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Vol. 9, Issue 4, 841-852, April 1998
*The Salk Institute for Biological Studies, La Jolla California
92037;
The Arp2/3 complex was first purified from Acanthamoeba
castellanii by profilin affinity chromatography. The mechanism
of interaction with profilin was unknown but was hypothesized to be
mediated by either Arp2 or Arp3. Here we show that the Arp2 subunit of
the complex can be chemically cross-linked to the actin-binding site of
profilin. By analytical ultracentrifugation,
rhodamine-labeled profilin binds Arp2/3 complex with a
Kd of 7 µM, an affinity intermediate between the low
affinity of profilin for barbed ends of actin filaments and its high
affinity for actin monomers. These data suggest the barbed end of Arp2
is exposed, but Arp2 and Arp3 are not packed together in the complex
exactly like two actin monomers in a filament. Arp2/3 complex also
cross-links actin filaments into small bundles and isotropic networks,
which are mechanically stiffer than solutions of actin filaments alone.
Arp2/3 complex is concentrated at the leading edge of motile
Acanthamoeba, and its localization is distinct from that
of Johns Hopkins University School of Medicine,
Baltimore Maryland 21205; and
§Johns Hopkins University,
Baltimore Maryland 21218
-actinin, another filament cross-linking protein. Based on
localization and actin filament nucleation and cross-linking
activities, we propose a role for Arp2/3 in determining the structure
of the actin filament network at the leading edge of motile cells.
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