Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament

Journal of Molecular Biology

Volumn 259, Issue 5, 1996, Pages 896-903

  Bennett, Pauline M ^a   Gautel, Mathias ^b  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Myosin; Sarcomeric assembly; Titin connectin

Indexed keywords

ANTIBODY; CONNECTIN; FIBRONECTIN; MYOSIN;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HUMAN; MYOFILAMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; SKELETAL MUSCLE;

EID: 0030604697     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0367     Document Type: Editorial

References (41)

1. Aarli, J. A., Stefansson, K., Marton, L. S. G. & Wollmann, R. L. (1990). Patients with myasthenia gravis and thymoma have in their sera IgG autoantibodies against titin. Clin. Expt. Immunol. 82, 284-288.
2. Craig, R. (1977). Structure of A-segments from frog and rabbit skeletal muscle. J. Mol. Biol. 109, 69-81.
3. Craig, R. & Offer, G. (1976). Axial arrangement of crossbridges in thick filaments of vertebrate skeletal muscle. J. Mol. Biol. 102, 325-332.
4. Fürst, D. O. & 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.
5. Fürst, D. O., Osborn, M., Nave, R. & 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.
6. Gautel, M., Lakey, A., Barlow, D. P., Holmes, Z., Scales, S., Leonard, K., Labeit, S., Mygland, A., Gilhus, S. & Aarli, J. A. (1993). Titin antibodies in myasthenia gravis: identification of a major autogenic region of titin. Neurology, 43, 1581-1585.
7. Harlow, E. & Lane, D. (1988). In Antibodies - a Laboratory Manual, pp. 174-238, Cold Spring Harbor Laboratory Press, Cold Spring Habor, NY.
8. Hawkins, C. J. & Bennett, P. M. (1995). Evaluation of freeze substitution in rabbit skeletal muscle. Comparison of electron microscopy to X-ray diffraction. J. Musc. Res. Cell. Motil. 16, 303-318.
9. Houmeida, A., Holt, J., Tskhovrebova, L. & Trinick, J. (1995). Studies of the interaction between titin and myosin. J. Cell Biol. 131, 1471-1481.
10. Itoh, Y., Suzuki, T., Kimura, S., Ohashi, K., Higushi, H., Sawada, H., Shimizu, T., Shibata, M. & Maruyama, K. (1988). Extensible and less extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. 104, 504-508.
11. Keller, C. S. (1995). Structure and function of titin and nebulin. Curr. Opin. Cell Biol. 7, 32-38.
12. Knight, P. K. & Trinick, J. A. (1982). Preparation of myofibrils. Methods Enzymol. 85B, 9-12.
13. Kurzban, G. P. & Wang, K. (1988). Giant polypeptides of skeletal muscle titin: sedimentation equilibrium in guanidine hydrochloride. Biochem. Biophys. Res. Commun. 150, 1155-1161.
14. Labeit, S. & Kolmerer, B. (1995). Titins, giant molecules in charge of muscle ultrastructure and elasticity. Science, 270, 293-296.
15. Labeit, S., Barlow, D. P., Gautel, M., Gibson, T., Hsieh, C.-L., Francke, U., Leonard, K., Wardale, J., Whiting, A. & Trinick, J. (1990). A regular pattern of two types of 100 residue motifs in the sequence of titin. Nature, 345, 273-276.
16. Labeit, S., Gautel, M., Lakey, A. & Trinick, J. (1992). Towards a molecular understanding of titin. EMBO J. 11, 1711-1716.
17. Maruyama, K. (1976). Connectin, an elastic protein from myofibrils. J. Biochem. 80, 405-407.
18. Maruyama, K. (1994). Connectin, an elastic protein of striated muscle. Biophys. Chem. 50, 73-85.
19. Maruyama, K., Natori, R. & Nonomura, Y. (1976). New elastic protein from muscle. Nature, 262, 58-59.
20. Maruyama, K., Matsubara, S., Natori, R., Nonomura, Y., Kimura, S., Ohashi, K., Murakami, F., Handa, S. & Eguchi, G. (1977). Connectin, an elastic protein of muscle: characterization and function. J. Biochem. 82, 317-337.
21. Maruyama, K., Kimura, S., Yoshidomi, H., Sawada, H. & Kikuchi, M. (1984). Molecular size and shape of β-connectin, an elastic protein of striated muscle. J. Biochem. 95, 1423-1493.
22. Maruyama, K., Yoshioka, T., Higuchi, H., Ohashi, K., Kimura, S. & Natori, R. (1985a). Connectin filaments link thick filaments and Z-lines in frog skeletal muscle as revealed by immunoelectron microscopy. J. Cell Biol. 101, 2167-2172.
23. Maruyama, K., Kimura, S., Yamamoto, K., Wakabayashi, T. & Suzuki, T. (1985b). Connectin causes aggregation of myosin rods but not myosin heads. Biomed. Res. 6, 423-427.
24. Maw, M. C. & Rowe, A. J. (1986). The reconstruction of myosin filaments in rabbit psoas muscle from solubilized myosin. J. Musc. Res. Cell Motil. 7, 97-109.
25. Moos, C., Offer, G., Starr, R. & Bennett, P. (1975). Interaction of C-protein with myosin, myosin rod and light meromyosin. J. Mol. Biol. 97, 1-9.
26. Nave, R., Fürst, D. O. & Weber, K. (1989). Visualization of the polarity of isolated titin molecules: a single globular head on a long thin rod as the M-band anchoring domain? J. Cell Biol. 109, 2177-2187.
27. Pfuhl, M. & 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.
28. Politou, A., Gautel, M., Pfuhl, M., Labeit, S. & Pasture, A. (1994a). Immunoglobulin-type domains of titin: same fold, different stability? Biochemistry, 33, 4730-4737.
29. Politou, A., Gautel, M., Joseph, C. & Pasture, A. (1994b). Immunoglobulin domains of titin are stabilized by N-terminal extension, FEBS Letters, 352, 27-31.
30. Politou, A., Gautel, M., Improta, S., Vangelista, L. & Pasture, 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.
31. Saiki, R. K., Scharf, S. J., Faloona, F., Mullis, G. T. & 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.
32. Sjöström, M. & Squire, J. M. (1977). Fine structure of the A-band in cryo-sections: the structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J. Mol. Biol. 109, 49-68.
33. Soteriou, A., Gamage, M. & Trinick, J. (1993). A survey of interactions made by the giant muscle protein titin. J. Cell Sci. 104, 119-123.
34. Trinick, J. (1994). Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci. 19, 405-409.
35. Trinick, J., Knight, P. & Whiting, A. (1984). Purification and properties of native titin. J. Mol. Biol. 180, 331-356.
36. Trombitás, K., Baatsen, P. H. W. W., Kellermayer, M. S. Z. & Pollack, G. H. (1991). Nature and origin of gap filaments in striated muscle. J. Cell Sci. 100, 809-814.
37. Wang, K. & 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.
38. Wang, K., McClure, J. & Tu, A. (1979). Titin: major myofibrillar components of striated muscle. Proc. Natl Acad. Sci. USA, 76, 3698-3702.
39. Wang, S.-M., Jeng, C. J. & Sun, M. C. (1992). Studies on the interaction between titin and myosin. Histol. Histopathol. 7, 333-337.
40. Whiting, A., Wardale, J. & Trinick, J. (1989). Does titin regulate the length of thick filaments? J. Mol. Biol. 205, 163-169.
41. Yagi, N. (1992). Effects of N-ethylmaleimide on the structure of skinned frog skeletal muscles. J. Musc. Res. Cell Motil. 13, 457-463.