The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization

Molecular Biology of the Cell

Volumn 13, Issue 11, 2002, Pages 4088-4099

  Copeland, John W ^a   Treisman, Richard ^a  

^a THE FRANCIS CRICK INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DIAPHANOUS RELATED FORMIN; F ACTIN; G ACTIN; GUANOSINE TRIPHOSPHATASE; METHENAMINE; PROTEIN MDIA1; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SERUM RESPONSE FACTOR; UNCLASSIFIED DRUG; ACTIN; CARRIER PROTEIN; DIAP1 PROTEIN, MOUSE; PHALLOIDIN;

ACTIN POLYMERIZATION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CORRELATION ANALYSIS; EFFECTOR CELL; GENE MUTATION; HUMAN; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN ISOLATION; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION; AMINO ACID SEQUENCE; ANIMAL; CELL STRAIN 3T3; CHEMISTRY; CYTOSKELETON; GENETICS; METABOLISM; MOLECULAR GENETICS; MOUSE; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; REPORTER GENE; SEQUENCE ALIGNMENT;

3T3 CELLS; ACTINS; AMINO ACID SEQUENCE; ANIMALS; CARRIER PROTEINS; CYTOSKELETON; GENES, REPORTER; MICE; MOLECULAR SEQUENCE DATA; PHALLOIDINE; PROTEIN STRUCTURE, TERTIARY; RHOA GTP-BINDING PROTEIN; SEQUENCE ALIGNMENT; SERUM RESPONSE FACTOR; SIGNAL TRANSDUCTION;

EID: 0036854328     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.02-06-0092     Document Type: Article

References (53)

1. Alberts, A.S. (2001). Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276, 2824-2830.
2. Arsenian, S., Weinhold, B., Oelgeschlager, M., Ruther, U., and Nordheim, A. (1998). Serum response factor is essential for mesoderm formation during mouse embryogenesis. EMBO J. 17, 6289-6299.
3. Bleul, C.C., Fuhlbrigge, R.C., Casasnovas, J.M., Aiuti, A., and Springer, T.A. (1996). A highly efficacious lymphocyte chemoattractant, stromal cell-derived factor 1 (SDF-1). J. Exp. Med. 184, 1101-1109.
4. Burger, J.A., Burger, M., and Kipps, T.J. (1999). Chronic lymphocytic leukemia B cells express functional CXCR4 chemokine receptors that mediate spontaneous migration beneath bone marrow stromal cells. Blood 94, 3658-3667.
5. Castrillon, D.H., and Wasserman, S.A. (1994). Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 120, 3367-3377.
6. Chan, D.C., Bedford, M.T., and Leder, P. (1996). Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15, 1045-1054.
7. Chang, F., Drubin, D., and Nurse, P. (1997). cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137, 169-182.
8. Chang, J.H., Gill, S., Settleman, J., and Parsons, S.J. (1995). c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation. J. Cell Biol. 130, 355-368.
9. Demma, M., Warren, V., Hock, R., Dharmawardhane, S., and Condeelis, J. (1990). Isolation of an abundant 50,000-dalton actin filament bundling protein from Dictyostelium amoebae. J. Biol. Chem. 265, 2286-2291.
10. Evangelista, M., Blundell, K., Longtine, M.S., Chow, C.J., Adames, N., Pringle, J.R., Peter, M., and Boone, C. (1997). Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122.
11. Evangelista, M., Pruyne, D., Amberg, D.C., Boone, C., and Bretscher, A. (2002). Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4, 32-41.
12. Feierbach, B., and Chang, F. (2001). Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr. Biol. 11, 1656-1665.
13. Fincham, V.J., Chudleigh, A., and Frame, M.C. (1999). Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation. J. Cell Sci. 112, 947-956.
14. Fincham, V.J., Unlu, M., Brunton, V.G., Pitts, J.D., Wyke, J.A., and Frame, M.C. (1996). Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J. Cell Biol. 135, 1551-1564.
15. Fujiwara, T., Mammoto, A., Kim, Y., and Takai, Y. (2000). Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2. Biochem. Biophys. Res. Commun. 271, 626-629.
16. Geneste, O., Copeland, J., and Treisman, R. (2002). LIM kinase and Diaphanous cooperate to regulate Serum Response Factor and actin dynamics. J. Cell Biol. 157, 831-838.
17. Grosse, R., Roelle, S., Herrlich, A., Hohn, J., and Gudermann, T. (2000). Epidermal growth factor receptor tyrosine kinase mediates Ras activation by gonadotropin-releasing hormone. J. Biol. Chem. 275, 12251-12260.
18. Habas, R., Kato, Y., and He, X. (2001). WNT/frizzled activation of Rho regulates vertebrate gastrulation and requires a novel formin homology protein DAAM1. Cell 107, 843-854.
19. Hill, C.S., Wynne, J., and Treisman, R. (1995). The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 81, 1159-1170.
20. Howard, T.H., and Meyer, W.H. (1984). Chemotactic peptide modulation of actin assembly and locomotion in neutrophils. J. Cell Biol. 98, 1265-1271.
21. Imamura, H., Tanaka, K., Hihara, T., Umikawa, M., Kamei, T., Takahashi, K., Sasaki, T., and Takai, Y. (1997). Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16, 2745-2755.
22. Ishizaki, T., Morishima, Y., Okamoto, M., Furuyashiki, T., Kato, T., and Narumiya, S. (2001). Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1. Nat. Cell. Biol. 3, 8-14.
23. Kohno, H. et al. (1996). Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15, 6060-6068.
24. Krebs, A., Rothkegel, M., Klar, M., and Jockusch, B.M. (2001). Characterization of functional domains of mDia1, a link between the small GTPase Rho and the actin cytoskeleton. J. Cell Sci. 114, 3663-3672.
25. Lyubimova, A., Bershadsky, A.D., and Ben-Ze'ev, A. (1997). Autoregulation of actin synthesis responds to monomeric actin levels. J. Cell Biochem. 65, 469-478.
26. Machesky, L.M., and Insall, R.H. (1999). Signaling to actin dynamics. J. Cell Biol. 146, 267-272.
27. Mack, C.P., Somlyo, A.V., Hautmann, M., Somlyo, A.P., and Owens, G.K. (2001). Smooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization. J. Biol. Chem. 276, 341-347.
28. Marais, R., Wynne, J., and Treisman, R. (1993). The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain. Cell 73, 381-393.
29. Mohun, T., Garrett, N., and Treisman, R. (1987). Xenopus cytoskeletal actin and human c-fos gene promoters share a conserved protein-binding site. EMBO J. 6, 667-673.
30. Murray, J.W., Edmonds, B.T., Liu, G., and Condeelis, J. (1996). Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends. J. Cell Biol. 135, 1309-1321.
31. Nakano, K., Takaishi, K., Kodama, A., Mammoto, A., Shiozaki, H., Monden, M., and Takai, Y. (1999). Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells. Mol. Biol. Cell 10, 2481-2491.
32. Ozaki-Kuroda, K., Yamamoto, Y., Nohara, H., Kinoshita, M., Fujiwara, T., Irie, K., and Takai, Y. (2001). Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 21, 827-839.
33. Palazzo, A.F., Cook, T.A., Alberts, A.S., and Gundersen, G.G. (2001). mDia mediates Rho-regulated formation, and orientation of stable microtubules. Nat. Cell Biol. 3, 723-729.
34. Petersen, J., Nielsen, O., Egel, R., and Hagan, I.M. (1998). FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation. J. Cell Biol. 141, 1217-1228.
35. Posern, G., Sotiropoulos, A., and Treisman, R. (2002). Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor. Mol. Biol. Cell (in press).
36. Pruyne, D., Evangelista, M., Yang, C., Bi, E., Zigmond, S., Bretscher, A., and Boone, C. (2002). Role of formins in actin assembly: Nucleation and barbed end association. Science, published online, June 6.
37. Reuner, K.H., Wiederhold, M., Dunker, P., Just, I., Bohle, R.M., Kroger, M., and Katz, N. (1995). Autoregulation of actin synthesis in hepatocytes by transcriptional and posttranscriptional mechanisms. Eur. J. Biochem. 230, 32-37.
38. Ridley, A.J. (1999). Stress fibers take shape. Nat. Cell Biol. 1, E64-E66.
39. Ridley, A.J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
40. Sagot, I., Klee, S.K., and Pellman, D. (2002). Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4, 42-50.
41. Satoh, S., and Tominaga, T. (2001). mDia-interacting protein acts downstream of Rho-mDia, and modifies Src activation, and stress fiber formation. J. Biol. Chem. 276, 39290-39294.
42. Sharpless, K.E., and Harris, S.D. (2002). Functional characterization, and localization of the aspergillus nidulans formin SEPA. Mol. Biol. Cell. 13, 469-479.
43. Sotiropoulos, A., Gineitis, D., Copeland, J., and Treisman, R. (1999). Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell 98, 159-169.
44. Tominaga, T., Sahai, E., Chardin, P., McCormick, F., Courtneidge, S.A., and Alberts, A.S. (2000). Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling. Mol. Cell 5, 13-25.
45. Uetz, P., Fumagalli, S., James, D., and Zeller, R. (1996). Molecular interaction between limb deformity proteins (formins) and Src family kinases. J. Biol. Chem. 271, 33525-33530.
46. Umikawa, M., Tanaka, K., Kamei, T., Shimizu, K., Imamura, H., Sasaki, T., and Takai, Y. (1998). Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: Implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Oncogene 16, 2011-2016.
47. Uruno, T., Liu, J., Zhang, P., Fan, Y., Egile, C., Li, R., Mueller, S.C., and Zhan, X. (2001). Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nat. Cell Biol. 3, 259-266.
48. Wasserman, S. (1998). FH proteins as cytoskeletal organizers. Trends Cell Biol. 8, 111-115.
49. Watanabe, N., Kato, T., Fujita, A., Ishizaki, T., and Narumiya, S. (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1, 136-143.
50. Watanabe, N. et al. (1997). p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056.
51. Weed, S.A., Karginov, A.V., Schafer, D.A., Weaver, A.M., Kinley, A.W., Cooper, J.A., and Parsons, J.T. (2000). Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J. Cell Biol. 151, 29-40.
52. Yang, F., Demma, M., Warren, V., Dharmawardhane, S., and Condeelis, J. (1990). Identification of an actin-binding protein from Dictyostelium as elongation factor 1a. Nature 347, 494-496.
53. Zeller, R., Haramis, A.G., Zuniga, A., McGuigan, C., Dono, R., Davidson, G., Chabanis, S., and Gibson, T. (1999). Formin defines a large family of morphoregulatory genes and functions in establishment of the polarising region. Cell Tissue Res. 296, 85-93.