Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band

Molecular Biology of the Cell

Volumn 9, Issue 4, 1998, Pages 829-840

  Obermann, Wolfgang M J ^a   Van Der Ven, Peter P M ^a,b   Steiner, Frank ^a   Weber, Klaus ^a   Fürst, Dieter O ^b  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b UNIVERSITY OF POTSDAM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; M PROTEIN; MEROMYOSIN; MYOSIN; STRUCTURAL PROTEIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING SITE; CATTLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; SARCOMERE;

EID: 0031897698     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.4.829     Document Type: Article

References (41)

1. Andersson, S., Davis, D.N., Dahlbäck, H., Jörnval, H., and Russel D.W. (1989) Cloning, structure and expression of the mitochondnal cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264, 8222-8229.
2. Ausubel, P.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. (1995). Short Protocols in Molecular Biology, 3rd ed., New York: Wiley and Sons, Inc.
3. Bähler, M., Wallimann T., and Eppenberger, H.M. (1985). Myofibrillar M-band proteins represent constituents of native thick filaments, frayed filaments and bare zone assemblages. J. Muscle Res. Cell Motil. 6, 783-800.
4. Carlsson, E., Grove, B.K., Wallimann, T., Eppenberger, H.M., and Thornell, L.-E. (1990). Myofibrillar M-band proteins in rat skeletal muscles during development. Histochemistry 95, 27-35.
5. Casnellie, J.E. (1991). Assay of protein kinases using peptides with basic residues for phosphocellulose binding. Methods Enzymol. 200, 115-120.
6. Freiburg, A., and Gautel, M. (1996). 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.
7. 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 non-repetitive epitopes starting at the Z line extends close to the M line. J. Cell Biol. 106, 1563-1572.
8. Fürst, D.O., Osborn, M., and K. Weber. (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.
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. Grove, B.K., Cerny, L., J.-Perriard, C., and Eppenberger, H.M. (1985). Myomesin and M-protein: Expression of two M-band proteins in pectoral muscle and heart during development. J. Cell Biol. 101, 1413-1421.
11. Grove, B.K., Holmbom, B., and L.-Thornell, E. (1987). Myomesin and M protein: differential expression in embryonic fibers during pectoral muscle development. Differentiation 34, 106-114.
12. Grove, B.K., Kurer, V., Lehner, C., Doetschmann, T.C., Perriard, J.-C., and Eppenberger, H.M. (1984). A new 185,000-dalton skeletal muscle protein detected by monoclonal antibodies. J. Cell Biol. 98, 518-524.
13. Kemp, B.E., Graves, D.J., Benjamini, E., and Krebs, E.G. (1977). Role of multiple basic residues in determining the substrate specifity of cyclic AMP-dependent protein kinase. J. Biol. Chem. 251, 4888-4894.
14. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
15. Luther, P.K., and Squire, J.M. (1978). Three -dimensional structure of the vertebrate muscle M-region. J. Mol. Biol. 125, 313-324.
16. Lutz-Freyermuth, C., Query, C.C., and Keene, J.D. (1990). Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA. Proc. Natl. Acad. Sci. USA 87, 6393-6397.
17. Maeda, K., Sczakiel, G., and Wittinghofer, A. (1987). Characterization of cDNA coding for the complete light meromyosin portion of a rabbit fast skeletal muscle myosin heavy chain. Eur. J. Biochem. 167, 97-102.
18. Mani, R.S., and Kay, C.M. (1978). Interaction studies of the 165,000 dalton protein component of the M-line with the S2 subfragment of myosin. Biochim. Biophys. Acta 536, 134-141.
19. Masaki, T., and Takaiti, O. (1974). M-protein. J. Biochem. 75, 367-380.
20. Nave, R., Fürst, D.O., and 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, 2177-2188.
21. Noguchi, J., Yanagisawa, M., Imamura, M., Kasuya, Y., Sakurai, T., Tanaka, T., and Masaki, T. (1992). Complete primary structure and tissue expression of chicken pectoralis M-protein. J. Biol. Chem. 267, 20302-20310.
22. Obermann, W., Plessmann, U., Weber, K., and Fürst, D.O. (1995). Purification and biochemical characterization of myomesin, a myosin and titin binding protein, from bovine skeletal muscle. Eur. J. Biochem. 233, 110-115.
23. Obermann, W.M.J., Gautel, M., Steiner, F., Van der Ven, P.F.M., Weber, K., and Fürst, D.O. (1996). The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein and the 250 kDa carboxyterminal region of titin by immunoelectron microscopy. J. Cell Biol. 134, 1441-1453.
24. Obermann, W.M.J., Gautel, M., Weber, K., and Fürst, D.O. (1997). Molecular structure of the sarcomeric M band: mapping of titin- and myosin-binding domains of myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO J. 26, 211-220.
25. Pearson, R.B., and Kemp, B.E. (1991). Protein kinase phosphorylation site sequences and consensus specifity motifs: tabulations. Methods Enzymol. 201, 62-81.
26. Perriard, J.-C. (1993). Myomesin and M-protein. In Guidebook to the Cytoskeletal and Motor Proteins, ed. T. Kreis and R. Vale, Oxford, England: Oxford University Press, 58-59.
27. Saiki, R.K., Scharf, S.J., Faloona, F., Mullis, G.T., and Ehrlich, H.A. (1985). Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science 230, 1350-1354.
28. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
29. Schaart, G., Pieper, F.R., Kuijpers, H.J.H., Bloemendal, H., and Ramaekers, F.C.S. (1991). Baby hamster kidney (BHK-21/C13) cells can express striated muscle type proteins. Differentiation 46, 105-115.
30. Small, J.V., Fürst, D.O., and Thornell, L.-E. (1992). The cytoskeletal lattice of muscle cells. Eur. J. Biochem. 208, 559-572.
31. Studier, F.W., Rosenberg, A.H., Dunn, J.J., and Dubendorff, J.W. (1990). Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
32. Tsai, D.E., Kenan, D.J., and Keene, J.D. (1992). In vitro selection of an RNA epitope immunologically cross-reactive with a peptide. Proc. Natl. Acad. Sci. USA 89, 8864.
33. 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.
34. Van der Ven, P.F.M., Schaart, G., Croes, H.J.E., Jap, P.H.K., Ginsel, L.A., and Ramaekers, F.C.S. (1993). Titin aggregates associated with intermediate filaments align along stress fiber-like structures during human skeletal muscle cell differentiation. J. Cell Sci. 106, 749-759.
35. Vinkemeier, U., Obermann, W., Weber, K., and Fürst, D.O. (1993). The globular head domain of titin extends into the center of the sarcomeric M band. J. Cell Sci. 106, 319-330.
36. Wallimann, T., Doetschman, T.C., and Eppenberger, H.M. (1983). Novel staining pattern of skeletal muscle M-lines upon incubation with antibodies against MM-creatine kinase. J. Cell Biol. 96, 1772-1779.
37. Wallimann, T., and Eppenberger, H.M. (1985). Localization and function of M-line-bound creatine kinase. Cell Muscle Motil. 6, 239-285.
38. Wang, S.M., and Greaser, M.L. (1985). Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils. J. Muscle Res. Cell Motil. 6, 293-312.
39. Wehland, J., Schröder, H.C., and Weber, K. (1984). Amino sequence requirements in the epitope recognized by the the a -rubulin-specific rat monoclonal antibody YL 1/2. EMBO J. 3, 1295-1300.
40. Wessel, D., and Flügge, U.J. (1984). A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141-143.
41. Woodhead, J.L., and Lowey, S. (1983). An in vitro study of the interactions of skeletal muscle M-protein and creatine kinase with myosin and its subfragments. J. Mol. Biol. 168, 831-846.