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pubmed:abstractText |
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.
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pubmed:affiliation |
Shanghai Research Center of Life Sciences and Open Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai, 200031, China.
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