Actin cytoskeleton: Formins lead the way

Current Biology

Volumn 14, Issue 13, 2004, Pages

  Harris, E S ^a   Higgs, H N ^a  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA;

EID: 3142530596     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2004.06.043     Document Type: Review

References (15)

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2. Wallar B.J., Alberts A.S. The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13:2003;435-446
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4. Zigmond S.H., Evangelista M., Boone C., Yang C., Dar A.C., Sicheri F., Forkey J., Pring M. Formin leaky cap allows elongation in the presence of tight capping proteins. Curr. Biol. 13:2003;1820-1823
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6. Xu Y., Moseley J., Sagot I., Poy F., Pellman D., Goode B.L., Eck M.J. Crystal Structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell. 116:2004;711-723
7. Harris E.S., Li F., Higgs H.N. The mouse formin, FRLa, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. J. Biol. Chem. 279:2004;20076-20087
8. Wear M.A., Yamashita A., Kim K., Maeda Y., Cooper J.A. How capping protein bind the barbed end of the actin filament. Curr. Biol. 13:2003;1531-1537
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