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Volumn 146, Issue 2, 1999, Pages 465-475

ZASP: A new Z-band alternatively spliced PDZ-motif protein

Author keywords

Alternative splicing; Immunoelectron microscopy; Muscle proteins; Sarcomeres; Skeletal muscle

Indexed keywords

ALPHA ACTININ; CELL PROTEIN; DYSTROPHIN; MUSCLE PROTEIN; NITRIC OXIDE SYNTHASE; PROTEIN ZASP; SPECTRIN; SYNTROPHIN; UNCLASSIFIED DRUG;

EID: 0033606789     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.146.2.465     Document Type: Article
Times cited : (193)

References (39)
  • 1
    • 0027375539 scopus 로고
    • Two forms of mouse syntrophin, a 58-kd dystrophin-associated protein, differ in primary structure and tissue distribution
    • Adams, M.E., M.H. Butler, T.M. Dwyer, M.F. Peters, A.A. Murnane, and S.C. Froehner. 1993. Two forms of mouse syntrophin, a 58-kd dystrophin-associated protein, differ in primary structure and tissue distribution. Neuron. 11: 531-540.
    • (1993) Neuron. , vol.11 , pp. 531-540
    • Adams, M.E.1    Butler, M.H.2    Dwyer, T.M.3    Peters, M.F.4    Murnane, A.A.5    Froehner, S.C.6
  • 2
    • 0003225549 scopus 로고    scopus 로고
    • Transformation of Saccharomyces cerevisiae by the lithium acetate/single-stranded carrier DNA/polyethylene glycol protocol
    • 01525
    • Agatep, R., R.D. Kirkpatrick, D.L. Parchaliuk, R.A. Woods, and R.D. Gietz. 1998. Transformation of Saccharomyces cerevisiae by the lithium acetate/single-stranded carrier DNA/polyethylene glycol protocol. Technical Tips Online. (http://tto.biomednet.com) 01525.
    • (1998) Technical Tips Online
    • Agatep, R.1    Kirkpatrick, R.D.2    Parchaliuk, D.L.3    Woods, R.A.4    Gietz, R.D.5
  • 6
    • 0026786782 scopus 로고
    • Cloning and characterization of two human skeletal muscle α-actinin genes located on chromosomes 1 and 11
    • Beggs, A.H., T.J. Byers, J.H. Knoll, F.M. Boyce, G.A. Bruns, and L.M. Kunkel. 1992. Cloning and characterization of two human skeletal muscle α-actinin genes located on chromosomes 1 and 11. J. Biol. Chem. 267:9281-9288.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9281-9288
    • Beggs, A.H.1    Byers, T.J.2    Knoll, J.H.3    Boyce, F.M.4    Bruns, G.A.5    Kunkel, L.M.6
  • 8
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in duchenne muscular dystrophy
    • Brenman, J.E., D.S. Chao, H. Xia, K. Aldape, and D.S. Bredt. 1995. Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell. 82:743-752.
    • (1995) Cell , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.3    Aldape, K.4    Bredt, D.S.5
  • 10
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho, K.O., C.A. Hunt, and M.B. Kennedy. 1992. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron. 9:929-942.
    • (1992) Neuron. , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 11
    • 0031916105 scopus 로고    scopus 로고
    • PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL
    • Cuppen, E., H. Gerrits, B. Pepers, B. Wieringa, and W. Hendriks. 1998. PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL. Mol. Biol. Cell. 9:671-683.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 671-683
    • Cuppen, E.1    Gerrits, H.2    Pepers, B.3    Wieringa, B.4    Hendriks, W.5
  • 13
    • 0032580809 scopus 로고    scopus 로고
    • The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • Ishikawa, K., T. Nagase, M. Suyama, N. Miyajima, A. Tanaka, H. Kotani, N. Nomura, and O. Ohara. 1998. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 5:169-176.
    • (1998) DNA Res. , vol.5 , pp. 169-176
    • Ishikawa, K.1    Nagase, T.2    Suyama, M.3    Miyajima, N.4    Tanaka, A.5    Kotani, H.6    Nomura, N.7    Ohara, O.8
  • 14
    • 0029374716 scopus 로고
    • Origin of PDZ (DHR, GLGF) domains
    • Kennedy, M.B. 1995. Origin of PDZ (DHR, GLGF) domains. Trends Biochem. Sci. 21:350.
    • (1995) Trends Biochem. Sci. , vol.21 , pp. 350
    • Kennedy, M.B.1
  • 15
    • 0028882810 scopus 로고
    • + channels by direct interaction with the PSD-95/ SAP90 family of membrane-associated guanylate kinases
    • + channels by direct interaction with the PSD-95/ SAP90 family of membrane-associated guanylate kinases. Nature. 378:85-88.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5
  • 16
    • 0029098659 scopus 로고
    • Domain interactions between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.-C., L.T. Schenker, M.B. Kennedy, and P.H. Seeburg. 1995. Domain interactions between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science. 269:1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.-C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 17
    • 0030744829 scopus 로고    scopus 로고
    • Interaction of ion channels and receptors with PDZ domains
    • Kornau, H.-C., P.H. Seeburg, and M.B. Kennedy. 1997. Interaction of ion channels and receptors with PDZ domains. Curr. Opin. Neurobiol. 7:368-373.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 368-373
    • Kornau, H.-C.1    Seeburg, P.H.2    Kennedy, M.B.3
  • 18
    • 0029869649 scopus 로고    scopus 로고
    • Identification of 4,370 expressed sequence tags from a 3′-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization
    • Lanfranchi, G., T. Muraro, F. Caldara, B. Pacchioni, A. Pallavicini, D. Pandolfo, S. Toppo, S. Trevisan, S. Scarso, and G. Valle. 1996. Identification of 4,370 expressed sequence tags from a 3′-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization. Genome Res. 6:35-42.
    • (1996) Genome Res. , vol.6 , pp. 35-42
    • Lanfranchi, G.1    Muraro, T.2    Caldara, F.3    Pacchioni, B.4    Pallavicini, A.5    Pandolfo, D.6    Toppo, S.7    Trevisan, S.8    Scarso, S.9    Valle, G.10
  • 20
    • 0032557642 scopus 로고    scopus 로고
    • Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin
    • Mues, A., P.F.M. van der Ven, P. Young, P.D.O. Fürst, and M. Gautel. 1998. Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin. FEBS Lett. 428:111-114.
    • (1998) FEBS Lett. , vol.428 , pp. 111-114
    • Mues, A.1    Van Der Ven, P.F.M.2    Young, P.3    Fürst, P.D.O.4    Gautel, M.5
  • 21
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai, K., and M. Kanehisa. 1992. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics. 14:897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 22
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • Niethammer, M., E. Kim, and M. Sheng. 1996. Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci. 16:2157-2163.
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 23
    • 0031560933 scopus 로고    scopus 로고
    • The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of α-actinin
    • Ohtsuka, H., H. Yajima, K. Maruyama, and S. Kimura. 1997. The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of α-actinin. Biochem. Biophys. Res. Commun. 235:1-3.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 1-3
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 24
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and D.J. Lipman. 1988. Improved tools for biological sequence comparison. Proc Natl. Acad. Sci. USA. 85:2444-2448.
    • (1988) Proc Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 25
    • 0019856283 scopus 로고
    • Cytoplasmic contractile proteins
    • Pollard, T. 1981. Cytoplasmic contractile proteins. J. Cell Biol. 91:156s-165s.
    • (1981) J. Cell Biol. , vol.91
    • Pollard, T.1
  • 26
    • 0028902098 scopus 로고
    • Dhr domains in syntrophins, neuronal NO synthase and other intracellular proteins
    • Ponting, C.P., and C. Phillips. 1995. DHR domains in syntrophins, neuronal NO synthase and other intracellular proteins. Trends Biol. Sci. 20:102-103.
    • (1995) Trends Biol. Sci. , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.2
  • 27
    • 0028158628 scopus 로고
    • PHD: An automatic mail server for protein secondary structure prediction
    • Rost, B., C. Sander, and R. Schneider. 1994. PHD: an automatic mail server for protein secondary structure prediction. CABIOS. 10:53-60.
    • (1994) CABIOS , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 28
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with FAS
    • Sato, T., S. Irie, S. Kitada, and J.C. Reed. 1995. FAP-1: a protein tyrosine phosphatase that associates with FAS. Science. 268:411-415.
    • (1995) Science , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 29
    • 0030995719 scopus 로고    scopus 로고
    • The neuronal nitric oxide synthase PDZ motif binds to -G(D < E)XV* carboxy-terminal sequences
    • Schepens, J., E. Cuppen, B. Wieringa, and W. Hendricks. 1997. The neuronal nitric oxide synthase PDZ motif binds to -G(D < E)XV* carboxy-terminal sequences. FEBS Lett. 409:53-56.
    • (1997) FEBS Lett. , vol.409 , pp. 53-56
    • Schepens, J.1    Cuppen, E.2    Wieringa, B.3    Hendricks, W.4
  • 30
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., F. Milpetz, P. Bork, and C.P. Ponting. 1998. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA. 95:5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 31
    • 0030273003 scopus 로고    scopus 로고
    • PDZs and receptor/channel clustering: Rounding up the latest suspects
    • Sheng, M. 1996. PDZs and receptor/channel clustering: rounding up the latest suspects. Neuron. 17:575-578.
    • (1996) Neuron. , vol.17 , pp. 575-578
    • Sheng, M.1
  • 32
    • 0029664550 scopus 로고    scopus 로고
    • 2+ channel by INAD in Drosophila photoreceptors
    • 2+ channel by INAD in Drosophila photoreceptors. Neuron. 16:991-998.
    • (1996) Neuron. , vol.16 , pp. 991-998
    • Shieh, B.-H.1    Zhu, M.Y.2
  • 37
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods, D.F., and P.J. Bryant. 1991. The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell. 66:451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Bryant, P.J.2
  • 38
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: Identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • Xia, H., S.T. Winnnokur, W.-L. Kuo, M.R. Altherr, and D.S. Bredt. 1997. Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs. J. Cell Biol. 139:507-515.
    • (1997) J. Cell Biol. , vol.139 , pp. 507-515
    • Xia, H.1    Winnnokur, S.T.2    Kuo, W.-L.3    Altherr, M.R.4    Bredt, D.S.5
  • 39
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • Young, P., C. Ferguson, S. Bañuelos, and M. Gautel. 1998. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EMBO (Eur. Mol. Biol. Organ.) J. 17:1614-1624.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Bañuelos, S.3    Gautel, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.