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Volumn 2, Issue 7, 1999, Pages 611-617

Interactions between β2-syntrophin and a family of microtubule- associated serine/threonine kinases

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; DYSTROPHIN; PROTEIN SERINE THREONINE KINASE; UTROPHIN;

EID: 0033363996     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/10165     Document Type: Article
Times cited : (137)

References (48)
  • 1
    • 0025648083 scopus 로고
    • Localization of dystrophin to postsynaptic regions of central nervous system cortical neurons
    • Lidov, H. G., Byers, T. J., Watkins, S. C. & Kunkel, L. M. Localization of dystrophin to postsynaptic regions of central nervous system cortical neurons. Nature 348, 725-728 (1990).
    • (1990) Nature , vol.348 , pp. 725-728
    • Lidov, H.G.1    Byers, T.J.2    Watkins, S.C.3    Kunkel, L.M.4
  • 2
    • 0028297196 scopus 로고
    • Dystrophin-related protein is found in the central nervous system of mice at various developmental stages, especially at the postsynaptic membrane
    • Kamakura, K. et al. Dystrophin-related protein is found in the central nervous system of mice at various developmental stages, especially at the postsynaptic membrane. J. Neurosci. Res. 37, 728-734 (1994).
    • (1994) J. Neurosci. Res. , vol.37 , pp. 728-734
    • Kamakura, K.1
  • 3
    • 0028845066 scopus 로고
    • Dystrophin-glycoprotein complex: Molecular organization and critical roles in skeletal muscle
    • Sunada, Y. & Campbell, K. P. Dystrophin-glycoprotein complex: molecular organization and critical roles in skeletal muscle. Curr. Opin. Neurol. 8, 379-384 (1995).
    • (1995) Curr. Opin. Neurol. , vol.8 , pp. 379-384
    • Sunada, Y.1    Campbell, K.P.2
  • 4
    • 0028178082 scopus 로고
    • Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • Gee, S. H., Montanaro, F., Lindenbaum, M. H. & Carbonetto, S. Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell 77, 675-686 (1994).
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3    Carbonetto, S.4
  • 5
    • 0031036977 scopus 로고    scopus 로고
    • Subtle neuromuscular defects in utrophin-deficient mice
    • Grady, R. M., Merlie, J. P. & Sanes, J. R. Subtle neuromuscular defects in utrophin-deficient mice. J. Cell Biol. 136, 871-882 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 871-882
    • Grady, R.M.1    Merlie, J.P.2    Sanes, J.R.3
  • 7
    • 0031451562 scopus 로고    scopus 로고
    • Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex
    • Crosbie, R. H., Heighway, J., Venzke, D. P., Lee, J. C. & Campbell, K. P. Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex. J. Biol. Chem. 272, 31221-31224 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31221-31224
    • Crosbie, R.H.1    Heighway, J.2    Venzke, D.P.3    Lee, J.C.4    Campbell, K.P.5
  • 8
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brenman, J. E., Chao, D. S., Xia, H. H., Aldape, K. & Bredt, D. S. Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 82, 743-752 (1995).
    • (1995) Cell , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.H.3    Aldape, K.4    Bredt, D.S.5
  • 9
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells - Caveolin-3 is a component of the sarcolemma and cofractionates with dystrophin and dystrophin-associated glycoproteins
    • Song, K. S. et al. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells - Caveolin-3 is a component of the sarcolemma and cofractionates with dystrophin and dystrophin-associated glycoproteins. J. Biol. Chem. 271, 15160-15165 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 15160-15165
    • Song, K.S.1
  • 10
    • 0029013870 scopus 로고
    • SH3 domain-mediated interaction of dystroglycan and Grb2
    • Yang, B. et al. SH3 domain-mediated interaction of dystroglycan and Grb2. J. Biol. Chem. 270, 11711-11714 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 11711-11714
    • Yang, B.1
  • 11
    • 0031974345 scopus 로고    scopus 로고
    • Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins
    • Gee, S. H. et al. Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins. J. Neurosci. 18, 128-137 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 128-137
    • Gee, S.H.1
  • 12
    • 0027375539 scopus 로고
    • Two forms of mouse syntrophin, a 58 kd dystrophin-associated protein, differ in primary structure and tissue distribution
    • Adams, M. E. et al. Two forms of mouse syntrophin, a 58 kd dystrophin-associated protein, differ in primary structure and tissue distribution. Neuron 11, 531-540 (1993).
    • (1993) Neuron , vol.11 , pp. 531-540
    • Adams, M.E.1
  • 13
    • 0028947998 scopus 로고
    • Syntrophin binds to an alternatively spliced exon of dystrophin
    • Ahn, A. H. & Kunkel, L. M. Syntrophin binds to an alternatively spliced exon of dystrophin. J. Cell Biol. 128, 363-371 (1995).
    • (1995) J. Cell Biol. , vol.128 , pp. 363-371
    • Ahn, A.H.1    Kunkel, L.M.2
  • 14
    • 0030872016 scopus 로고    scopus 로고
    • Differential association of syntrophin pairs with the dystrophin complex
    • Peters, M. F., Adams, M. E. & Froehner, S. C. Differential association of syntrophin pairs with the dystrophin complex. J. Cell Biol. 138, 81-93 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 81-93
    • Peters, M.F.1    Adams, M.E.2    Froehner, S.C.3
  • 15
    • 0028972476 scopus 로고
    • Mouse α1- and β2-syntrophin gene structure, chromosome localization, and homology with a discs large domain
    • Adams, M. E., Dwyer, T. M., Dowler, L. L., White, R. A. & Froehner, S. C. Mouse α1- and β2-syntrophin gene structure, chromosome localization, and homology with a discs large domain. J. Biol.Chem. 270, 25859-25865 (1995).
    • (1995) J. Biol.chem. , vol.270 , pp. 25859-25865
    • Adams, M.E.1    Dwyer, T.M.2    Dowler, L.L.3    White, R.A.4    Froehner, S.C.5
  • 16
    • 0027360184 scopus 로고
    • A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette
    • Walden, P. D. & Cowan, N. J. A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette. Mol. Cell. Biol. 13, 7625-7635 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7625-7635
    • Walden, P.D.1    Cowan, N.J.2
  • 17
    • 0029858084 scopus 로고    scopus 로고
    • Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis
    • Walden, P. D. & Millette, C. F. Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis. Biol. Reprod. 55, 1039-1044 (1996).
    • (1996) Biol. Reprod. , vol.55 , pp. 1039-1044
    • Walden, P.D.1    Millette, C.F.2
  • 18
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang, Z. et al. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 275, 73-77 (1997).
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1
  • 20
    • 0026067790 scopus 로고
    • Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma
    • Ohlendieck, K., Ervasti, J. M., Snook, K. P. & Campbell, K. P. Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma. J. Cell Biol. 112, 135-148 (1991).
    • (1991) J. Cell Biol. , vol.112 , pp. 135-148
    • Ohlendieck, K.1    Ervasti, J.M.2    Snook, K.P.3    Campbell, K.P.4
  • 21
    • 0028211227 scopus 로고
    • Dystrophin and dystrophin-related protein in the brains of normal and mdx mice
    • Uchino, M. et al. Dystrophin and dystrophin-related protein in the brains of normal and mdx mice. Muscle Nerve 17, 533-538 (1994).
    • (1994) Muscle Nerve , vol.17 , pp. 533-538
    • Uchino, M.1
  • 22
    • 0029975426 scopus 로고    scopus 로고
    • Beta-dystroglycan: Subcellular localisation in rat brain and detection of a novel immunologically related, postsynaptic density-enriched protein
    • Mummery, R., Sessay, A., Lai, F. A. & Beesley, P. W. Beta-dystroglycan: subcellular localisation in rat brain and detection of a novel immunologically related, postsynaptic density-enriched protein. J. Neurochem. 66, 2455-2459 (1996).
    • (1996) J. Neurochem. , vol.66 , pp. 2455-2459
    • Mummery, R.1    Sessay, A.2    Lai, F.A.3    Beesley, P.W.4
  • 23
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho, K. O., Hunt, C. A. & Kennedy, M. B. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9, 929-942 (1992).
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 24
    • 0033066109 scopus 로고    scopus 로고
    • Characterization of dystrophin and utrophin diversity in the mouse
    • Lumeng, C. N. et al. Characterization of dystrophin and utrophin diversity in the mouse. Hum. Mol. Genet. 8, 593-599 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 593-599
    • Lumeng, C.N.1
  • 25
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains
    • Brenman, J. E. et al. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-Syntrophin mediated by PDZ domains. Cell 84, 757-767 (1996).
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1
  • 26
    • 0032522739 scopus 로고    scopus 로고
    • Two distantly positioned PDZ domains mediate multivalent INAD-phospholipase C interactions essential for G protein-coupled signaling
    • van Huizen, R. et al. Two distantly positioned PDZ domains mediate multivalent INAD-phospholipase C interactions essential for G protein-coupled signaling. EMBO J. 17, 2285-2297 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2285-2297
    • Van Huizen, R.1
  • 27
    • 0030848969 scopus 로고    scopus 로고
    • Utrophin-dystrophin-deficient mice as a model for Duchenne muscular dystrophy
    • Deconinck, A. E. et al. Utrophin-dystrophin-deficient mice as a model for Duchenne muscular dystrophy. Cell 90, 717-727 (1997).
    • (1997) Cell , vol.90 , pp. 717-727
    • Deconinck, A.E.1
  • 28
    • 0025275519 scopus 로고
    • Compartmentalization of cold-stable and acetylated microtubules in the subsynaptic domain of chick skeletal muscle fibre
    • Jasmin, B. J., Changeux, J. P. & Cartaud, J. Compartmentalization of cold-stable and acetylated microtubules in the subsynaptic domain of chick skeletal muscle fibre. Nature 344, 673-675 (1990).
    • (1990) Nature , vol.344 , pp. 673-675
    • Jasmin, B.J.1    Changeux, J.P.2    Cartaud, J.3
  • 29
    • 0027190703 scopus 로고
    • The distribution of dystrophin in the murine central nervous system: An immunocytochemical study
    • Lidov, H. G., Byers, T. J. & Kunkel, L. M. The distribution of dystrophin in the murine central nervous system: An immunocytochemical study. Neuroscience 54, 167-187 (1993).
    • (1993) Neuroscience , vol.54 , pp. 167-187
    • Lidov, H.G.1    Byers, T.J.2    Kunkel, L.M.3
  • 30
    • 0026474587 scopus 로고
    • Detection of dystrophin in the postsynaptic density of rat brain and deficiency in a mouse model of Duchenne muscular dystrophy
    • Kim, T., Wu, K., Xu, J. & Black, I. B. Detection of dystrophin in the postsynaptic density of rat brain and deficiency in a mouse model of Duchenne muscular dystrophy. Proc. Natl Acad. Sci. USA 89, 11642-11644 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11642-11644
    • Kim, T.1    Wu, K.2    Xu, J.3    Black, I.B.4
  • 31
    • 0031442806 scopus 로고    scopus 로고
    • Enlightening the postsynaptic density
    • Ziff, E. B. Enlightening the postsynaptic density. Neuron 19, 1163-1174 (1997).
    • (1997) Neuron , vol.19 , pp. 1163-1174
    • Ziff, E.B.1
  • 32
    • 0032520827 scopus 로고    scopus 로고
    • Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1
    • Lin, J. W. et al. Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1. J. Neurosci. 18, 2017-2027 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 2017-2027
    • Lin, J.W.1
  • 33
    • 0032055632 scopus 로고    scopus 로고
    • CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90
    • Niethammer, M. et al. CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90. Neuron 20, 693-707 (1998).
    • (1998) Neuron , vol.20 , pp. 693-707
    • Niethammer, M.1
  • 34
    • 17344367357 scopus 로고    scopus 로고
    • Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A
    • Brenman, J. F. et al. Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A. J. Neurosci. 18, 8805-8813 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 8805-8813
    • Brenman, J.F.1
  • 35
    • 0028998303 scopus 로고
    • The postsynaptic localization of the glycine receptor-associated protein gephyrin is regulated by the cytoskeleton
    • Kirsch, J. & Betz, H. The postsynaptic localization of the glycine receptor-associated protein gephyrin is regulated by the cytoskeleton. J. Neurosci. 15, 4148-4156 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 4148-4156
    • Kirsch, J.1    Betz, H.2
  • 36
    • 0028134623 scopus 로고
    • Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy
    • Cox, G. A., Sunada, Y., Campbell, K. P. & Chamberlain, J. S. Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy. Nat. Genet. 8, 333-339 (1994).
    • (1994) Nat. Genet. , vol.8 , pp. 333-339
    • Cox, G.A.1    Sunada, Y.2    Campbell, K.P.3    Chamberlain, J.S.4
  • 37
    • 0028261751 scopus 로고
    • Tyrosine and serine phosphorylation of dystrophin and the 58-kDa protein in the postsynaptic membrane of Torpedo electric organ
    • Wagner, K. R. & Huganir, R. L. Tyrosine and serine phosphorylation of dystrophin and the 58-kDa protein in the postsynaptic membrane of Torpedo electric organ. J. Neurochem. 62, 1947-1952 (1994).
    • (1994) J. Neurochem. , vol.62 , pp. 1947-1952
    • Wagner, K.R.1    Huganir, R.L.2
  • 38
    • 0027481757 scopus 로고
    • The 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin
    • Wagner, K. R., Cohen, J. B. & Huganir, R. L. The 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin. Neuron 10, 511-522 (1993).
    • (1993) Neuron , vol.10 , pp. 511-522
    • Wagner, K.R.1    Cohen, J.B.2    Huganir, R.L.3
  • 39
    • 0026022605 scopus 로고
    • IYES: A multifunctional cDNA expression vector for the isolation of genes by complementation of yeast and Escheria coli mutations
    • Elledge, S., Mulligan, J. T., Ramer, S. W., Spottswood, M. & Davis, R. W. IYES: A multifunctional cDNA expression vector for the isolation of genes by complementation of yeast and Escheria coli mutations. Proc. Natl. Acad. Sci. USA 88, 1731-1735 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1731-1735
    • Elledge, S.1    Mulligan, J.T.2    Ramer, S.W.3    Spottswood, M.4    Davis, R.W.5
  • 40
    • 0027251721 scopus 로고
    • The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit
    • Durfee, T. et al. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7, 555-569 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 555-569
    • Durfee, T.1
  • 41
    • 0029985652 scopus 로고    scopus 로고
    • Formation and activation by phosphorylation of activin receptor complexes
    • Willis, S. A., Zimmerman, C. M., Li, L. I. & Mathews, L. S. Formation and activation by phosphorylation of activin receptor complexes. Mol. Endocrinol. 10, 367-379 (1996).
    • (1996) Mol. Endocrinol. , vol.10 , pp. 367-379
    • Willis, S.A.1    Zimmerman, C.M.2    Li, L.I.3    Mathews, L.S.4
  • 42
    • 0030331567 scopus 로고    scopus 로고
    • Activin receptors: Cellular signalling by receptor serine kinases
    • Zimmerman, C. M. & Mathews, L. S. Activin receptors: cellular signalling by receptor serine kinases. Biochem. Soc. Symp. 62, 25-38 (1996).
    • (1996) Biochem. Soc. Symp. , vol.62 , pp. 25-38
    • Zimmerman, C.M.1    Mathews, L.S.2
  • 43
    • 0020509332 scopus 로고
    • A rapid procedure for preparing fluorescein-labeled specific antibodies from whole antiserum: Its use in analyzing cytoskeletal architecture
    • Talian, J. C., Olmsted, J. B. & Goldman, R. D. A rapid procedure for preparing fluorescein-labeled specific antibodies from whole antiserum: its use in analyzing cytoskeletal architecture. J. Cell Biol., 97, 1277-1282 (1983).
    • (1983) J. Cell Biol. , vol.97 , pp. 1277-1282
    • Talian, J.C.1    Olmsted, J.B.2    Goldman, R.D.3
  • 44
    • 0026355180 scopus 로고
    • Localization of the DMDL gene-encoded dystrophin-related protein using a panel of nineteen monoclonal antibodies: Presence at neuromuscular junctions, in the sarcolemma of dystrophic skeletal muscle, in vascular and other smooth muscles, and in proliferating brain cell lines
    • Thi Man, N. et al. Localization of the DMDL gene-encoded dystrophin-related protein using a panel of nineteen monoclonal antibodies: Presence at neuromuscular junctions, in the sarcolemma of dystrophic skeletal muscle, in vascular and other smooth muscles, and in proliferating brain cell lines. J. Cell Biol. 115, 1695-1700 (1991).
    • (1991) J. Cell Biol. , vol.115 , pp. 1695-1700
    • Thi Man, N.1
  • 45
    • 0029959354 scopus 로고    scopus 로고
    • Forced expression of dystrophin deletion constructs reveals structure-function correlations
    • Rafael, J. A. et al. Forced expression of dystrophin deletion constructs reveals structure-function correlations. J. Cell Biol. 134, 93-102 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 93-102
    • Rafael, J.A.1
  • 46
    • 0024416129 scopus 로고
    • Culture conditions affect the cholinergic development of an isolated subpopulation of chick mesencephalic neural crest cells
    • Barald, K. F. Culture conditions affect the cholinergic development of an isolated subpopulation of chick mesencephalic neural crest cells. Dev. Biol. 135, 349-366 (1989).
    • (1989) Dev. Biol. , vol.135 , pp. 349-366
    • Barald, K.F.1
  • 47
    • 0023034195 scopus 로고
    • Reversible assembly purification of microtubules without assembly-promoting agents and further purification of tubulin, microtubule-associated proteins, and MAP fragments
    • Vallee, R. B. Reversible assembly purification of microtubules without assembly-promoting agents and further purification of tubulin, microtubule-associated proteins, and MAP fragments. Methods Enzymol. 134, 89-104 (1986).
    • (1986) Methods Enzymol. , vol.134 , pp. 89-104
    • Vallee, R.B.1
  • 48
    • 0001643541 scopus 로고    scopus 로고
    • Crystal structure of a PDZ domain
    • Cabral, J. H. et al. Crystal structure of a PDZ domain. Nature 382, 649-652 (1996).
    • (1996) Nature , vol.382 , pp. 649-652
    • Cabral, J.H.1


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