| http://purl.uniprot.org/citations/10588661 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10588661 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10588661 | http://www.w3.org/2000/01/rdf-schema#comment | "The espins are actin-binding and -bundling proteins localized to parallel actin bundles. The 837-amino-acid "espin" of Sertoli cell-spermatid junctions (ectoplasmic specializations) and the 253-amino-acid "small espin" of brush border microvilli are splice isoforms that share a C-terminal 116-amino-acid actin-bundling module but contain different N termini. To investigate the roles of espin and its extended N terminus, we examined the actin-binding and -bundling properties of espin constructs and the stoichiometry and developmental accumulation of espin within the ectoplasmic specialization. An espin construct bound to F-actin with an approximately threefold higher affinity (K(d) = approximately 70 nM) than small espin and was approximately 2.5 times more efficient at forming bundles. The increased affinity appeared to be due to an additional actin-binding site in the N terminus of espin. This additional actin-binding site bound to F-actin with a K(d) of approximately 1 microM, decorated actin stress fiber-like structures in transfected cells, and was mapped to a peptide between the two proline-rich peptides in the N terminus of espin. Espin was detected at approximately 4-5 x 10(6) copies per ectoplasmic specialization, or approximately 1 espin per 20 actin monomers and accumulated there coincident with the formation of parallel actin bundles during spermiogenesis. These results suggest that espin is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.10.12.4327"xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.10.12.4327"xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Chen B."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Chen B."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Li A."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Li A."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Wang M."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Wang M."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Zheng L."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Zheng L."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Bartles J.R."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/author | "Bartles J.R."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/pages | "4327-4339"xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/pages | "4327-4339"xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/title | "Espin contains an additional actin-binding site in its N terminus and is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization junctional plaque."xsd:string |
| http://purl.uniprot.org/citations/10588661 | http://purl.uniprot.org/core/title | "Espin contains an additional actin-binding site in its N terminus and is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization junctional plaque."xsd:string |