ArticleProceedings of the National Academy of Sciences of the United States of America2009
The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- New targets for cancer promotion and therapy in gliomas: Scinderin.World journal of clinical oncology · 2024Article
- Studies of functional properties of espin 1: Its interaction to actin filaments.Frontiers in cell and developmental biology · 2022Article
- Article
- Scinderin-knockdown inhibits proliferation and promotes apoptosis in human breast carcinoma cells.Oncology letters · 2018Article
- Loss of scinderin decreased expression of epidermal growth factor receptor and promoted apoptosis of castration-resistant prostate cancer cells.FEBS open bio · 2018Article
- The evolution of Sex-linked barring alleles in chickens involves both regulatory and coding changes in CDKN2A.PLoS genetics · 2017Article
- Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Adseverin mediates RANKL-induced osteoclastogenesis by regulating NFATc1.Experimental & molecular medicine · 2015Article
- Calcium-controlled conformational choreography in the N-terminal half of adseverin.Nature communications · 2015Article
- Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin.Nature communications · 2014Article
- Article
- Transcriptome analysis of newt lens regeneration reveals distinct gradients in gene expression patterns.PloS one · 2013Article
- Novel actin-like filament structure from Clostridium tetani.The Journal of biological chemistry · 2012Article
- Adseverin: a novel cisplatin-resistant marker in the human bladder cancer cell line HT1376 identified by quantitative proteomic analysis.Molecular oncology · 2012Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Adseverin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins. Adseverin comprises 6 homologous domains (A1-A6), which share 60% identity with the 6 domains from gelsolin (G1-G6). Adseverin is truncated in comparison to gelsolin, lacking the C-terminal extension that masks the F-actin binding site in calcium-free gelsolin. Biochemical assays have indicated differences in the interaction of the C-terminal halves of adseverin and gelsolin with actin. Gelsolin contacts actin through a major site on G4 and a minor site on G6, whereas adseverin uses a site on A5. Here, we present the X-ray structure of the activated C-terminal half of adseverin (A4-A6). This structure is highly similar to that of the activated form of the C-terminal half of gelsolin (G4-G6), both in arrangement of domains and in the 3 bound calcium ions. Comparative analysis of the actin-binding surfaces observed in the G4-G6/actin structure suggests that adseverin in this conformation will also be able to interact with actin through A4 and A6, whereas the A5 surface is obscured. A single residue mutation in A4-A6 located at the predicted A4/actin interface completely abrogates actin sequestration. A model of calcium-free adseverin, constructed from the structure of gelsolin, predicts that in the absence of a gelsolin-like C-terminal extension the interaction between A2 and A6 provides the steric inhibition to prevent interaction with F-actin. We propose that calcium binding to the N terminus of adseverin dominates the activation process to expose the F-actin binding site on A2.
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