Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 26 March 2004:
Vol. 303. no. 5666, pp. 2007 - 2010
DOI: 10.1126/science.1093923
Prev | Table of Contents | Next

Reports

Actin Polymerization-Driven Molecular Movement of mDia1 in Living Cells

Chiharu Higashida,1 Takushi Miyoshi,1 Akiko Fujita,1 Fabian Oceguera-Yanez,1 James Monypenny,1 Yoshikazu Andou,1 Shuh Narumiya,1 Naoki Watanabe1,2*

mDia1, a Rho effector, belongs to the Formin family of proteins, which shares the conserved tandem FH1-FH2 unit structure. Formins including mDia1 accelerate actin nucleation while interacting with actin filament fast-growing ends. Here our single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells. The movement of mDia1 FH1-FH2 was blocked by actin-perturbing drugs, and the speed of mDia1 FH1-FH2 movement appeared to correlate with actin elongation rates. In vitro, mDia1 FH1-FH2 associated persistently with the growing actin barbed end. mDia1 probably moves processively along the growing end of actin filaments in cells, and Formins may be a molecular motility machinery that is independent from motor proteins.

1 Department of Pharmacology, Kyoto University Faculty of Medicine, Yoshida Konoe-cho, Sakyo-ku, Kyoto, Japan.
2 PRESTO, Japan Science and Technology Agency, 4-1-8 Honcho Kawaguchi, Saitama, Japan.

* To whom correspondence should be addressed. E-mail: naoki-w{at}mfour.med.kyoto-u.ac.jp

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Energetic Requirements for Processive Elongation of Actin Filaments by FH1FH2-formins.
A. S. Paul and T. D. Pollard (2009)
J. Biol. Chem. 284, 12533-12540
   Abstract »    Full Text »    PDF »
Diaphanous-Related Formins Are Required for Invadopodia Formation and Invasion of Breast Tumor Cells.
F. Lizarraga, R. Poincloux, M. Romao, G. Montagnac, G. Le Dez, I. Bonne, G. Rigaill, G. Raposo, and P. Chavrier (2009)
Cancer Res. 69, 2792-2800
   Abstract »    Full Text »    PDF »
Imatinib Mesylate (STI571)-Induced Cell Edge Translocation of Kinase-Active and Kinase-Defective Abelson Kinase: Requirements of Myristoylation and src Homology 3 Domain.
A. Fujita, T. Shishido, Y. Yuan, E. Inamoto, S. Narumiya, and N. Watanabe (2009)
Mol. Pharmacol. 75, 75-84
   Abstract »    Full Text »    PDF »
Specificity of Interactions between mDia Isoforms and Rho Proteins.
M. Lammers, S. Meyer, D. Kuhlmann, and A. Wittinghofer (2008)
J. Biol. Chem. 283, 35236-35246
   Abstract »    Full Text »    PDF »
Shootin1 interacts with actin retrograde flow and L1-CAM to promote axon outgrowth.
T. Shimada, M. Toriyama, K. Uemura, H. Kamiguchi, T. Sugiura, N. Watanabe, and N. Inagaki (2008)
J. Cell Biol. 181, 817-829
   Abstract »    Full Text »    PDF »
G-actin regulates rapid induction of actin nucleation by mDia1 to restore cellular actin polymers.
C. Higashida, S. Suetsugu, T. Tsuji, J. Monypenny, S. Narumiya, and N. Watanabe (2008)
J. Cell Sci. 121, 3403-3412
   Abstract »    Full Text »    PDF »
The formin mDia2 stabilizes microtubules independently of its actin nucleation activity.
F. Bartolini, J. B. Moseley, J. Schmoranzer, L. Cassimeris, B. L. Goode, and G. G. Gundersen (2008)
J. Cell Biol. 181, 523-536
   Abstract »    Full Text »    PDF »
Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers.
H. Y. Kueh, G. T. Charras, T. J. Mitchison, and W. M. Brieher (2008)
J. Cell Biol. 182, 341-353
   Abstract »    Full Text »    PDF »
Regulation and Targeting of the Fission Yeast Formin cdc12p in Cytokinesis.
A. Yonetani, R. J. Lustig, J. B. Moseley, T. Takeda, B. L. Goode, and F. Chang (2008)
Mol. Biol. Cell 19, 2208-2219
   Abstract »    Full Text »    PDF »
Crystal structure of human DAAM1 formin homology 2 domain..
M. Yamashita, T. Higashi, S. Suetsugu, Y. Sato, T. Ikeda, R. Shirakawa, T. Kita, T. Takenawa, H. Horiuchi, S. Fukai, et al. (2007)
Genes Cells 12, 1255-1265
   Abstract »    Full Text »    PDF »
mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration.
S. L. Gupton, K. Eisenmann, A. S. Alberts, and C. M. Waterman-Storer (2007)
J. Cell Sci. 120, 3475-3487
   Abstract »    Full Text »    PDF »
Impaired T lymphocyte trafficking in mice deficient in an actin-nucleating protein, mDia1.
D. Sakata, H. Taniguchi, S. Yasuda, A. Adachi-Morishima, Y. Hamazaki, R. Nakayama, T. Miki, N. Minato, and S. Narumiya (2007)
J. Exp. Med. 204, 2031-2038
   Abstract »    Full Text »    PDF »
Yeast Formins Bni1 and Bnr1 Utilize Different Modes of Cortical Interaction during the Assembly of Actin Cables.
S. M. Buttery, S. Yoshida, and D. Pellman (2007)
Mol. Biol. Cell 18, 1826-1838
   Abstract »    Full Text »    PDF »
How ATP Hydrolysis Controls Filament Assembly from Profilin-Actin: IMPLICATION FOR FORMIN PROCESSIVITY.
S. Romero, D. Didry, E. Larquet, N. Boisset, D. Pantaloni, and M.-F. Carlier (2007)
J. Biol. Chem. 282, 8435-8445
   Abstract »    Full Text »    PDF »
RhoA-Dependent Vascular Smooth Muscle Cell-Specific Transcription: Adding Diaphanous Formins to the Puzzle.
E. Larsson, X. Zhou, and L. M. Akyurek (2007)
Arterioscler. Thromb. Vasc. Biol. 27, 448-449
   Full Text »    PDF »
Agrin and laminin induce acetylcholine receptor clustering by convergent, Rho GTPase-dependent signaling pathways.
C. A. Weston, G. Teressa, B. S. Weeks, and J. Prives (2007)
J. Cell Sci. 120, 868-875
   Abstract »    Full Text »    PDF »
Diaphanous 1 and 2 Regulate Smooth Muscle Cell Differentiation by Activating the Myocardin-Related Transcription Factors.
D. P. Staus, A. L. Blaker, J. M. Taylor, and C. P. Mack (2007)
Arterioscler. Thromb. Vasc. Biol. 27, 478-486
   Abstract »    Full Text »    PDF »
Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing.
T. Miyoshi, T. Tsuji, C. Higashida, M. Hertzog, A. Fujita, S. Narumiya, G. Scita, and N. Watanabe (2006)
J. Cell Biol. 175, 947-955
   Abstract »    Full Text »    PDF »
Reassembly of contractile actin cortex in cell blebs.
G. T. Charras, C.-K. Hu, M. Coughlin, and T. J. Mitchison (2006)
J. Cell Biol. 175, 477-490
   Abstract »    Full Text »    PDF »
Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1.
W. M. Brieher, H. Y. Kueh, B. A. Ballif, and T. J. Mitchison (2006)
J. Cell Biol. 175, 315-324
   Abstract »    Full Text »    PDF »
The Yeast Actin Cytoskeleton: from Cellular Function to Biochemical Mechanism.
J. B. Moseley and B. L. Goode (2006)
Microbiol. Mol. Biol. Rev. 70, 605-645
   Abstract »    Full Text »    PDF »
The Rho-mDia1 Pathway Regulates Cell Polarity and Focal Adhesion Turnover in Migrating Cells through Mobilizing Apc and c-Src..
N. Yamana, Y. Arakawa, T. Nishino, K. Kurokawa, M. Tanji, R. E. Itoh, J. Monypenny, T. Ishizaki, H. Bito, K. Nozaki, et al. (2006)
Mol. Cell. Biol. 26, 6844-6858
   Abstract »    Full Text »    PDF »
The bundling activity of vasodilator-stimulated phosphoprotein is required for filopodium formation.
A. Schirenbeck, R. Arasada, T. Bretschneider, T. E. B. Stradal, M. Schleicher, and J. Faix (2006)
PNAS 103, 7694-7699
   Abstract »    Full Text »    PDF »
Stress fibers are generated by two distinct actin assembly mechanisms in motile cells.
P. Hotulainen and P. Lappalainen (2006)
J. Cell Biol. 173, 383-394
   Abstract »    Full Text »    PDF »
Biochemical Characterization of the Diaphanous Autoregulatory Interaction in the Formin Homology Protein FHOD1.
A. Schonichen, M. Alexander, J. E. Gasteier, F. E. Cuesta, O. T. Fackler, and M. Geyer (2006)
J. Biol. Chem. 281, 5084-5093
   Abstract »    Full Text »    PDF »
A novel mechanism of actin filament processive capping by formin: solution of the rotation paradox.
T. Shemesh, T. Otomo, M. K. Rosen, A. D. Bershadsky, and M. M. Kozlov (2005)
J. Cell Biol. 170, 889-893
   Abstract »    Full Text »    PDF »
The Formin Homology 1 Domain Modulates the Actin Nucleation and Bundling Activity of Arabidopsis FORMIN1.
A. Michelot, C. Guerin, S. Huang, M. Ingouff, S. Richard, N. Rodiuc, C. J. Staiger, and L. Blanchoin (2005)
PLANT CELL 17, 2296-2313
   Abstract »    Full Text »    PDF »
Subsecond reorganization of the actin network in cell motility and chemotaxis.
S. Diez, G. Gerisch, K. Anderson, A. Muller-Taubenberger, and T. Bretschneider (2005)
PNAS 102, 7601-7606
   Abstract »    Full Text »    PDF »
Profilin-mediated Competition between Capping Protein and Formin Cdc12p during Cytokinesis in Fission Yeast.
D. R. Kovar, J.-Q. Wu, and T. D. Pollard (2005)
Mol. Biol. Cell 16, 2313-2324
   Abstract »    Full Text »    PDF »
RhoGEF2 and the formin Dia control the formation of the furrow canal by directed actin assembly during Drosophila cellularisation.
J. Grosshans, C. Wenzl, H.-M. Herz, S. Bartoszewski, F. Schnorrer, N. Vogt, H. Schwarz, and H.-A. Muller (2005)
Development 132, 1009-1020
   Abstract »    Full Text »    PDF »
Dissecting Requirements for Auto-inhibition of Actin Nucleation by the Formin, mDia1.
F. Li and H. N. Higgs (2005)
J. Biol. Chem. 280, 6986-6992
   Abstract »    Full Text »    PDF »
The role of the Rho GTPases in neuronal development.
E.-E. Govek, S. E. Newey, and L. Van Aelst (2005)
Genes & Dev. 19, 1-49
   Abstract »    Full Text »    PDF »
Processive capping by formin suggests a force-driven mechanism of actin polymerization.
M. M. Kozlov and A. D. Bershadsky (2004)
J. Cell Biol. 167, 1011-1017
   Abstract »    Full Text »    PDF »
From the Cover: Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces.
D. R. Kovar and T. D. Pollard (2004)
PNAS 101, 14725-14730
   Abstract »    Full Text »    PDF »
Two Distinct Actin Networks Drive the Protrusion of Migrating Cells.
A. Ponti, M. Machacek, S. L. Gupton, C. M. Waterman-Storer, and G. Danuser (2004)
Science 305, 1782-1786
   Abstract »    Full Text »    PDF »
Activation of Endogenous Cdc42 Visualized in Living Cells.
P. Nalbant, L. Hodgson, V. Kraynov, A. Toutchkine, and K. M. Hahn (2004)
Science 305, 1615-1619
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)