ArticleThe Journal of biological chemistry2013
Structural insights into the unusually strong ATPase activity of the AAA domain of the Caenorhabditis elegans fidgetin-like 1 (FIGL-1) protein.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Discovery of the microtubule-severing protein as the target of antifungal compound heat-stable antifungal factor in Fusarium graminearum and rational design of novel inhibitors.Pest management science · 2026Article
- The FLIP-FIGNL1 complex regulates the dissociation of RAD51/DMC1 in homologous recombination and replication fork restart.Nucleic acids research · 2023Article
- The AAA+ ATPase Msp1 is a processive protein translocase with robust unfoldase activity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Microtubule-severing enzymes: From cellular functions to molecular mechanism.The Journal of cell biology · 2018Review
- Motor axon navigation relies on Fidgetin-like 1-driven microtubule plus end dynamics.The Journal of cell biology · 2018Article
- The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding.The EMBO journal · 2017Article
- Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins.Molecular cell · 2017Article
- The Rice AAA-ATPase OsFIGNL1 Is Essential for Male Meiosis.Frontiers in plant science · 2017Article
- Fidgetin-like 1 is a ciliogenesis-inhibitory centrosome protein.Cell cycle (Georgetown, Tex.) · 2016Article
- Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.Journal of molecular biology · 2016Review
- AAA-ATPase FIDGETIN-LIKE 1 and Helicase FANCM Antagonize Meiotic Crossovers by Distinct Mechanisms.PLoS genetics · 2015Article
- An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.Acta crystallographica. Section D, Biological crystallography · 2014Article
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6 authors.
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Abstract
The FIGL-1 (fidgetin like-1) protein is a homolog of fidgetin, a protein whose mutation leads to multiple developmental defects. The FIGL-1 protein contains an AAA (ATPase associated with various activities) domain and belongs to the AAA superfamily. However, the biological functions and developmental implications of this protein remain unknown. Here, we show that the AAA domain of the Caenorhabditis elegans FIGL-1 protein (CeFIGL-1-AAA), in clear contrast to homologous AAA domains, has an unusually high ATPase activity and forms a hexamer in solution. By determining the crystal structure of CeFIGL-1-AAA, we found that the loop linking helices α9 and α10 folds into the short helix α9a, which has an acidic surface and interacts with a positively charged surface of the neighboring subunit. Disruption of this charge interaction by mutagenesis diminishes both the ATPase activity and oligomerization capacity of the protein. Interestingly, the acidic residues in helix α9a of CeFIGL-1-AAA are not conserved in other homologous AAA domains that have relatively low ATPase activities. These results demonstrate that the sequence of CeFIGL-1-AAA has adapted to establish an intersubunit charge interaction, which contributes to its strong oligomerization and ATPase activity. These unique properties of CeFIGL-1-AAA distinguish it from other homologous proteins, suggesting that CeFIGL-1 may have a distinct biological function.
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