DOI: 10.1016/j.cell.2005.11.038. Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin

Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin

10.1016/j.cell.2005.11.038

Crossref journal-article

Elsevier BV

Cell (78)

Bibliography

Kovar, D. R., Harris, E. S., Mahaffy, R., Higgs, H. N., & Pollard, T. D. (2006). Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin. Cell, 124(2), 423â435.

Authors 5

David R. Kovar (first)
Elizabeth S. Harris (additional)
Rachel Mahaffy (additional)
Henry N. Higgs (additional)
Thomas D. Pollard (additional)

References 32 Referenced 508

10.1073/pnas.211556398 / Proc. Natl. Acad. Sci. USA / Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy by Amann (2001)
10.1021/bi011214b / Biochemistry / Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin by Blanchoin (2002)
10.1083/jcb.137.1.169 / J. Cell Biol. / cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin by Chang (1997)
10.1016/S0021-9258(18)67157-1 / J. Biol. Chem. / Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules by Drenckhahn (1986)
10.1038/ncb718 / Nat. Cell Biol. / Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast by Evangelista (2002)
10.1016/S0960-9822(01)00525-5 / Curr. Biol. / Roles of the fission yeast formin for3p in cell polarity, actin cable formation, and symmetric cell division by Feierbach (2001)
10.1074/jbc.M312718200 / J. Biol. Chem. / The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments by Harris (2004)
10.1126/science.1093923 / Science / Actin polymerization-driven molecular movement of mDia1 in living cells by Higashida (2004)
10.1091/mbc.E04-07-0565 / Mol. Biol. Cell / Phylogenetic analysis of the formin homology 2 domain by Higgs (2005)
10.1038/ncb1075 / Nat. Cell Biol. / Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables by Kobielak (2004)
10.1073/pnas.0405902101 / Proc. Natl. Acad. Sci. USA / Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces by Kovar (2004)
10.1083/jcb.200211078 / J. Cell Biol. / The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin by Kovar (2003)
10.1091/mbc.E04-09-0781 / Mol. Biol. Cell / Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast by Kovar (2005)
10.1529/biophysj.104.047399 / Biophys. J. / Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy by Kuhn (2005)
10.1016/S0960-9822(03)00540-2 / Curr. Biol. / The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition by Li (2003)
10.1091/mbc.E03-08-0621 / Mol. Biol. Cell / A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin by Moseley (2004)
10.1038/nature03251 / Nature / Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain by Otomo (2005)
10.1016/j.cub.2005.01.011 / Curr. Biol. / The Rho family GTPase Rif induces filopodia through mDia2 by Pellegrin (2005)
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10.1021/bi026520j / Biochemistry / Mechanism of formin-induced nucleation of actin filaments by Pring (2003)
10.1126/science.1072309 / Science / Role of formins in actin assembly: nucleation and barbed-end association by Pruyne (2002)
10.1016/j.cell.2004.09.039 / Cell / Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis by Romero (2004)
10.1038/ncb719 / Nat. Cell Biol. / Yeast formins regulate cell polarity by controlling the assembly of actin cables by Sagot (2002)
10.1038/ncb834 / Nat. Cell Biol. / An actin nucleation mechanism mediated by Bni1 and profilin by Sagot (2002)
10.1083/jcb.200504156 / J. Cell Biol. / A novel mechanism of actin filament processive capping by formin: solution of the rotation paradox by Shemesh (2005)
10.1038/ncb1266 / Nat. Cell Biol. / The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia by Schirenbeck (2005)
10.1038/365810a0 / Nature / The structure of crystalline profilin-beta-actin by Schutt (1993)
10.1016/S0960-9822(02)01355-6 / Curr. Biol. / A formin homology protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans by Severson (2002)
10.1016/j.molcel.2006.01.016 / Mol. Cell / Model of formin-associated actin filament elongation by Vavylonis (2006)
10.1021/bi980093l / Biochemistry / Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin by Vinson (1998)
10.1016/S0092-8674(04)00210-7 / Cell / Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture by Xu (2004)
10.1016/j.cub.2003.09.057 / Curr. Biol. / Formin leaky cap allows elongation in the presence of tight capping proteins by Zigmond (2003)

Dates

Type	When
Created	19 years, 7 months ago (Jan. 27, 2006, 11:35 a.m.)
Deposited	4 years, 1 month ago (July 23, 2021, 4:46 a.m.)
Indexed	4 weeks, 2 days ago (Aug. 3, 2025, 7:05 p.m.)
Issued	19 years, 8 months ago (Jan. 1, 2006)
Published	19 years, 8 months ago (Jan. 1, 2006)
Published Print	19 years, 8 months ago (Jan. 1, 2006)

Funders 0

None

BibTeX

@article{Kovar_2006, title={Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin}, volume={124}, ISSN={0092-8674}, url={http://dx.doi.org/10.1016/j.cell.2005.11.038}, DOI={10.1016/j.cell.2005.11.038}, number={2}, journal={Cell}, publisher={Elsevier BV}, author={Kovar, David R. and Harris, Elizabeth S. and Mahaffy, Rachel and Higgs, Henry N. and Pollard, Thomas D.}, year={2006}, month=jan, pages={423–435} }

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