Evidence for a conformational change in actin induced by fimbrin (N375) binding

Journal of Cell Biology

Volumn 139, Issue 2, 1997, Pages 387-396

  Hanein, Dorit ^a   Matsudaira, Paul ^b   DeRosier, David J ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; CALPONIN; F ACTIN;

ACTIN FILAMENT; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CYTOSKELETON; INTERMEDIATE FILAMENT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; SEQUENCE HOMOLOGY;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM-BINDING PROTEINS; CLONING, MOLECULAR; COMPUTER SIMULATION; CONSERVED SEQUENCE; HUMANS; MEMBRANE GLYCOPROTEINS; MICROFILAMENT PROTEINS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MODELS, STRUCTURAL; PROTEIN BINDING; PROTEIN CONFORMATION; RABBITS; RECOMBINANT PROTEINS;

EID: 0030727339     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.2.387     Document Type: Article

References (70)

1. Adams, A.E., D. Botstein, and D.G. Drubin. 1991. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature (Lond.). 354: 404-408.
2. Amos L.A., and A. Klug. 1975. Three-dimensional image reconstructions of the contractile tail of T4 bacteriophage. J. Mol. Biol. 99:51-64.
3. Anderson, N.L., M.A. Gemmell, P.M. Coussens, S. Murao, and E. Huberman. 1985. Specific protein phosphorylation in human promyelocytic HL-60 leukemia cells susceptible or resistant to induction of cell differentiation by phorbol-12-myristate-13-acetate. Cancer Res. 45:4955-4962.
4. Bremer, A., R.C. Millonig, R. Sutterlin, A. Engel, T.D. Pollard, and U. Aebi. 1991. The structural basis for the intrinsic disorder of the actin filament: the "lateral slipping" model. J. Cell Biol. 115:689-703.
5. Bresnick, A.R., P.A. Janmey, and J. Condeelis. 1991. Evidence that a 27-residue sequence is the actin-binding site of ABP-120. J. Biol. Chem. 266:12989-12993.
6. Bretscher, A. 1981. Fimbrin is a cytoskeletal protein that cross-links F-actin in vitro. Proc. Natl. Acad. Sci. USA. 78:6849-6853.
7. Bretscher, A., and K. Weber. 1980. Fimbrin, a new microfilament-associated protein present in rnicrovilli and other cell surface structures. J. Cell Biol. 86: 335-340.
8. Brown, A., G. Bernier, M. Mathieu, J. Rossant, and R. Kothary. 1995a. The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1. Nat. Genet. 10:301-306.
9. Brown, A., G. Dalpe, M. Mathieu, and R. Kothary. 1995b. Cloning and characterization of the neural isoforms of human dystonin. Genomics. 29:777-780.
10. Bullitt, E.S., D.J. DeRosier, L.M. Coluccio, and L.G. Tilney. 1988. Three-dimensional reconstruction of an actin bundle. J. Cell Biol. 107:597-611.
11. Castellani, L., B.W. Elliott, Jr., D.A. Winkelmann, P. Vibert, and C. Cohen. 1987. Myosin binding to actin. Structural analysis using myosin fragments. J. Mol. Biol. 196:955-960.
12. Castresana, J., and M. Saraste. 1995. Does Vav bind to F-actin through a CH domain? FEBS Lett. 374:149-151.
13. Chapel, M.M., W. Shen, and P. Matsudaira. 1995. Sequential expression and differential localization of I-, L-, and T-Fimbrin during differentiation of the mouse intestine and yolk sac. Dev. Dynamics. 203:141-151.
14. de Arruda, M.V., S. Watson, C.S. Lin, J. Leavitt, and P. Matsudaira. 1990. Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. J. Cell Biol. 111:1069-1079.
15. DeRosier, D.J., and P.B. Moore. 1970. Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry. J. Mol. Biol. 52:355-369.
16. Drewes, G., and H. Faulstich. 1993. Cooperative effects on filament stability in actin modified at the C-terminus by substitution or truncation. Eur. J. Biochem. 212:247-253.
17. Dubochet, J., M. Adrian, J.-J. Chang, J.-C. Homo. J. Lepault, A.W. McDowall, and P. Schultz. 1988. Cryo-electron microscopy of vitrified specimens. Q. Rev. Biophys. 21:129-228.
18. Dubreuil, R.R. 1991. Structure and evolution of the actin cross linking proteins. Bioessays. 13:219-226.
19. Egelman, E.H., N. Francis, and D.J. DeRosier. 1982. F-actin is a helix with a random variable twist. Nature (Lond.). 298:131-135.
20. Egelman, E.H. 1986. An algorithm for straightening images of curved filamentous structures. Ultramicroscopy. 19:367-374.
21. Egelman, E.H., and D.J. DeRosier. 1992. Image analysis shows that variations in actin crossover spacins are random, not compensatory. Biophys. J. 63: 1299-1305.
22. Fabbrizio, E., A. Bonet-Kerrache, J.J. Leger, and D. Mornet. 1993. Actin-dystrophin interface. Biochemistry. 32:10457-10463.
23. Glenney, J.R., P. Kaulfus, P. Matsudaira, and K. Weber. 1981. F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvil-lus core filaments. J. Biol. Chem. 256:9283-9288.
24. Goldsmith, S.C., N. Pokala, W. Shen, A.A. Federov, P. Matsudaira, and S.C. Almo. 1997. The structure of an actin-crosslinking domain from human fimbrin. Nat. Struct. Biol. 4:708-712.
25. Goldstein, D., J. Djeu, G. Latter, S. Burbeck, and J. Leavitt. 1985. Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes. Cancer Res. 45:5643-5647.
26. Hartwig, J.H., and D.J. Kwiatkowski. 1991. Actin-binding proteins. Curr. Opin. Cell Biol. 3:87-97.
27. Hirose, K., A. Lockhart, R.A. Cross, and L.A. Amos. 1996. Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules. Proc. Nail. Acad. Sci. USA. 93:9539-9544.
28. Hodgkinson, J.L., M. El-Mezgueldi, R. Craig, P. Vibert, S.B. Marston, and W. Lehman. 1997. 3D image reconstruction of reconstituted smooth muscle thin filaments containing calponin. J. Mol. Biol. 273:150-159.
29. Holtzman, D.A., K.F. Wertman, and D.G. Drubin. 1994. Mapping actin surfaces required for functional interactions in vivo. J. Cell Biol. 126:423-432.
30. Honts. J.E., T.S. Sandrock, S.M. Brower, J.L. O'Dell, and A.E. Adams. 1994. Actin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin. J. Cell Biol. 126:413-422.
31. Jones, T.A., J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard. 1991. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Cryst. A. 47:110-119.
32. Kubler, E., and H. Riezman. 1993. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12:2855-2862.
33. Lebart, M.C., C. Mejean, M. Boyer, C. Roustan, and Y. Benyamin. 1990. Localization of a new alpha-actinin binding site in the COOH-terminal part of actin sequence. Biochem. Biophys. Res. Commun. 173:120-126.
34. Lebart, M.C., C. Mejean, C. Roustan, and Y. Benyamin. 1993. Further characterization of the alpha-actinin-actin interface and comparison with filamin-binding sites on actin. J. Biol. Chem. 268:5642-5648.
35. Lepault, J., J.-L. Ranck, I. Erk, and M.-F. Carlier. 1994. Small angle X-ray scattering and electron cryomicroscopy study of actin filaments: role of the bound nucleotide in the structure of F-actin. J. Struct. Biol. 112:79-91.
36. Levine, B.A., A.J. Moir, V.B. Patchell, and S.V. Perry. 1990. The interaction of actin with dystrophin. FEBS Lett. 263:159-162.
37. Levine, B.A., A.J. Moir, V.B. Patchell, and S.V. Perry. 1992. Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. FEBS Lett. 298:44-48.
38. Lin, C.S., R.H. Aerbersold, S.B. Kent, M. Varma, and J. Leavitt. 1988. Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts. Mol. Cell Biol. 8:4659-4668.
39. Lin, C.S., T. Park, Z.P. Chen, and J. Leavitt. 1993, Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. J. Biol. Chem. 268:2781-2792.
40. Lin, C.S., W. Shen, Z.P. Chen, Y.H. Tu, and P. Matsudaira. 1994. Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney. Mol. Cell Biol. 14:2457-2467.
41. Lorenz, M., D. Popp, and K.C. Holmes. 1993. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
42. Matsudaira, P.T., and D.R. Burgess. 1979. Identification and organization of the components in the isolated microvillus cytoskeleton. J. Cell Biol. 83:667-673.
43. Matsudaira, P. 1991. Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 16:87-92.
44. Matsudaira, P. 1994. The fimbrin and alpha-actinin footprint on actin. J. Cell Biol. 126:285-287.
45. McGough, A., M. Way, and D. DeRosier. 1994. Determination of the α-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126:433-443.
46. Messier, J.M., L.M. Shaw. M. Chapel, P. Matsudaira, and A.M. Mercurion. 1993. Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages. Cell Motil. Cytoskelelon. 25:223-233.
47. Milligan, R.A., and P.F. Flicker. 1987. Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy. J. Cell Biol. 105:29-39.
48. Milligan, R.A., M. Whittaker, and D. Safer, 1990. Molecular structure of F-actin and location of surface binding sites. Nature (Lond.). 348:217-221.
49. Mimura, N., and A. Asano. 1987. Further characterization of a conserved actinbinding 27-kDa fragment of actinogelin and alpha-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking. J. Biol. Chem. 262:4717-4723.
50. Morgan, D.G., and D.J. DeRosier. 1992. Processing images of helical structures: a new twist. Ultramicroscopy. 46:263-285.
51. Morgan, D.G., C. Owen, L.A. Melanson, and D.J. DeRosier. 1995. Structure of bacterial flagellar filaments at 11 A resolution: packing of the alpha-helices. J. Mol. Biol. 249:88-110.
52. Muhlrad, A., P. Cheung, B.C. Phan, C. Miller, and E. Reisler. 1994. Dynamic properties of actin. Structural changes induced by beryllium fluoride. J. Biol. Chem. 269:11852-11858.
53. Namba. Y., M. Ito, Y. Zu, K. Shigesada, and K. Maruyama. 1992. Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J. Biochem. (Tokyo). 112:503-507.
54. Orlova, A., and E.H. Egelman. 1992. Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis. J. Mol. Biol. 227: 1043-1053.
55. Orlova, A., and E.H. Egelman. 1993. A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol Biol. 232:334-341.
56. 2 terminus. Biophys. J. 66:276-285.
57. Orlova, A., and E.H. Egelman. 1995. Structural dynamics of F-actin. I. Changes in the C terminus. J. Mol. Biol. 245:582-597.
58. Orlova, A., E. Prochniewicz, and E.H. Egelman. 1995. Structural dynamics of F-actin. II. Cooperativity in structural transitions. J. Mol. Biol. 245:598-607.
59. Otto, J.J. 1994. Actin-bundling proteins. Curr. Opin. Cell Biol. 6:105-109.
60. Owen, C., and D. DeRosier. 1993. A 13-A map of the actin-scruin filament from the limulus acrosomal process. J. Cell Biol. 123:337-344.
61. Owen, C.H., D.O. Morgan, and D.J. DeRosier. 1996. Image analysis of helical objects: the Brandeis helical package. J. Struct. Biol. 116:167-175.
62. Pardee, J.D., and J.A. Spudich. 1982. Purification of muscle actin. Methods Enzymol. 85 Pt. B:164-181.
63. Stewart, M., R.W. Kensler, and R.J. Levine. 1981. Structure of Limnulus telson muscle thick filaments. J. Mol. Biol. 153:781-790.
64. Stokes, D.L., and D.J. DeRosier. 1987. The variable twist of actin and its modulation by actin-binding proteins. J. Cell Biol. 104:1005-1017.
65. Taylor, K.A., and D.W. Taylor. 1993. Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers. J. Mol. Biol. 230:196-205.
66. Tilney, L.G., and D.J. DeRosier. 1986. Actin filaments, stereocilia, and hair cells of the bird cochlea. IV. How the actin filaments become organized in developing stereocilia and in the cuticular plate. Dev. Biol. 116:119-129.
67. Tilney, L.G., D.J. Derosier, and M.J. Mulroy. 1980. The organization of actin filaments in the stereocilia of cochlear hair cells. J. Cell Biol. 86:244-259.
68. Tilney, M.S., L.G. Tilney, R.E. Stephens. C. Merte, D. Drenckhahn, D.A. Cotanche, and A. Bretscher. 1989. Preliminary biochemical characterization of the stereocilia and cuticular plate of hair cells of the chick cochlea. J. Cell Biol. 109:1711-1723.
69. Toyoshima, C., and T. Wakabayashi. 1985. Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. IV. Reconstitution from minimal- and high-dose images of the actin-tropomyosin-myosin subfragment-1 complex. J. Biochem. (Tokyo). 97:219-243.
70. Trachtenberg, S., and D. DeRosier. 1987. Three-dimensional structure of the frozen-hydrated flagellar filament: the left-handed filament of Salmonella typhimurium. J. Mol. Biol. 195:581-601.