| http://purl.uniprot.org/citations/23355471 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23355471 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23355471 | http://www.w3.org/2000/01/rdf-schema#comment | "Dematin (band 4.9) is an F-actin binding and bundling protein best known for its role within red blood cells, where it both stabilizes as well as attaches the spectrin/actin cytoskeleton to the erythrocytic membrane. Here, we investigate the structural consequences of phosphorylating serine 381, a covalent modification that turns off F-actin bundling activity. In contrast to the canonical doctrine, in which phosphorylation of an intrinsically disordered region/protein confers affinity for another domain/protein, we found the converse to be true of dematin: phosphorylation of the well folded C-terminal villin-type headpiece confers affinity for its intrinsically disordered N-terminal core domain. We employed analytical ultracentrifugation to demonstrate that dematin is monomeric, in contrast to the prevailing view that it is trimeric. Next, using a series of truncation mutants, we verified that dematin has two F-actin binding sites, one in the core domain and the other in the headpiece domain. Although the phosphorylation-mimicking mutant, S381E, was incapable of bundling microfilaments, it retains the ability to bind F-actin. We found that a phosphorylation-mimicking mutant, S381E, eliminated the ability to bundle, but not bind F-actin filaments. Lastly, we show that the S381E point mutant caused the headpiece domain to associate with the core domain, leading us to the mechanism for cAMP-dependent kinase control of dematin's F-actin bundling activity: when unphosphorylated, dematin's two F-actin binding domains move independent of one another permitting them to bind different F-actin filaments. Phosphorylation causes these two domains to associate, forming a compact structure, and sterically eliminating one of these F-actin binding sites."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m112.438861"xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m112.438861"xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Brown J.W."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Brown J.W."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "McKnight C.J."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "McKnight C.J."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Hatters D.M."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Hatters D.M."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Mok Y.F."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/author | "Mok Y.F."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/pages | "8313-8320"xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/pages | "8313-8320"xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/title | "The allosteric mechanism induced by protein kinase A (PKA) phosphorylation of dematin (band 4.9)."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/title | "The allosteric mechanism induced by protein kinase A (PKA) phosphorylation of dematin (band 4.9)."xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/volume | "288"xsd:string |
| http://purl.uniprot.org/citations/23355471 | http://purl.uniprot.org/core/volume | "288"xsd:string |