Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub.
The Arp2/3 complex is critical for nucleation and crosslinking of actin filaments. To gain insight into its subunit topology and assembly pathway, we systematically examined interactions among subunits of human Arp2/3 complex by yeast two-hybrid assays. It was shown that p20-Arc was able to interact with p21-Arc, p34-Arc, and p16-Arc, respectively. In contrast, p41-Arc only interacted with p20-Arc/p16-Arc heterodimer. In addition, we found that structural integrity was important for association between p20-Arc and p21-Arc, while the N-terminal half of p34-Arc was dispensable for its binding to p20-Arc. Our data suggest a key role of p20-Arc and a multistep pathway for the complex formation.[1]References
- Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub. Zhao, X., Yang, Z., Qian, M., Zhu, X. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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