Structural basis for activation of the titin kinase domain during myofibrillogenesis

Nature

Volumn 395, Issue 6705, 1998, Pages 863-869

  Mayans, Olga ^a   Van Der Ven, Peter F M ^b   Wilm, Matthias ^c   Mues, Alexander ^c   Young, Paul ^c   Fürst, Dieter O ^b   Wilmanns, Matthias ^a   Gautel, Mathias ^c  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF POTSDAM   (Germany)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; MUSCLE PROTEIN; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN SERINE KINASE; TYROSINE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MOUSE; MUSCLE DEVELOPMENT; MUSCLE FIBRIL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; SARCOMERE; SKELETAL MUSCLE;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CELL DIFFERENTIATION; CELL LINE; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; MUSCLE, SKELETAL; MYOFIBRILS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN KINASE INHIBITORS; PROTEIN KINASES; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TYROSINE;

EID: 0032578901     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/27603     Document Type: Article

References (47)

1. Taylor, S. S., Radzio-Andelzelm, E. & Hunter, T. How do protein kinases discriminate between serine/ threonine and tyrosine? Structural insights from the insulin receptor tyrosine kinase. FASEB J. 9, 1255-1266 (1995).
2. Johnson, L. N., Noble, M. E. M. & Owen, D. J. Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158 (1996).
3. Johnson, L. N., Lowe, E. D., Noble, M. E. M. & Owen, D. J. The structural basis for substrate recognition and control by protein kinases. FEBS Lett. 430, 1-11 (1998).
4. Trinick, J. Titin as a scaffold and spring. Curr. Biol. 6, 258-260 (1996).
5. Maruyama, K. Connectin/titin, giant elastic protein of muscle. FASEB J. 11, 341-345 (1997).
6. Heierhorst, J. et al. Autophosphorylation of molluscan twitchin and interaction of its kinase domain with calcium/calmodulin. J. Biol. Chem. 269, 21086-21093 (1994).
7. Vibert, P., Edelstein, S. M., Castellani, L. & Elliot, B. W. Mini-titins in striated and smooth molluscan muscles: structure, location and immunological crossreactivity. J. Muscle Res. Cell Motil. 14, 598-607 (1993).
8. Obermann, W. M. J. et al. The structure of the sarcomeric M band: localization of defined domains of myomesin, M.-protein and the 250 kD carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol. 134, 1441-1453 (1996).
9. Gautel, M. et al. A calmodulin-binding sequence in the C-terminus of human cardiac titin kinase. Eur. J. Biochem. 230, 752-759 (1995).
10. Kobe, B. et al. Giant protein kinases: domain interactions and structural basis of autoregulation. EMBO J. 15, 6810-6821 (1996).
11. Sebestyén, M. G., Fritz, J. D., Wolff, J. A. & Greaser, M. L. Primary structure of the kinase domain region of rabbit skeletal and cardiac titin. J. Muscle Res. Cell Motil. 17, 343-348 (1996).
12. 2+/S100 regulation of giant protein kinases. Nature 380, 636-639 (1996).
13. Goldberg, J., Nairn, A. C. & Kuriyan, J. Structural basis for the auto-inhibition of calcium/calmodulin-dependent protein kinase I. Cell 84, 875-887 (1996).
14. Crivici, A. & Ikura, M. Modular and structural basis of target recognition by calmodulin. Annu. Rev. Biomol. Struct. 24, 85-116 (1995).
15. Heierhorst, J. et al. Phosphorylation of myosin regulatory light chains by the molluscan twitchin kinase. Eur. J. Biochem. 233, 426-431 (1995).
16. Chin, D., Winkler, K. E. & Means, A. R. Characterisation of substrate phosphorylation and use of calmodulin mutants to address implications from the enzyme crystal structure of calmodulin-dependent protein kinase I. J. Biol. Chem. 272, 31235-31240 (1997).
17. Hubbard, S. R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16, 5572-5581 (1997).
18. Zhang, F. et al. Atomic stucture of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704-711 (1994).
19. Songyang, Z. et al. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinase I and II, phosphorylatse kinase, calmodulin-dependent kinase II, CDK5 and Erk1. Mol. Cell. Biol. 16, 6486-6493 (1996).
20. Lowe, E. D. et al. The crystal structure of a phosphorylase inase peptide substrate complex: kinase substrate recognition. EMBO J. 16, 6648-6658 (1997).
21. Taylor, S. S. et al. A template for the protein kinase family. Trends Bochem. Sci. 18, 84-89 (1993).
22. Valle, G. et al. Telethonin, a novel sarcomeric protein of heart and skeletal muscle. FEBS Lett. 415, 163-168 (1997).
23. Mues, A. et al. Two immunoglobulin-like domains of the Z-disk portion of titin interact in a conformation-dependent way with telethonin. FEBS Lett. 428, 111-114 (1998).
24. Engelkamp, D., Schäfer, B. W., Erne, P. & Heizmann, C. W. S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart. Biochemistry 31, 10258-10264 (1992).
25. Hubbard, S. R., Wei, L., Ellis, L. & Hendrickson, W. A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372, 746-754 (1994).
26. 2+/S100-dependent protein kinases. Eur. J. Biochem. 242, 454-459 (1996).
27. Songyang, Z. et al. Use of an oriented peptide library to determine the optimal substrates of protein kinases. Curr. Biol. 4, 973-982 (1994).
28. 2. Proc. Natl Acad. Sci. USA 94, 11233-11237 (1992).
29. Andersson, S. et al. Cloning, structure, and expression of mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264, 8222-8229 (1989).
30. Young, P., Ferguson, C., Bañuelos, S. & Gautel, M. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EMBO J. 17, 1614-1624 (1998).
31. Cohen, O., Feinstein, E. & Kimchi, A. DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell-death inducing functions that depend on its catalytic activity. EMBO J. 16, 998-1008 (1997).
32. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
33. Weijland, A. et al. The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Eur. J. Biochem. 240, 756-764 (1996).
34. Wilm, M. & Mann, M. Analytical properties of the nanoelectrospray ion source. Anal. Chem. 68, 1-8 (1996).
35. Dedman, J. R. & Kaetzel, M. A. Calmodulin purification and fluorescence labeling. Methods Enzymol. 102, 1-8 (1983).
36. Chayen, N. E. A novel technique to control the rate of vapour diffusion, giving larger protein crystals. J. Appl. Crystallogr. 30, 198-202 (1997).
37. Otkinowski, Z. in Proceedings of the CCP4 Study Weekend (eds Sawyer, L., Isaacs, N. & Bailey, S.) 56-62 (SERC Daresbury Lab., 1993).
38. Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 577-587 (1994).
39. Collaborative Computaitonal Project 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-767 (1994).
40. Kleywegt, G. T. & Jones, T. A. in Proceedings of the CCP4 Study Weekend (eds Sawyer, L., Isaacs, N. & Bailey, S.) 56-62 (SERC, Daresbury Lab., 1994).
41. Brünger, A. T., Kuriyan, J. & Karplus, M. Crystallographic R factor refinement by molecular dynamics. Science 235, 458-466 (1987).
42. Tan, J. L. & Spudich, J. Characterization and bacterial expression of the Dictyostelium myosin light chain kinase cDNA. J. Biol. Chem. 266, 16044-16049 (1991).
43. Cohen, G. E. A program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Crystallogr. 30, 1160-1161 (1991).
44. Kraulis, P. J. MOLSCRIPT: a program to produce detailed and schematic plots protein structure. J. Appl. Crystallogr. 24, 251-259 (1991).
45. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insight from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
46. Jones, T. A. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171 (1985).
47. Fürst, D. O., Osborn, M., Nave, R. & Weber, K. 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 (1988).