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Vol. 14, Issue 7, 2645-2654, July 2003

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Interactions between the Evolutionarily Conserved, Actin-related Protein, Arp11, Actin, and Arp1

D. Mark Eckley ^*, and Trina A. Schroer 

Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218

Submitted January 27, 2003; Revised February 25, 2003; Accepted February 25, 2003
Monitoring Editor: David Drubin

The dynein activator dynactin is a multiprotein complex with distinct microtubule- and cargo-binding domains. The cargo-binding domain contains a short, actin-like filament of the actin-related protein Arp1, a second actin-related protein, Arp11, and conventional actin. The length of this filament is invariant in dynactin isolated from multiple species and tissues, suggesting that activities that regulate Arp1 polymerization are important for dynactin assembly. Arp11 is present in a protein complex localized at the pointed end of the Arp1 minifilament, whereas actin capping protein (CapZ) is present at the barbed end. Either might cooperate with conventional actin to cap Arp1. We tested the ability of Arp11 to interact with conventional actin and found it could coassemble. Like Arp1, cytosolic Arp11 is found only in dynactin, suggesting that Arp11 and free cytosolic actin do not interact significantly. Recombinant Arp11 and Arp1 were demonstrated to interact by coprecipitation. We developed an in vivo assay for Arp11–Arp1 interaction based on previous observations that Arp1 forms filamentous assemblies when overexpressed in cultured cells. Arp11 significantly decreases the formation of these organized Arp1 assemblies. Finally, this assay was used to confirm the identity of a putative Arp11 homolog in Drosophila melanogaster.

^* Current address: McKusick-Nathans Institute of Genetic Medicine, 850 Ross Bldg., 720 Rutland Ave., The Johns Hopkins School of Medicine, Baltimore, MD 21205.

Corresponding author. E-mail address: schroer{at}jhu.edu.

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