Formin-1 protein associates with microtubules through a peptide domain encoded by exon-2

Experimental Cell Research

Volumn 312, Issue 7, 2006, Pages 1119-1126

  Zhou, Fen ^a   Leder, Philip ^a   Martin, Stuart S ^b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

Actin; Cytoskeleton; FH1; FH2; FH3; Fmn1; Formin; GFP; Microtubule; Nocodazole

Indexed keywords

ACTIN BINDING PROTEIN; GREEN FLUORESCENT PROTEIN; METHENAMINE; NOCODAZOLE; PROTEIN FMN1 IB; TUBULIN; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CYTOPLASM; DISSOCIATION; EXON; FIBROBLAST; GENE DELETION; GENETIC TRANSFECTION; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN LOCALIZATION;

ANIMALIA;

EID: 33645236356     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.12.035     Document Type: Article

References (29)

1. B.J. Wallar, and A.S. Alberts The formins: active scaffolds that remodel the cytoskeleton Trends Cell Biol. 13 2003 435 446
2. L. Lee, S.K. Klee, M. Evangelista, C. Boone, and D. Pellman Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p J. Cell Biol. 144 1999 947 961
3. H. Imamura, K. Tanaka, T. Hihara, M. Umikawa, T. Kamei, K. Takahashi, T. Sasaki, and Y. Takai 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 1997 2745 2755
4. F. Chang Microtubule and actin-dependent movement of the formin cdc12p in fission yeast Microsc. Res. Tech. 49 2000 161 167
5. G.G. Gundersen Evolutionary conservation of microtubule-capture mechanisms Nat. Rev., Mol. Cell Biol. 3 2002 296 304
6. Y. Wen, C.H. Eng, J. Schmoranzer, N. Cabrera-Poch, E.J. Morris, M. Chen, B.J. Wallar, A.S. Alberts, and G.G. Gundersen EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration Nat. Cell Biol. 6 2004 820 830
7. B. Leader, H. Lim, M.J. Carabatsos, A. Harrington, J. Ecsedy, D. Pellman, R. Maas, and P. Leder Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle in mouse oocytes Nat. Cell Biol. 4 2002 921 928
8. 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
9. L. Manseau, J. Calley, and H. Phan Profilin is required for posterior patterning of the Drosophila oocyte Development 122 1996 2109 2116
10. 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
11. 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
12. 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
13. I. Sagot, S.K. Klee, and D. Pellman Yeast formins regulate cell polarity by controlling the assembly of actin cables Nat. Cell Biol. 4 2002 42 50
14. M.M. Kozlov, and A.D. Bershadsky Processive capping by formin suggests a force-driven mechanism of actin polymerization J. Cell Biol. 167 2004 1011 1017
15. D.R. Kovar, and T.D. Pollard Progressing actin: formin as a processive elongation machine Nat. Cell Biol. 6 2004 1158 1159
16. T. Otomo, D.R. Tomchick, C. Otomo, S.C. Panchal, M. Machius, and M.K. Rosen Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain Nature 433 2005 488 494
17. B. Feierbach, F. Verde, and F. Chang Regulation of a formin complex by the microtubule plus end protein tea1p J. Cell Biol. 165 2004 697 707
18. 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
19. T. Kato, N. Watanabe, Y. Morishima, A. Fujita, T. Ishizaki, and S. Narumiya Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells J. Cell Sci. 114 2001 775 784
20. R.P. Woychik, R.L. Maas, R. Zeller, T.F. Vogt, and P. Leder 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene Nature 346 1990 850 853
21. C.C. Wang, D.C. Chan, and P. Leder The mouse formin (Fmn) gene: genomic structure, novel exons, and genetic mapping Genomics 39 1997 303 311
22. A. Kobielak, H.A. Pasolli, and E. Fuchs Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables Nat. Cell Biol. 6 2004 21 30
23. D.C. Chan, and P. Leder Genetic evidence that formins function within the nucleus J. Biol. Chem. 271 1996 23472 23477
24. D.A. O'Rourke, Z.X. Liu, L. Sellin, K. Spokes, R. Zeller, and L.G. Cantley Hepatocyte growth factor induces MAPK-dependent formin IV translocation in renal epithelial cells J. Am. Soc. Nephrol. 11 2000 2212 2221
25. L. Jackson-Grusby, A. Kuo, and P. Leder A variant limb deformity transcript expressed in the embryonic mouse limb defines a novel formin Genes Dev. 6 1992 29 37
26. D.C. Chan, A. Wynshaw-Boris, and P. Leder Formin isoforms are differentially expressed in the mouse embryo and are required for normal expression of fgf-4 and shh in the limb bud Development 121 1995 3151 3162
27. M.K. Khokha, D. Hsu, L.J. Brunet, M.S. Dionne, and R.M. Harland Gremlin is the BMP antagonist required for maintenance of Shh and Fgf signals during limb patterning Nat. Genet. 34 2003 303 307
28. A. Zuniga, O. Michos, F. Spitz, A.P. Haramis, L. Panman, A. Galli, K. Vintersten, C. Klasen, W. Mansfield, S. Kuc, D. Duboule, R. Dono, and R. Zeller Mouse limb deformity mutations disrupt a global control region within the large regulatory landscape required for Gremlin expression Genes Dev. 18 2004 1553 1564
29. J. Peng, B.J. Wallar, A. Flanders, P.J. Swiatek, and A.S. Alberts Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42 Curr. Biol. 13 2003 534 545