The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers

Journal of Cell Science

Volumn 109, Issue 11, 1996, Pages 2747-2754

  Gautel, Mathias ^a   Goulding, David ^a   Bullard, Belinda ^a   Weber, Klaus ^b   Fürst, Dieter O ^c  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^c UNIVERSITY OF POTSDAM   (Germany)

Author keywords

Connectin; Isoform; Phosphorylation; Sarcomere; Titin; Z disk

Indexed keywords

CONNECTIN; FIBRONECTIN; IMMUNOGLOBULIN; MUSCLE PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CELL ULTRASTRUCTURE; HEART MUSCLE; IMMUNOELECTRON MICROSCOPY; MOUSE; NEWBORN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; SARCOMERE; SKELETAL MUSCLE;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; DNA, COMPLEMENTARY; EPITOPE MAPPING; GENE DOSAGE; HUMANS; MICE; MICE, INBRED BALB C; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; PROLINE; PROTEIN KINASES; RABBITS; REPETITIVE SEQUENCES, NUCLEIC ACID; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; VARIATION (GENETICS);

ANIMALIA;

EID: 0029859276     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (44)

1. Astier, C., Labbé, J.-P., Roustan, C. and Benjamin. Y. (1993). Effects of different enzymatic treatments on the release of titin fragments from rabbit skeletal myofibrils. Biochem. J. 290, 731-734.
2. 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.
3. Debus, E., Weber, K. and Osborn, M. (1983). Monoclonal antibodies to desmin, the muscle-specific intermediate filament protein. EMBO J. 2, 2305-2312.
4. Devereux, J., Haeberli, P. and Smithies O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids Res. 12, 387-395.
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 filaments 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 and the involvement of titin in myofibril assembly. J. Cell Biol. 109, 517-527.
8. Fürst, D. O. and Gautel, M. (1995). The anatomy of a molecular giant: how the sarcomeric cytoskeleton is assembled from molecules of the immunoglobulin superfamily. J. Mol. Cell. Cardiol. 27, 951-959.
9. 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
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). Monoclonal antibodies. Antibodies: A Laboratory Manual, pp. 174-238. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
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. Labeit, S. and Kolmerer, B. (1995). The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol. 248, 308-315.
16. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
17. 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. Cytoskel. 29, 1-19.
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. Moncman, C. L. and Wang, K. (1995). Nebulette: a 107 kD nebulin-like protein in cardiac muscle. Cell Motil. Cytoskel. 32, 205-225.
22. Pfuhl, M. and Pastore, A. (1995). Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the I-set. Structure 3, 391-401.
23. Politou, A., Gautel, M., Pfuhl, M., Labeit, S. and Pastore, A. (1994a). Immunoglobulin-type domains of titin: same fold, different stability? Biochemistry 33, 4730-4737.
24. Politou, A., Gautel, M., Joseph, C. and Pastore, A. (1994b). Immunoglobulin domains of titin are stabilized by N-terminal extension. FEBS Lett. 352, 27-31.
25. Politou, A. S., Gautel, M., Improta, S., Vangelisia, L. and Pastore, A. (1996). The elastic I-band region of titin is assembled in a 'modular' fashion by weakly interacting Ig-like domains. J. Mol. Biol. 255, 604-616.
26. 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.
27. Sebestyén, 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.
28. 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. Curr. Biol. 4, 973-982.
29. Soteriou, A., Gamage, M. and Trinick, J. (1993). A survey of interactions made by the giant protein titin. J. Cell Sci. 104, 119-123.
30. Squire, J. (1981). Structure of the Z-band. The Structural Basis of Muscular Contraction. pp. 364-375. Plenum Press, New York and London.
31. 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.
32. Tokayasu K. T. (1973). A technique for ultracryotomy of cell suspensions and tissues. J. Cell Biol. 57, 551-565.
33. 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.
34. 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.
35. Thompson, 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. Nucl. Acids Res. 22, 4673-4680.
36. Vigoreaux, J. O. (1994). The muscle Z-band: lessons in stress management. J. Muscle Res. Cell Motil. 15, 237-255.
37. van der Loop, F. T. L., van der Ven, P. F. M., Fürst, D. O., Gautel, M., van Eys, G. J. J. M. and Ramaekers, F. C. S. (1996). Integration of titin into the sarcomeres of cultured differentiating human skeletal muscle cells. Eur. J. Cell Biol. 69, 301-307
38. Wang, K., McClure, J. and Tu, A. (1979). Titin: major myofibrillar components of striated muscle. Proc. Nat. Acad. Sci. USA 76, 3698-3702.
39. 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.
40. 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.
41. Wang, S.-M. and Jeng, C.-J. (1992). Interaction between titin and α-actinin. Biomed. Res. 13, 197-202.
42. 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.
43. Whiting, A., Wardale, J. and Trinick, J. (1989). Does titin regulate the length of muscle thick filaments? J. Mol. Biol. 205, 263-268.
44. 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.