Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V

Protein Science

Volumn 11, Issue 12, 2002, Pages 2909-2923

  Martin, Stephen R ^a   Bayley, Peter M ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

Calmodulin; IQ motif; Motility; Myosin V; Regulatory complex

Indexed keywords

CALMODULIN; MYOSIN V; APOPROTEIN; CALCIUM; DROSOPHILA PROTEIN; MYO5A PROTEIN, MOUSE; MYOSIN HEAVY CHAIN; PEPTIDE FRAGMENT;

ALPHA HELIX; ANIMAL CELL; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; GENE SEQUENCE; GENE TARGETING; MOLECULAR INTERACTION; MOUSE; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; STOICHIOMETRY; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; METABOLISM; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SPECTROFLUOROMETRY;

ANIMALIA; MURINAE;

AMINO ACID MOTIFS; ANIMALS; APOPROTEINS; BINDING SITES; CALCIUM; CALMODULIN; CIRCULAR DICHROISM; DROSOPHILA PROTEINS; MICE; MODELS, MOLECULAR; MYOSIN HEAVY CHAINS; MYOSIN TYPE V; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE;

EID: 0036892412     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0210402     Document Type: Article

References (56)

1. Alexander, K.A., Cimler, B.M., Meier, K.E., and Storm, D.R. 1987. Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein. J. Biol. Chem. 262: 6108-6113.
2. Anson, M., Geeves, M.A., Kurzawa, S.E., and Manstein, D.J. 1996. Myosin motors with artificial lever arms. EMBO J. 15: 6069-6074.
3. Bähler, M. and Rhoads, A.R. 2002. Calmodulin signalling via the IQ motif. FEBS Letts. 513: 107-113.
4. Bähler, M., Kroschewski, R., Stoffler, H.E., and Behrmann, T. 1994. Rat myr 4 defines a novel subclass of myosin I: Identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity. J. Cell Biol. 126: 375-389.
5. Barth, A., Martin, S.R., and Bayley, P.M. 1998. Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence. J. Biol. Chem. 273: 2174-2183.
6. Bayley, P.M., Findlay, W.A., and Martin, S.R. 1996. Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences. Protein Sci. 5: 1215-1228.
7. Bayley, P.M., Martin, S.R., Browne, J.P., and Royer, C.A. 2002. Time-resolved anisotropy studies of domain-specific interactions of calmodulin with target sequences of myosin V. Biophys. J. 82: 409A.
8. Berridge, M.A., Lipp, P., and Bootman, M.D. 2001. The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell. Biol. 1: 11-21.
9. Brown, S.E., Martin, S.R., and Bayley, P.M. 1997. Kinetic control of the dissociation pathway of calmodulin-peptide complexes. J. Biol. Chem. 272: 3389-3397.
10. Browne, J.P., Strom, M., Martin, S.R., and Bayley, P.M. 1997. The role of β-sheet interactions in domain stability, folding, and target recognition reactions of calmodulin. Biochemistry 36: 9550-9561.
11. Cheney, R.E. and Mooseker, M.S. 1992. Unconventional myosins. Curr. Opin. Cell Biol. 4: 27-35.
12. Chin, D. and Means, A.R. 2001. Calmodulin: A prototypical calcium sensor. Trends Cell Biol. 10: 322-328.
13. Cimler, B.M., Andreasen, T.J., Andreasen, K.I., and Storm, D.R. 1985. P-57 is a neural specific calmodulin-binding protein. J. Biol. Chem. 260: 10784-10788.
14. Collins, K., Sellers, J.R., and Matsudaira, P. 1990. Calmodulin dissociation regulates brush border mysoin I (110kD-calmodulin) mechanochemical activity in vitro. J. Cell Biol. 110: 1137-1147.
15. Coluccio, L.M. and Bretscher, A. 1987. Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to F-actin: Formation of decorated filaments. J. Cell Biol. 105: 325-333.
16. Cope, M.J., Whisstock, J., Rayment, I., and Kendrick-Jones, J. 1996. Conservation within the myosin motor domain: Implications for structure and function. Structure 4: 969-987.
17. Crivici, A. and Ikura, M. 1995. Molecular and structural basis of target recognition by calmodulin. Ann. Rev. Biophys. Biomol. Struct. 24: 85-116.
18. De La Cruz, E.M., Wells, A.L., Sweeney, H.L., and Ostap, E.M. 2000. Actin and light chain isoform dependence of myosin V kinetics. Biochemistry 39: 14196-14202.
19. Drum, C.L., Yan, S.-Z., Bard, J., Shen, Y.-Q., Lu, D., Soelaiman, S., Grabarek, Z., Bohm, A., and Tang, W.-J. 2002. Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415: 396-402.
20. 2+ channels revealed by FRET in single living cells. Neuron 31: 973-985.
21. Finn, B.E., Evenäs, J., Drakenberg, T., Waltho, J.P., Thulin, E., and Forsén, S. 1995. Calcium-induced structural changes and domain autonomy in calmodulin. Nat. Struct. Biol. 2: 777-783.
22. Geeves, M.A. 2002. Stretching the lever-arm theory. Nature 415: 129-130.
23. Geeves, M.A., Perreault-Micale, C., and Coluccio, L.M. 2000. Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding. J. Biol. Chem. 275: 21624-21630.
24. Guex, N. and Peitsch, M.C. 1997. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18: 2714-2723.
25. 2+-dependent regulation of the motor activity of myosin V. J. Biol. Chem. 275: 34766-34771.
26. Houdusse, A. and Cohen, C. 1996. Structure of the regulatory domain of scallop myosin at 2 Å resolution: Implications for regulation. Structure 4: 21-32.
27. 2+-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switch. Structure 4: 1475-1490.
28. Houdusse, A., Kalabokis, V.N., Himmel, D., Szent-Györgyi, A.G., and Cohen, C. 1999. Atomic structure of scallop myosin subfragment SI complexed with MgADP: A novel conformation of the myosin head. Cell 97: 459-470.
29. Houdusse, A., Gaucher, J.-F., Mui, S., Krementsova, E., Trybus, K.M., and Cohen, C. 2000. Crystal structure of calmodulin bound to the IQ motifs of myosin V. Biophys. J. 78: 272A.
30. Inoue, A. and Ikebe, M. 2001. Role of the IQ motifs on the regulation of motor activities of myosin 1β. Mol. Biol. Cell 12: 1606.
31. Kemp, B.E., Pearson, R.B., Guerriero, V.J., Bagchi, I., and Means, A.R. 1987. The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. J. Biol. Chem. 262: 2542-2548.
32. Kuboniwa, H., Tjandra, N., Grzesiek, S., Ren, H., Klee, C.B., and Bax, A. 1995. Solution structure of calcium-free calmodulin. Nat. Struct. Biol. 2: 768-776.
33. 2+-calmodulin-dependent kinase kinase peptide. J. Mol. Biol. 312: 59-68.
34. Linse, S., Helmersson, A., and Forsén, S. 1991. Calcium binding to calmodulin and its globular domains. J. Biol. Chem. 266: 8050-8054.
35. 2+-dependent interactions of calmodulin with target sequences. Protein Sci. 9: 2477-2488.
36. 2+binding sites of calmodulin. J. Biol. Chem. 267: 5286-5295.
37. Meador, W.E., Means, A.R., and Quiocho, F.A. 1993. Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. Science 262: 1718-1721.
38. 2+-calmodulin-dependent kinase kinase. Nat. Struct. Biol. 6: 819-824.
39. Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4: 2411-2423.
40. 2+-sensitive motility. J. Biol. Chem. 275: 21618-21623.
41. Persechini, A., McMillan, K., and Leakey, P. 1994. Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments. J. Biol. Chem. 269: 16148-16154.
42. Rhoads, A.R. and Friedberg, F. 1997. Sequence motifs for calmodulin recognition. FASEB J. 11: 331-340.
43. Ruff, C., Furch, M., Brenner, B., Manstein, D.J., and Meyerhöfer, E. 2001. Single-molecule tracking of myosins with genetically amplified domains. Nat. Struct. Biol. 8: 226-229.
44. 2+-calmodulin. Nature 410: 1120-1124.
45. 2+-CaM-dependent protein kinase (CaM-kinase) cascade. Trends Biochem. Sci. 24: 232-236.
46. 2+-APTase activity of brush border myosin I with three or four calmodulin light chains but inhibits with less than two bound. J. Biol. Chem. 266: 1312-1319.
47. Swindells, M.B. and Ikura, M. 1996. Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications for binding IQ-motifs. Nat. Struct. Biol. 3: 501-504.
48. Trybus, K.M., Krementsova, E., and Freyzon, Y. 1999. Kinetic characterization of a monomeric unconventional myosin V construct. J. Biol. Chem. 274: 27448-27456.
49. Tsvetkov, P.O., Protasevich, I.I., Gilli, R., Lafitte, D., Lobachov, V.M., Haiech, J., Briand, C., and Makarov, A.A. 1999. Apocalmodulin binds to the myosin light chain kinase calmodulin target site. J. Biol. Chem. 274: 18161-18164.
50. Uyeda, T.Q., Abramson, P.D., and Spudich, J.A. 1996. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl. Acad. Sci. 93: 4459-4464.
51. Wang, F., Chen, L., Arcucci, O., Harvey, E.V., Bowers, B., Xu, Y., Hammer III, J.A., and Sellers, J.R. 2000. Effect of ADP and ionic strength on the kinetic and motile properties of recombinant mouse myosin V. J. Biol. Chem. 275: 4329-4335.
52. Whittaker, M. and Milligan, R.A. 1997. Conformational changes due to calcium-induced calmodulin dissociation in brush border myosin I-decorated F-actin revealed by cryoelectron microscopy and image analysis. J. Mol. Biol. 269: 548-557.
53. Wolenski, J.S., Hayden, S.M., Forscher, P., and Mooseker, M.S. 1993. Calciumcalmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry. J. Cell Biol. 122: 613-621.
54. Zhang, M., Tanaka, T., and Ikura, M. 1995. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2: 758-767.
55. Zhu, T., Sata, M., and Ikebe, M. 1996. Functional expression of mammalian myosin Ib: Analysis of its motor activity. Biochemistry 35: 513-522.
56. 2+ binding sites of calmodulin are critical for the regulation of myosin Ib motor function. J. Biol. Chem. 273: 20481-20486.