DOI: 10.1083/jcb.136.2.331. Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from <i>Acanthamoeba</i>

Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

10.1083/jcb.136.2.331

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography on profilin, consists of seven polypeptides; two actinrelated proteins, Arp2 and Arp3; and five apparently novel proteins, p40, p35, p19, p18, and p14 (Machesky et al., 1994). The complex is homogeneous by hydrodynamic criteria with a Stokes' radius of 5.3 nm by gel filtration, sedimentation coefficient of 8.7 S, and molecular mass of 197 kD by analytical ultracentrifugation. The stoichiometry of the subunits is 1:1:1:1:1:1:1, indicating the purified complex contains one copy each of seven polypeptides. In electron micrographs, the complex has a bilobed or horseshoe shape with outer dimensions of ∼13 × 10 nm, and mathematical models of such a shape and size are consistent with the measured hydrodynamic properties. Chemical cross-linking with a battery of cross-linkers of different spacer arm lengths and chemical reactivities identify the following nearest neighbors within the complex: Arp2 and p40; Arp2 and p35; Arp3 and p35; Arp3 and either p18 or p19; and p19 and p14. By fluorescent antibody staining with anti-p40 and -p35, the complex is concentrated in the cortex of the ameba, especially in linear structures, possibly actin filament bundles, that lie perpendicular to the leading edge. Purified Arp2/3 complex binds actin filaments with a Kd of 2.3 μM and a stoichiometry of approximately one complex molecule per actin monomer. In electron micrographs of negatively stained samples, Arp2/3 complex decorates the sides of actin filaments. EDC/NHS cross-links actin to Arp3, p35, and a low molecular weight subunit, p19, p18, or p14. We propose structural and topological models for the Arp2/3 complex and suggest that affinity for actin filaments accounts for the localization of complex subunits to actinrich regions of Acanthamoeba.

Bibliography

Mullins, R. D., Stafford, W. F., & Pollard, T. D. (1997). Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba. The Journal of Cell Biology, 136(2), 331â343.

Authors 3

R. Dyche Mullins (first)
Walter F. Stafford (additional)
Thomas D. Pollard (additional)

References 35 Referenced 196

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Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 12:47 p.m.)
Deposited	2 years, 1 month ago (July 28, 2023, 6:52 p.m.)
Indexed	3 weeks, 4 days ago (Aug. 5, 2025, 9:04 a.m.)
Issued	28 years, 7 months ago (Jan. 27, 1997)
Published	28 years, 7 months ago (Jan. 27, 1997)
Published Online	28 years, 7 months ago (Jan. 27, 1997)
Published Print	28 years, 7 months ago (Jan. 27, 1997)

Funders 0

None

BibTeX

@article{Mullins_1997, title={Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba}, volume={136}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.136.2.331}, DOI={10.1083/jcb.136.2.331}, number={2}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Mullins, R. Dyche and Stafford, Walter F. and Pollard, Thomas D.}, year={1997}, month=jan, pages={331–343} }

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