| http://purl.uniprot.org/citations/15262991 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15262991 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15262991 | http://www.w3.org/2000/01/rdf-schema#comment | "Ankyrin-B is a spectrin-binding protein that is required for localization of inositol 1,4,5-trisphosphate receptor and ryanodine receptor in neonatal cardiomyocytes. This work addresses the interaction between ankyrin-B and beta(2)-spectrin in these cells. Ankyrin-B and beta(2)-spectrin are colocalized in an intracellular striated compartment overlying the M-line and distinct from T-tubules, sarcoplasmic reticulum, Golgi, endoplasmic reticulum, lysosomes, and endosomes. Beta(2)-Spectrin is absent in ankyrin-B-null cardiomyocytes and is restored to a normal striated pattern by rescue with green fluorescent protein-220-kDa ankyrin-B. We identified two mutants (A1000P and DAR976AAA) located in the ZU5 domain which eliminate spectrin binding activity of ankyrin-B. Ankyrin-B mutants lacking spectrin binding activity are normally targeted but do not reestablish beta(2)-spectrin in ankyrin-B(+/-) cardiomyocytes. However, both mutant forms of ankyrin-B are still capable of restoring inositol 1,4,5-trisphosphate receptor localization and normal contraction frequency of cardiomyocytes. Therefore, direct binding of beta(2)-spectrin to ankyrin-B is required for the normal targeting of beta(2)-spectrin in neonatal cardiomyocytes. In contrast, ankyrin-B localization and function are independent of beta(2)-spectrin. In summary, this work demonstrates that interaction between members of the ankyrin and beta-spectrin families previously established in erythrocytes and axon initial segments also occurs in neonatal cardiomyocytes with ankyrin-B and beta(2)-spectrin. This work also establishes a functional hierarchy in which ankyrin-B determines the localization of beta(2)-spectrin and operates independently of beta(2)-spectrin in its role in organizing membrane-spanning proteins."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m406018200"xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m406018200"xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/author | "Bennett V."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/author | "Bennett V."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/author | "Yoon W."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/author | "Yoon W."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/author | "Mohler P.J."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/author | "Mohler P.J."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/pages | "40185-40193"xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/pages | "40185-40193"xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/title | "Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/title | "Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes."xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15262991 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15262991 |
| http://purl.uniprot.org/citations/15262991 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15262991 |
| http://purl.uniprot.org/citations/15262991 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15262991 |
| http://purl.uniprot.org/citations/15262991 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15262991 |