| http://purl.uniprot.org/citations/11101506 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11101506 | http://www.w3.org/2000/01/rdf-schema#comment | "The assembly of stable cytoskeletal structures from dynamically recycled molecules requires developmental and spatial regulation of protein interactions. In muscle, titin acts as a molecular ruler organizing the actin cytoskeleton via interactions with many sarcomeric proteins, including the crosslinking protein alpha-actinin. An interaction between the C-terminal domain of alpha-actinin and titin Z-repeat motifs targets alpha-actinin to the Z-disk. Here we investigate the cellular regulation of this interaction. alpha-actinin is a rod shaped head-to-tail homodimer. In contrast to C-terminal fragments, full-length alpha-actinin does not bind Z-repeats. We identify a 30-residue Z-repeat homologous sequence between the actin-binding and rod regions of alpha-actinin that binds the C-terminal domain with nanomolar affinity. Thus, Z-repeat binding is prevented by this 'pseudoligand' interaction between the subunits of the alpha-actinin dimer. This autoinhibition is relieved upon binding of the Z-disk lipid phosphatidylinositol-bisphosphate to the actin-binding domain. We suggest that this novel mechanism is relevant to control the site-specific interactions of alpha-actinin during sarcomere assembly and turnover. The intramolecular contacts defined here also constrain a structural model for intrasterical regulation of all alpha-actinin isoforms."xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/19.23.6331"xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://purl.uniprot.org/core/author | "Gautel M."xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://purl.uniprot.org/core/author | "Young P."xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/11101506 | http://purl.uniprot.org/core/name | "EMBO J"xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://purl.uniprot.org/core/pages | "6331-6340"xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://purl.uniprot.org/core/title | "The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism."xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://purl.uniprot.org/core/volume | "19"xsd:string |
| http://purl.uniprot.org/citations/11101506 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11101506 |
| http://purl.uniprot.org/citations/11101506 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11101506 |
| http://purl.uniprot.org/uniprot/#_P35609-mappedCitation-11101506 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11101506 |
| http://purl.uniprot.org/uniprot/#_P12814-mappedCitation-11101506 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11101506 |
| http://purl.uniprot.org/uniprot/#_Q8WZ42-mappedCitation-11101506 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11101506 |
| http://purl.uniprot.org/uniprot/P35609 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11101506 |
| http://purl.uniprot.org/uniprot/Q8WZ42 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11101506 |
| http://purl.uniprot.org/uniprot/P12814 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11101506 |