Constitutive and variable regions of Z-disk titin/connectin in myofibril formation: A dominant-negative screen

Cell Structure and Function

Volumn 22, Issue 1, 1997, Pages 95-101

  Peckham, Michelle ^b   Young, Paul ^a   Gautel, Mathias ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

Isoforms; Sarcomere assembly; Titin connectin; Z disk

Indexed keywords

CONNECTIN;

ANIMAL TISSUE; CONFERENCE PAPER; GENETIC TRANSFECTION; MUSCLE; MUSCLE DEVELOPMENT; MUSCLE FIBRIL; NONHUMAN; PRIORITY JOURNAL; SARCOMERE;

ANIMALIA; GALLUS GALLUS;

EID: 0030913881     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.22.95     Document Type: Conference Paper

References (40)

1. ANDERSSON, S., DAVIS, D.N., DAHLBÄCK, H., JÖRNVALL, H., and RUSSELL, D.W. 1989. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-Hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem., 264: 8222-8229.
2. ASTIER, C., LABBÉ, J.-P., ROUSTAN, C., and BENYAMIN, Y. 1993. Effects of different enzymatic treatments on the release of titin fragments from rabbit skeletal myofibrils. Biochem. J., 290: 731-734.
3. BENNETT, P.M. and GAUTEL, M. 1996. Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament. J. Mol. Biol., 259: 896-903.
4. CHURCH, G.M. and GILBERT, W. 1984. Genomic sequencing. Proc. Natl. Acad. Sci. USA, 81: 1991-1995.
5. FREIBURG, A. and GAUTEL, M. 1995. A molecular map of the interactions of titin and myosin-binding protein C: implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem., 235: 317-323.
6. FÜRST, D.O., OSBORN, M., NAVE, R., and WEBER, K. 1988. The organization of titin in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M-line. J. Cell Biol., 106: 1563-1572.
7. FÜRST, D.O., OSBORN, M., and WEBER, K. 1989. Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins the involvement of titin in myofibril assembly. J. Cell Biol., 109: 517-527.
8. GAUTEL, M., LEONARD, K., and LABEIT, S. 1993. Phosphorylation of KSP-motifs in the C-terminal region of titin in differentiating myoblasts. EMBO J., 12: 3827-3834.
9. GAUTEL, M., GOULDING, B., BULLARD, B., WEBER, K., and FÜRST, D.O. 1996. The central Z-disk region of titin is assembled form a novel repeat in variable copy numbers. J. Cell Sci., 109: 2747-2754.
10. HANDEL, S.E., WANG, S.-M., GREASER, M.L., SCHULTZ, E., BULINSKI, J.C., and LESSARD, J.L. 1989. Skeletal muscle myofibrillogenesis as revealed with a monoclonal antibody to titin in combination with detection of the α-and γ-isoforms of actin. Dev. Biol., 132: 35-44.
11. HARLOW, E. and LANE, D. 1988. Antibodies - a laboratory manual. pp 174-238. Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
12. ITOH, Y., SUZUKI, T., KIMURA, S., OHASHI, K., HIGUSHI, H., SAWADA, H., SHIMIZU, T., SHIBATA, M., and MARUYAMA, K. 1988. Extensible and less extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectronmicroscopy using monoclonal antibodies. J. Biochem., 104: 504-508.
13. LABEIT, S., GAUTEL, M., LAKEY, A., and TRINICK, J. 1992. Towards a molecular understanding of titin. EMBO J., 11: 1711-1716.
14. LABEIT, S. and KOLMERER, B. 1995. Titins, giant molecules in charge of muscle ultrastructure and elasticity. Science, 270: 293-296.
15. LAEMMLI, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
16. LIN, Z., LU, M.H., SCHULTHEISS, T., CHOI, J., HOLTZER, S., DILULLO, C., FISCHMAN, D.A., and HOLTZER, H. 1994. Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: evidence for a conserved myoblast differentiation program in skeletal muscle. Cell Motil. Cytoskeleton, 29: 1-19.
17. MARUYAMA, K. 1976. Connectin, an elastic protein from myofibrils. J. Biochem., 80: 405-407.
18. MARUYAMA, K., NATORI, R., and NONOMURA, Y. 1976. New elastic protein from muscle. Nature, 262: 58-59.
19. MARUYAMA, K., MATSUBARA, S., NATORI, R., NONOMURA, Y., KIMURA, S., OHASHI, K., MURAKAMI, F., HANDA, S., and EGUCHI, G. 1977. Connectin, an elastic protein of muscle: characterization and function. J. Biochem., 82: 317-337.
20. MARUYAMA, K., KIMURA, S., YAMAMOTO, K., WAKABAYASHI, T., and SUZUKI, T. 1985. Connectin causes aggregation of myosin rods but not myosin heads. Biomed. Res., 6: 423-427.
21. MORGAN, J.E., BEAUCHAMP, J.R., PAGEL, C.N., PECKHAM, M., ATALIOTIS, P., JAT, P.S., NOBLE, M.D., FARMER, K., and PARTRIDGE, T.A. 1994. Myogenic cell lines derived from transgenic mice carrying a thermolabile T-antigen: a model system for derivation of tissue specific and mutation specific cell lines. Dev. Biol., 162: 486-498.
22. OBERMANN, W.M.J., PLESSMANN, U., WEBER, K., and FÜRST, D.O. 1995. Purification and biochemical characterization of myomesin, a myosin-binding and titin-binding protein, from bovine skeletal muscle. Eur. J. Biochem., 233: 110-115.
23. SAIKI, R.K., SCHARF, S.J., FALOONA, F., MULLIS, G.T., and ERLICH, H.A. 1985. Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science, 230: 1350-1354.
24. SEBESTYEN, M.G., WOLFF, J.A., and GREASER, M.L. 1995. Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases. J. Cell Sci., 108: 3029-3027.
25. SONGYANG, Z., BLECHNER, S., HOAGLAND, N., HOEKSTRA, M.F., PIWNICA-WORMS, H., and CANTLEY, L.C. 1994. Use of an oriented peptide library to determine the optimal substrates of protein kinases. Current Biology, 4: 973-982.
26. SQUIRE, J. 1981. The Structural Basis of Muscular Contraction, Plenum Press, New York and London, pp. 364-375.
27. TANABE, R., TATSUMI, R., and TAKAHASHI, K. 1994. Purification and characterization of the 1200-kDa subfragment of connectin filaments produced by 0.1 mM calcium ions. J. Biochem., 115: 351-355.
28. TOKAYASU, K.T. and MAHER, P.A. 1987a. Immunocytochemical studies of cardiac myofibrillogenesis in early chick embryos. I. Presence of immunofluorescent titin spots in premyofibril stages. J. Cell Biol., 105: 2781-2793.
29. TOKAYASU, K.T. and MAHER, P.A. 1987b. Immunocytochemical studies of cardiac myofibrillogenesis in early chick embryos. II. Generation of α-actinin dots within titin spots at the time of the first myofibril formation. J. Cell Biol., 105: 2781-2793.
30. THOMPSOM, J.D., HIGGINS, D.G., and GIBSON, T.J. 1994. CLUSTAL-W: improving the sensitivity of progressive, multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22: 4673-4680.
31. VIGOREAUX, J.O. 1994. The muscle Z-band: lessons in stress management. J. Muscle Res. Cell Motil., 15: 237-255.
32. VON ARX, P., BANTLE, S., SOLDATI, T., and PERRIARD, J.-C. 1995. Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function. J. Cell Biol., 131: 1759-1773.
33. WANG, K., MCCLURE, J., and TU, A. 1979. Titin: major myofibrillar components of striated muscle. Proc. Natl. Acad. Sci., USA, 76: 3698-3702.
34. WANG, K. and WRIGHT, J. 1988. Architecture of the sarcomeric matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol., 107: 2199-2212.
35. WANG, K., MCCARTER, R., WRIGHT, J., BEVERLY, J., and RAMIREZ-MITCHELL, R. 1993. Viscoelasticity of the sarcomere matrix of skeletal muscle - the titin-myosin composite filament is a dual stage molecular spring. Biophys. J., 64: 1161-1177.
36. WANG, S.-M. and JENG, C.-J. 1992. Interaction between titin and α-actinin. Biomed. Res., 13: 197-202.
37. WANG, S.-M., GREASER, M.L., SCHULTZ, E., BULINSKI, J.C., LIN, J.J.-C., and LESSARD, J.L. 1988. Studies on cardiac myofibrillogenesis with antibodies to titin, actin, tropomosin, and myosin. J. Cell Biol., 107: 1075-1083.
38. WHITING, A., WARDALE, J., and TRINICK, J. 1989. Does titin regulate the length of muscle thick filaments? J. Mol. Biol., 205: 263-268.
39. YAJIMA, H., OHTSUKA, H., KAWAMURA, Y., KUME, H., MURAYAMA, T., ABE, H., KIMURA, S., and MARUYAMA, K. 1996. A 11.5-kb 5′-terminal cDNA sequence of chicken connectin/titin reveals its Z line binding region. Biochem. Biophys. Res. Commun., 223: 160-164.
40. YAMAGUCHI, M., IZUMIMOTO, M., ROBSON, R.M., and STROMER, M.H. 1985. Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture. J. Mol. Biol., 184: 621-644.