Cellular Motility Driven by Assembly and Disassembly of Actin Filaments
- T. Pollard, G. Borisy
- BiologyCell
- 2003
Molecular mechanisms controlling actin filament dynamics in nonmuscle cells.
- T. Pollard, L. Blanchoin, R. Mullins
- BiologyAnnual Review of Biophysics and Biomolecular…
- 2000
How motile cells regulate actin filament assembly at their leading edge is reviewed, including how Arp2/3 complex is incorporated into the network, and new filaments are capped rapidly, so that activated Arp1/2 complex must be supplied continuously to keep the network growing.
Regulation of actin filament assembly by Arp2/3 complex and formins.
- T. Pollard
- BiologyAnnual Review of Biophysics and Biomolecular…
- 3 May 2007
This review summarizes what is known about the biochemical and biophysical mechanisms that initiate the assembly of actin filaments in cells and focuses on Arp2/3 complex and formins.
Actin, a Central Player in Cell Shape and Movement
- T. Pollard, J. Cooper
- BiologyScience
- 27 November 2009
Comparisons of quantitative measurements of reactions in live cells with computer simulations of mathematical models will help generate meaningful insights and present a summary of the key questions in the field.
Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
- T. Pollard
- BiologyJournal of Cell Biology
- 1 December 1986
I measured the rate of elongation at the barbed and pointed ends of actin filaments by electron microscopy with Limulus sperm acrosomal processes as nuclei to show that the nucleotide composition at or near the end of the growing filament is either the same over this range of growth rates or has no detectable effect on the rate constants.
The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.
- R. Mullins, J. Heuser, T. Pollard
- BiologyProceedings of the National Academy of Sciences…
- 26 May 1998
It is shown that Arp2/3 complex purified from Acanthamoeba caps the pointed ends of actin filaments with high affinity and increases the critical concentration for polymerization at the pointed end from 0.6 to 1.0 microM.
Characterization of two classes of small molecule inhibitors of Arp2/3 complex
- B. Nolen, N. Tomašević, T. Pollard
- BiologyNature
- 2 August 2009
Two classes of small molecules that bind to different sites on the Arp2/3 complex and inhibit its ability to nucleate actin filaments are described and provide a powerful approach for studying the ArP2/ 3 complex in living cells.
Actin and Actin-Binding Proteins.
- T. Pollard
- Biology, ChemistryCold Spring Harbor Perspectives in Biology
- 17 March 2016
This review provides an overview of the properties of actin and shows how dozens of proteins control both the assembly and disassembly of actIn filaments, including nucleotide exchange on actin monomers, polymerization, phosphate dissociation, cap the ends of polymers, cross-link filaments to each other and other cellular components, and sever filaments.
Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis.
- Jian-Qiu Wu, J. Kuhn, D. Kovar, T. Pollard
- BiologyDevelopmental Cell
- 1 November 2003
Counting Cytokinesis Proteins Globally and Locally in Fission Yeast
- Jian-Qiu Wu, T. Pollard
- BiologyScience
- 14 October 2005
Fluorescence measured by microscopy or flow cytometry was directly proportional to protein concentration measured by quantitative immunoblotting, which can be used to measure the global and local concentrations of any fusion protein.
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