The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition

Current Biology

Volumn 13, Issue 15, 2003, Pages 1335-1340

  Li, Fang ^a   Higgs, Henry N ^a  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; EUKARYOTA; MURINAE; SACCHAROMYCETALES; SCHIZOSACCHAROMYCES POMBE;

EID: 0043202969     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(03)00540-2     Document Type: Article

References (22)

1. Evangelista, M., Zigmond, S., and Boone, C. (2003). Formins: signaling effectors for assembly and polarization of actin filaments. J. Cell Sci. 116, 2603-2611.
2. Wallar, B.J., and Alberts, A.S. (2003). The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol., in press.
3. Wasserman, S. (1998). FH proteins as cytoskeletal organizers. Trends Cell Biol. 8, 111-115.
4. 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 297, 612-615.
5. Sagot, I., Rodal, A.A., Moseley, J., Goode, B.L., and Pellman, D. (2002). An actin nucleation mechanism mediated by Bni1 and profilin. Nat. Cell Biol. 8, 626-631.
6. Pring, M., Evangelista, M., Boone, C., Yang, C., and Zigmond, S.H. (2003). Mechanism of formin-induced nucleation of actin filaments. Biochemistry 42, 486-496.
7. Kovar, D.R., Kuhn, J.R., Tichy, A.L., and Pollard, T.D. (2003). The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol., 161, 875-887.
8. Alberts, A.S. (2002). Diaphanous-related Formin homology proteins. Curr. Biol. 12, R796.
9. 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.
10. Alberts, A.S. (2001). Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276, 2824-2830.
11. Petrella, E.C., Machesky, L.M., Kaiser, D.A., and Pollard, T.D. (1996). Structural requirements and thermodynamics of the interaction of proline peptides with profilin. Biochemistry 35, 16535-16543.
12. Pollard, T.D., Blanchoin, L., and Mullins, R.D. (2000). Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29, 545-576.
13. Pollard, T.D. (1986). Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103, 2747-2754.
14. Pelham, R.J., and Chang, F. (2002). Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 419, 82-86.
15. Severson, A.F., Baillie, D.L., and Bowerman, B. (2002). A Formin Homology Protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans. Curr. Biol. 12, 2066-2075.
16. Tolliday, N., VerPlank, L., and Li, R. (2002). Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis. Curr. Biol. 12, 1864-1870.
17. Carlier, M.F., and Pantaloni, D. (1988). Binding of phosphate to F-ADP-actin and role of F-ADP-Pi-actin in ATP-actin polymerization. J. Biol. Chem. 263, 817-825.
18. MacLaan-Fletcher, S., and Pollard, T.D. (1980). Mechanism of action of cytochalasin B on actin. Cell 20, 329-341.
19. Watanabe, N., Madaule, P., Reid, T., Ishizaki, T., Watanabe, G., Kakizuka, A., Saito, Y., Nakao, K., Jockusch, B.M., and Narumiya, S. (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.
20. Higgs, H.N., and Pollard, T.D. (2001). Regulation of actin filament formation through Arp2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70, 649-676.
21. Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
22. Zhang, B., and Zheng, Y. (1998). Negative regulation of Rho family GTPases Cdc42 and Rac2 by homodimer formation. J. Biol. Chem. 273, 25728-25733.