Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities

FEBS Letters

Volumn 579, Issue 2, 2005, Pages 441-448

  Madrid, Ricardo ^a   Gasteier, Judith E ^b   Bouchet, Jérôme ^a   Schröder, Sebastian ^b   Geyer, Matthias ^c   Benichou, Serge ^a   Fackler, Oliver T ^b  

^a INSERM   (France)

^b UNIVERSITY HOSPITAL HEIDELBERG   (Germany)

^c MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

Coiled coil motif; Cytoskeleton; Diaphanous related formin; Formin homology 2 domain containing protein 1; Oligomerization

Indexed keywords

HYBRID PROTEIN; PROTEIN SUBUNIT; RAC1 PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CYTOSKELETON; HUMAN; HUMAN CELL; HYBRID; IMMUNOPRECIPITATION; MAMMAL CELL; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; TRANSCRIPTION INITIATION; YEAST;

AMINO ACID MOTIFS; ANIMALS; FETAL PROTEINS; HELA CELLS; HUMANS; MICE; MODELS, MOLECULAR; NIH 3T3 CELLS; NUCLEAR PROTEINS; PROTEIN STRUCTURE, SECONDARY; RAC1 GTP-BINDING PROTEIN; SEQUENCE DELETION; STRESS FIBERS; TRANS-ACTIVATION (GENETICS); TWO-HYBRID SYSTEM TECHNIQUES;

MAMMALIA;

EID: 11844255388     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.009     Document Type: Article

References (28)

1. B.J. Wallar, and A.S. Alberts The formins: active scaffolds that remodel the cytoskeleton Trends Cell Biol. 13 2003 435 446
2. M. Evangelista, S. Zigmond, and C. Boone Formins: signaling effectors for assembly and polarization of actin filaments J. Cell Sci. 116 2003 2603 2611
3. A.F. Palazzo, T.A. Cook, A.S. Alberts, and G.G. Gundersen mDia mediates Rho-regulated formation and orientation of stable microtubules Nat. Cell Biol. 3 2001 723 729
4. T. Ishizaki, Y. Morishima, M. Okamoto, T. Furuyashiki, T. Kato, and S. Narumiya Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1 Nat. Cell Biol. 3 2001 8 14
5. M. Evangelista, D. Pruyne, D.C. Amberg, C. Boone, and A. Bretscher Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast Nat. Cell Biol. 4 2002 260 269
6. F. Li, and H.N. Higgs The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition Curr. Biol. 13 2003 1335 1340
7. J.B. Moseley, I. Sagot, A.L. Manning, Y. Xu, M.J. Eck, D. Pellman, and B.L. Goode A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin Mol. Biol. Cell 15 2004 896 907
8. D. Pruyne, M. Evangelista, C. Yang, E. Bi, S. Zigmond, A. Bretscher, and C. Boone Role of formins in actin assembly: nucleation and barbed-end association Science 297 2002 612 615
9. I. Sagot, A.A. Rodal, J. Moseley, B.L. Goode, and D. Pellman An actin nucleation mechanism mediated by Bni1 and profilin Nat. Cell Biol. 4 2002 626 631
10. M. Pring, M. Evangelista, C. Boone, C. Yang, and S.H. Zigmond Mechanism of formin-induced nucleation of actin filaments Biochemistry 42 2003 486 496
11. N. Watanabe 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
12. T. Tominaga, E. Sahai, P. Chardin, F. McCormick, S.A. Courtneidge, and A.S. Alberts Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling Mol. Cell 5 2000 13 25
13. D.H. Castrillon, and S.A. Wasserman 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
14. A.S. Alberts Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain J. Biol. Chem. 276 2001 2824 2830
15. A. Sotiropoulos, D. Gineitis, J. Copeland, and R. Treisman Signal-regulated activation of serum response factor is mediated by changes in actin dynamics Cell 98 1999 159 169
16. J.W. Copeland, and R. Treisman The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization Mol. Biol. Cell 13 2002 4088 4099
17. J.E. Gasteier, R. Madrid, E. Krautkramer, S. Schroder, W. Muranyi, S. Benichou, and O.T. Fackler Activation of the Rac-binding partner FHOD1 induces actin stress fibers via a ROCK-dependent mechanism J. Biol. Chem. 278 2003 38902 38912
18. J.J. Westendorf The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element J. Biol. Chem. 276 2001 46453 46459
19. S. Koka, C.L. Neudauer, X. Li, R.E. Lewis, J.B. McCarthy, and J.J. Westendorf The formin-homology-domain-containing protein FHOD1 enhances cell migration J. Cell Sci. 116 2003 1745 1755
20. R. Takeya, and H. Sumimoto 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
21. L. Selig Interaction with the p6 domain of the gag precursor mediates incorporation into virions of Vpr and Vpx proteins from primate lentiviruses J. Virol. 73 1999 592 600
22. L. Erdtmann Two independent regions of HIV-1 Nef are required for connection with the endocytic pathway through binding to the mu 1 chain of AP1 complex Traffic 1 2000 871 883
23. A. Shimada, M. Nyitrai, I.R. Vetter, D. Kuhlmann, B. Bugyi, S. Narumiya, M.A. Geeves, and A. Wittinghofer The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization Mol. Cell 13 2004 511 522
24. Y. Xu, J.B. Moseley, I. Sagot, F. Poy, D. Pellman, B.L. Goode, and M.J. Eck Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture Cell 116 2004 711 723
25. T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: An automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385
26. F. Miralles, G. Posern, A.I. Zaromytidou, and R. Treisman Actin dynamics control SRF activity by regulation of its coactivator MAL Cell 113 2003 329 342
27. J.W. Copeland, S.J. Copeland, and R. Treisman Homo-oligomerisation is essential for F-actin assembly by the formin family FH2 domain J. Biol. Chem. 2004
28. N. Watanabe, T. Kato, A. Fujita, T. Ishizaki, and S. Narumiya Cooperation between mDia1 and ROCK in Rho-induced actin reorganization Nat. Cell Biol. 1 1999 136 143