscular dystrophies in 2004: A century of exciting progress
    • Muntoni, F., and Voit, T. (2004) The congenital muscular dystrophies in 2004: a century of exciting progress, Neuromuscul. Disord. 14, 635-49.
    • (2004) Neuromuscul. Disord. , vol.14 , pp. 635-649
    • Muntoni, F.1    Voit, T.2
  • 13
    • 0036086733 scopus 로고    scopus 로고
    • ECM is required for skeletal muscle differentiation independently of muscle regulatory factor expression
    • Osses, N., and Brandan, E. (2002) ECM is required for skeletal muscle differentiation independently of muscle regulatory factor expression, Am. J. Physiol. Cell Physiol. 282, 383-394.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282 , pp. 383-394
    • Osses, N.1    Brandan, E.2
  • 14
    • 0029033193 scopus 로고
    • Temporal and spatial appearance of alpha-dystroglycan in differentiated mouse myoblasts in culture
    • Kostrominova, T. Y., and Tanzer, M. L. (1995) Temporal and spatial appearance of alpha-dystroglycan in differentiated mouse myoblasts in culture, J. Cell Biochem. 58, 527-534.
    • (1995) J. Cell Biochem. , vol.58 , pp. 527-534
    • Kostrominova, T.Y.1    Tanzer, M.L.2
  • 15
    • 0038158092 scopus 로고    scopus 로고
    • Integrins, redundant or important players in skeletal muscle?
    • Mayer, U. (2003) Integrins, redundant or important players in skeletal muscle?, J. Biol. Chem. 278, 14587-14590.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14587-14590
    • Mayer, U.1
  • 16
    • 0029671374 scopus 로고    scopus 로고
    • Beta 1D integrin displaces the beta 1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin, A. M., Zhidkova, N. I., Balzac, F., Altruda, F., Tomatis, D., Maier, A., Tarone, G., Koteliansky, V. E., and Burridge, K. (1996) Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells, J. Cell Biol. 132, 211-226.
    • (1996) J. Cell Biol. , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 17
    • 0032870170 scopus 로고    scopus 로고
    • Differential distribution of dystrophin and beta-spectrin at the sarcolemma of fast twitch skeletal muscle fibers
    • Williams, M. W., and Bloch, R. J. (1999) Differential distribution of dystrophin and beta-spectrin at the sarcolemma of fast twitch skeletal muscle fibers, J. Muscle Res. Cell Motil. 20, 383-393.
    • (1999) J. Muscle Res. Cell Motil. , vol.20 , pp. 383-393
    • Williams, M.W.1    Bloch, R.J.2
  • 18
    • 0031939073 scopus 로고    scopus 로고
    • Bidirectional signaling between sarcoglycans and the integrin adhesion system in cultured L6 myocytes
    • Yoshida, T., Pan, Y., Hanada, H., Iwata, Y., and Shigekawa, M. (1998) Bidirectional signaling between sarcoglycans and the integrin adhesion system in cultured L6 myocytes, J. Biol. Chem. 273, 1583-1590.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1583-1590
    • Yoshida, T.1    Pan, Y.2    Hanada, H.3    Iwata, Y.4    Shigekawa, M.5
  • 19
    • 0034600063 scopus 로고    scopus 로고
    • Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin
    • Tisi, D., Talts, J. F., Timpl, R., and Hohenester, E. (2000) Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin, EMBO J. 19, 1432-1440.
    • (2000) EMBO J. , vol.19 , pp. 1432-1440
    • Tisi, D.1    Talts, J.F.2    Timpl, R.3    Hohenester, E.4
  • 20
    • 0025315789 scopus 로고
    • Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain
    • Deutzmann, R., Aumailley, M., Wiedemann, H., Pysny, W., Timpl, R., and Edgar, D. (1990) Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain, Eur. J. Biochem. 191, 513-522.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 513-522
    • Deutzmann, R.1    Aumailley, M.2    Wiedemann, H.3    Pysny, W.4    Timpl, R.5    Edgar, D.6
  • 21
    • 0038414615 scopus 로고    scopus 로고
    • Beta1 integrin and alpha-dystroglycan binding sites are localized to differenl laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain
    • Yu, H., and Talts, J. F. (2003) Beta1 integrin and alpha-dystroglycan binding sites are localized to differenl laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain, Biochem. J. 371, 289-299.
    • (2003) Biochem. J. , vol.371 , pp. 289-299
    • Yu, H.1    Talts, J.F.2
  • 23
    • 0035755874 scopus 로고    scopus 로고
    • Dystroglycan binding to laminin alpha1LG4 module influences epithelial morphogenesis of salivary gland and lung in vitro
    • Durbeej, M., Talts, J. F., Henry, M. D., Yurchenco, P. D., Campbell, K. P., and Ekblom, P. (2001) Dystroglycan binding to laminin alpha1LG4 module influences epithelial morphogenesis of salivary gland and lung in vitro, Differentiation 69, 121-134.
    • (2001) Differentiation , vol.69 , pp. 121-134
    • Durbeej, M.1    Talts, J.F.2    Henry, M.D.3    Yurchenco, P.D.4    Campbell, K.P.5    Ekblom, P.6
  • 24
    • 0030612270 scopus 로고    scopus 로고
    • Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle developmenl and in muscular dystrophies
    • Tiger, C. F., Champliaud, M. F., Pedrosa-Domellof, F., Thornell, L. E., Ekblom, P., and Gullberg, D. (1997) Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle developmenl and in muscular dystrophies., J Biol. Chem. 272, 28590-28595.
    • (1997) J Biol. Chem. , vol.272 , pp. 28590-28595
    • Tiger, C.F.1    Champliaud, M.F.2    Pedrosa-Domellof, F.3    Thornell, L.E.4    Ekblom, P.5    Gullberg, D.6
  • 25
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins
    • Talts, J. F., Andac, Z., Gohring, W., Brancaccio, A., and Timpl, R. (1999) Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins, EMBO J. 18, 863-870.
    • (1999) EMBO J. , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Gohring, W.3    Brancaccio, A.4    Timpl, R.5
  • 26
    • 0033231551 scopus 로고    scopus 로고
    • The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin
    • Hohenester, E., Tisi, D., Talts, J. F., and Timpl, R. (1999) The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin, Mol. Cell. 4, 783-792.
    • (1999) Mol. Cell. , vol.4 , pp. 783-792
    • Hohenester, E.1    Tisi, D.2    Talts, J.F.3    Timpl, R.4
  • 27
    • 0028178082 scopus 로고
    • Dystroglycan-α, a dystrophin-associated glycoprotein is a functional agrin receptor
    • Gee, S. H., Montanaro, F., Lindenbaum, M. H., and Carbonetta, S. (1994) Dystroglycan-α, a dystrophin-associated glycoprotein is a functional agrin receptor, Cell 77, 675-686.
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3    Carbonetta, S.4
  • 28
    • 0035908889 scopus 로고    scopus 로고
    • Mouse alpha1-syntrophin binding to Grb2: Further evidence of a role for syntrophin in cell signaling
    • Oak, S. A., Russo, K., Petrucci, T. C., and Jarrett, H. W. (2001) Mouse alpha1-syntrophin binding to Grb2: further evidence of a role for syntrophin in cell signaling, Biochemistry 40, 11270-11278.
    • (2001) Biochemistry , vol.40 , pp. 11270-11278
    • Oak, S.A.1    Russo, K.2    Petrucci, T.C.3    Jarrett, H.W.4
  • 29
    • 0035807788 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins
    • Sotgia, F., Lee, H., Bedford, M. T., Petrucci, T., Sudol, M., and Lisanti, M. P. (2001) Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins, Biochemistry 40, 14585-92.
    • (2001) Biochemistry , vol.40 , pp. 14585-14592
    • Sotgia, F.1    Lee, H.2    Bedford, M.T.3    Petrucci, T.4    Sudol, M.5    Lisanti, M.P.6
  • 31
    • 0032799032 scopus 로고    scopus 로고
    • Molecular and cellular analysis of Grb2 SH3 domain mutants: Interaction with Sos and dynamin
    • Vidal, M., Goudreau, N., Cornille, F., Cussac, D., Gincel, E., and Garbay, C. (1999) Molecular and cellular analysis of Grb2 SH3 domain mutants: interaction with Sos and dynamin, J. Mol. Biol. 290, 717-730.
    • (1999) J. Mol. Biol. , vol.290 , pp. 717-730
    • Vidal, M.1    Goudreau, N.2    Cornille, F.3    Cussac, D.4    Gincel, E.5    Garbay, C.6
  • 32
    • 0032828167 scopus 로고    scopus 로고
    • Phosphorylation of dystrophin and alpha-syntrophin by Ca(24-)-calmodulin dependent protein kinase II
    • Madhavan, R., and Jarrett, H. W. (1999) Phosphorylation of dystrophin and alpha-syntrophin by Ca(24-)-calmodulin dependent protein kinase II., Biochim. Biophys. Acta 1434, 260-274.
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 260-274
    • Madhavan, R.1    Jarrett, H.W.2
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding., Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0030583157 scopus 로고    scopus 로고
    • Localization of the dystrophin binding site at the carboxyl terminus of beta-dystroglycan
    • Rosa, G., Ceccarini, M., Cavaldesi, M., Zini, M., and Petrucci, T. C. (1996) Localization of the dystrophin binding site at the carboxyl terminus of beta-dystroglycan., Biochem. Biophys. Res. Commun. 223, 272-277.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 272-277
    • Rosa, G.1    Ceccarini, M.2    Cavaldesi, M.3    Zini, M.4    Petrucci, T.C.5
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4., Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0033531955 scopus 로고    scopus 로고
    • Characterization of Rac and Cdc42 Activation in chemoattractant- stimulated Human Nutrophils Using a Novel Assay for Active GTPases
    • Benard, V., Bohl, B. P., and Bokoch, G. M. (1999) Characterization of Rac and Cdc42 Activation in chemoattractant-stimulated Human Nutrophils Using a Novel Assay for Active GTPases, J. Biol. Chem. 274, 13198-13204.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13198-13204
    • Benard, V.1    Bohl, B.P.2    Bokoch, G.M.3
  • 37
    • 0034254730 scopus 로고    scopus 로고
    • The oligomerization of mouse a1-syntrophin and self-association of its pleckstrin homology domain 1
    • Oak, S., and Jarrett, H. W. (2000) The oligomerization of mouse a1-syntrophin and self-association of its pleckstrin homology domain 1, Biochemistry 39, 8870-8877.
    • (2000) Biochemistry , vol.39 , pp. 8870-8877
    • Oak, S.1    Jarrett, H.W.2
  • 38
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Ab1, Cortactin, p53bp2, PLCgamma, Crk, and Grb2
    • Sparks, A. B., Rider, J. E., Hoffman, N. G., Fowlkes, D. M., Quillam, L. A., and Kay, B. K. (1996) Distinct ligand preferences of Src homology 3 domains from Src, Yes, Ab1, Cortactin, p53bp2, PLCgamma, Crk, and Grb2., Proc. Natl. Acad. Sci. U.S.A. 93, 1540-1544.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4    Quillam, L.A.5    Kay, B.K.6
  • 39
    • 0034027602 scopus 로고    scopus 로고
    • Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin
    • James, M., Nuttall, A., Ilsley, J. L., Ottersbach, K., Tinsley, J. M., Sudol, M., and Winder, S. J. (2000) Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin, J. Cell Sci. 113, 1717-1726.
    • (2000) J. Cell Sci. , vol.113 , pp. 1717-1726
    • James, M.1    Nuttall, A.2    Ilsley, J.L.3    Ottersbach, K.4    Tinsley, J.M.5    Sudol, M.6    Winder, S.J.7
  • 40
    • 0034903234 scopus 로고    scopus 로고
    • The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation
    • Ilsley, J. L., Sudol, M., and Winder, S. J. (2001) The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation, Cell Signal. 13, 625-632.
    • (2001) Cell Signal , vol.13 , pp. 625-632
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 42
    • 0032759070 scopus 로고    scopus 로고
    • Lammins during muscle development and in muscular dystrophies
    • Gullberg, D., Tiger, C-F., and Veiling, T. (1999) Lammins during muscle development and in muscular dystrophies, Cell. Mol. Life Sci. 56, 442-460.
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 442-460
    • Gullberg, D.1    Tiger, C.-F.2    Veiling, T.3
  • 43
    • 0036197136 scopus 로고    scopus 로고
    • Merosin-integrin promotion of skeletal myofiber cell survival: Differentiation state-distinct involvement of p60Fyn tyrosine kinase and p38alpha stress-activated MAP kinase
    • Laprise, P., Poirier, E. M., Vezina, A., Rivard, N., and Vachon, P. H. (2002) Merosin-integrin promotion of skeletal myofiber cell survival: Differentiation state-distinct involvement of p60Fyn tyrosine kinase and p38alpha stress-activated MAP kinase, J. Cell Physiol. 191, 69-81.
    • (2002) J. Cell Physiol. , vol.191 , pp. 69-81
    • Laprise, P.1    Poirier, E.M.2    Vezina, A.3    Rivard, N.4    Vachon, P.H.5
  • 44
    • 0034978861 scopus 로고    scopus 로고
    • The elastin-laminin receptor functions as a mechanotransducer in vascular smooth muscle
    • Spofford, C. M., and Chilian, W. M. (2001) The elastin-laminin receptor functions as a mechanotransducer in vascular smooth muscle. Am. J. Physiol. Heart Circ. Physiol. 280, H1354-H1360.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.280
    • Spofford, C.M.1    Chilian, W.M.2


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