| First Author | Zheng LS | Year | 2014 |
| Journal | FEBS J | Volume | 281 |
| Issue | 20 | Pages | 4622-32 |
| PubMed ID | 25117763 | Mgi Jnum | J:229222 |
| Mgi Id | MGI:5751056 | Doi | 10.1111/febs.12966 |
| Citation | Zheng LS, et al. (2014) Structure and mechanism of the unique C2 domain of Aida. FEBS J 281(20):4622-32 |
| abstractText | Axin interactor, dorsalization-associated (Aida) was identified as a regulatory factor that utilizes its C-terminal region to interact with axis formation inhibitor (Axin). Aida abrogates the Axin-mediated Jun N-terminal kinase activation required for proper dorsalization during zebrafish embryonic development, and thus functions as a proventralization factor. Here, we report the structure of Aida C-terminal fragments, which adopt a conventional C2 domain topology. We also demonstrate that Aida can specifically bind to phosphoinositides in a Ca(2+) -independent manner, and is able to associate with the cell membrane via a novel positively charged surface, namely a basic loop. Mutation of the positively charged patch on the basic loop leads to destabilization of the Aida-membrane association or disruption of the Aida-Axin interaction, resulting in impaired Jun N-terminal kinase inhibition. Together, our findings provide a molecular basis for C2 domain-mediated Aida-membrane and Aida-Axin associations. DATABASE: The atomic coordinates and structure factors of the mouse Aida C2 domain (code: 2QZ5) and the zebrafish Aida C2 domain (code: 2QZQ) have been deposited in the Protein Data Bank (http://www.rcsb.org/) STRUCTURED DIGITAL ABSTRACT: AIDA physically interacts with Axin by anti tag coimmunoprecipitation (View interaction). |
