ArticleProtein science : a publication of the Protein Society2009
Dematin exhibits a natively unfolded core domain and an independently folded headpiece domain.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- The Role of Liquid-Liquid Phase Separation in Actin Polymerization.International journal of molecular sciences · 2023Review
- A Plasmid-Based Fluorescence Reporter System for Monitoring Oxidative Damage inSensors (Basel, Switzerland) · 2022Article
- Self-construction of actin networks through phase separation-induced abLIM1 condensates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- abLIM1 constructs non-erythroid cortical actin networks to prevent mechanical tension-induced blebbing.Cell discovery · 2018Article
- Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme.Biochimica et biophysica acta · 2013Article
- An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.Journal of biomolecular structure & dynamics · 2013Article
- The allosteric mechanism induced by protein kinase A (PKA) phosphorylation of dematin (band 4.9).The Journal of biological chemistry · 2013Article
- Headpiece domain of dematin regulates calcium mobilization and signaling in platelets.The Journal of biological chemistry · 2012Article
- Refined views of multi-protein complexes in the erythrocyte membrane.Blood cells, molecules & diseases · 2012Review
- Juxtanodin is an intrinsically disordered F-actin-binding protein.Scientific reports · 2012Article
- Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions.Biophysical reviews · 2010Review
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Abstract
Dematin is an actin-binding protein originally identified in the junctional complex of the erythrocyte plasma membrane, and is present in many nonerythroid cells. Dematin headpiece knockout mice display a spherical red cell phenotype and develop a compensated anemia. Dematin has two domains: a 315-residue, proline-rich "core" domain and a 68-residue carboxyl-terminal villin-type "headpiece" domain. Expression of full-length dematin in E. coli as a GST recombinant protein results in truncation within a proline, glutamic acid, serine, threonine rich region (PEST). Therefore, we designed a mutant construct that replaces the PEST sequence. The modified dematin has high actin binding activity as determined by actin sedimentation assays. Negative stain electron microscopy demonstrates that the modified dematin also exhibits actin bundling activity like that of native dematin. Circular dichroism (CD) and NMR spectral analysis, however, show little secondary structure in the modified dematin. The lack of secondary structure is also observed in native dematin purified from human red blood cells. (15)N-HSQC NMR spectra of modified dematin indicate that the headpiece domain is fully folded whereas the core region is primarily unfolded. Our finding suggests that the core is natively unfolded and may serve as a scaffold to organize the components of the junctional complex.
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