| http://purl.uniprot.org/citations/21673315 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21673315 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21673315 | http://www.w3.org/2000/01/rdf-schema#comment | "Subcellular localization of the actin-binding transcriptional coactivator MRTF-A is controlled by its interaction with monomeric actin (G-actin). Signal-induced decreases in G-actin concentration reduce MRTF-A nuclear export, leading to its nuclear accumulation, whereas artificial increases in G-actin concentration in resting cells block MRTF-A nuclear import, retaining it in the cytoplasm. This regulation is dependent on three actin-binding RPEL motifs in the regulatory domain of MRTF-A. We describe the structures of pentavalent and trivalent G-actin•RPEL domain complexes. In the pentavalent complex, each RPEL motif and the two intervening spacer sequences bound an actin monomer, forming a compact assembly. In contrast, the trivalent complex lacked the C-terminal spacer- and RPEL-actins, both of which bound only weakly in the pentavalent complex. Cytoplasmic localization of MRTF-A in unstimulated fibroblasts also required binding of G-actin to the spacer sequences. The bipartite MRTF-A nuclear localization sequence was buried in the pentameric assembly, explaining how increases in G-actin concentration prevent nuclear import of MRTF-A. Analyses of the pentavalent and trivalent complexes show how actin loads onto the RPEL domain and reveal a molecular mechanism by which actin can control the activity of one of its binding partners."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.org/dc/terms/identifier | "doi:10.1126/scisignal.2001750"xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.org/dc/terms/identifier | "doi:10.1126/scisignal.2001750"xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "McDonald N.Q."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "McDonald N.Q."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Mouilleron S."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Mouilleron S."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Treisman R."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Treisman R."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Guettler S."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Guettler S."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Langer C.A."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/author | "Langer C.A."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/name | "Sci. Signal."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/name | "Sci. Signal."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/pages | "ra40"xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/pages | "ra40"xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/title | "Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/title | "Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator."xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/volume | "4"xsd:string |
| http://purl.uniprot.org/citations/21673315 | http://purl.uniprot.org/core/volume | "4"xsd:string |