The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization

Molecular Cell

Volumn 13, Issue 4, 2004, Pages 511-522

  Shimada, Atsushi ^a   Nyitrai, Miklós ^b,c   Vetter, Ingrid R ^a   Kühlmann, Dorothee ^a   Bugyi, Beáta ^c   Narumiya, Shuh ^d   Geeves, Michael A ^b   Wittinghofer, Alfred ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b UNIVERSITY OF KENT   (United Kingdom)

^c UNIVERSITY OF PÉCS   (Hungary)

^d KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ELONGATION FACTOR;

ACTIN FILAMENT; ACTIN POLYMERIZATION; ARTICLE; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS INHIBITION; X RAY ANALYSIS;

ACTINS; ALANINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; KINETICS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 1542285173     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00059-0     Document Type: Article

References (44)

1. Alberts A.S. Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276:2001;2824-2830.
2. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S.et al. Crystallography & NMR system. a new software suite for macromolecular structure determination Acta Crystallogr. D Biol. Crystallogr. 54:1998;905-921.
3. Castrillon D.H., Wasserman S.A. Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development. 120:1994;3367-3377.
4. Chai J., Du C., Wu J.W., Kyin S., Wang X., Shi Y. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature. 406:2000;855-862.
5. CCP4 Collaborative Computational Project, Number 4) Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763.
6. Conibear P.B., Geeves M.A. Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin. Biophys. J. 75:1998;926-937.
7. Copeland J.W., Treisman R. The Diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization. Mol. Biol. Cell. 13:2002;4088-4099.
8. Criddle A.H., Geeves M.A., Jeffries T. The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem. J. 232:1985;343-349.
9. de La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Acta Crystallogr. A. 276:1997;472-494.
10. Djinovic-Carugo K., Young P., Gautel M., Saraste M. Structure of the α-actinin rod. molecular basis for cross-linking of actin filaments Cell. 98:1999;537-546.
11. Evangelista M., Blundell K., Longtine M.S., Chow C.J., Adames N., Pringle J.R., Peter M., Boone C. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science. 276:1997;118-122.
12. Fernandez I., Ubach J., Dulubova I., Zhang X., Sudhof T.C., Rizo J. Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A. Cell. 94:1998;841-849.
13. Goody R.S., Holmes K.C. Cross-bridges and the mechanism of muscle contraction. Biochim. Biophys. Acta. 726:1983;13-39.
14. Grum V.L., Li D., MacDonald R.I., Mondragón A. Structures of two repeats of spectrin suggest models of flexibility. Cell. 98:1999;523-535.
15. Holm L., Sander C. The FSSP database of structurally aligned protein fold families. Nucleic Acids Res. 22:1994;3600-3609.
16. Ishizaki T., Morishima Y., Okamoto M., Furuyashiki T., Kato T., Narumiya S. Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1. Nat. Cell Biol. 3:2001;8-14.
17. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
18. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:1993;795-800.
19. Kohno H., Tanaka K., Mino A., Umikawa M., Imamura H., Fujiwara T., Fujita Y., Hotta K., Qadota H., Watanabe T.et al. Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15:1996;6060-6068.
20. Koradi R., Billeter M., Wüthrich K. Molmol. a program for display and analysis of macromolecular structures J. Mol. Graph. 14:1996;51-55.
21. Kovar D.R., Kuhn J.R., Tichy A.L., Pollard T.D. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161:2003;875-887.
22. Kraulis P.J. MolScript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
23. Kurzawa S.E., Geeves M.A. A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein. J. Muscle Res. Cell Motil. 17:1996;669-676.
24. Li F., Higgs H.N. The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr. Biol. 13:2003;1335-1340.
25. Merrit E.A., Murphy M.E.P. Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D. 50:1994;869-873.
26. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Acta Crystallogr. A. 276:1997;307-326.
27. Palazzo A.F., Cook T.A., Alberts A.S., Gundersen G.G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 3:2001;723-729.
28. Posern G., Sotiropoulos A., Treisman R. Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor. Mol. Biol. Cell. 13:2002;4167-4178.
29. Pring M., Evangelista M., Boone C., Yang C., Zigmond S.H. Mechanism of formin-induced nucleation of actin filaments. Biochemistry. 42:2003;486-496.
30. Pruyne D., Evangelista M., Yang C., Bi E., Zigmond S., Bretscher A., Boone C. Role of formins in actin assembly. nucleation and barbed-end association Science. 297:2002;612-615.
31. Sagot I., Klee S.K., Pellman D. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4:2002;42-50. a.
32. Sagot I., Rodal A.A., Moseley J., Goode B.L., Pellman D. An actin nucleation mechanism mediated by Bni1 and Profilin. Nat. Cell Biol. 4:2002;626-631. b.
33. Sotiropoulos A., Gineitis D., Copeland J., Treisman R. Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell. 98:1999;159-169.
34. Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:1971;4866-4871.
35. Sternlicht H., Ringel I. Colchicine inhibition of microtubule assembly via copolymer formation. J. Biol. Chem. 254:1979;10540-10550.
36. Takeya R., Sumimoto H. Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation. J. Cell Sci. 116:2003;4567-4575.
37. Terwilliger T.C., Berendzen J. Bayesian difference refinement. Acta Crystallogr. D. 52:1996;1004-1011.
38. Usón I., Sheldrick G.M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9:1999;643-648.
39. Wallar B.J., Alberts A.S. The formins. active scaffolds that remodel the cytoskeleton Trends Cell Biol. 13:2003;435-446.
40. Watanabe N., Kato T., Fujita A., Ishizaki T., Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1:1999;136-143.
41. Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S. p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16:1997;3044-3056.
42. Wear M.A., Yamashita A., Kim K., Maéda Y., Cooper J.A. How capping protein binds the barbed end of the actin filament. Curr. Biol. 13:2003;1531-1537.
43. Weeks C.M., Miller R. Optimizing Shake-and-Bake for proteins. Acta Crystallogr. D. 55:1999;492-500.
44. Zigmond S.H., Evangelista M., Boone C., Yang C., Dar A.C., Sicheri F., Forkey J., Pring M. Formin leaky cap allows elongation in the presence of tight capping proteins. Curr. Biol. 13:2003;1820-1823.