| http://purl.uniprot.org/citations/25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25228691 | http://www.w3.org/2000/01/rdf-schema#comment | "Srv2/CAP is a conserved actin-binding protein with important roles in driving cellular actin dynamics in diverse animal, fungal, and plant species. However, there have been conflicting reports about whether the activities of Srv2/CAP are conserved, particularly between yeast and mammalian homologs. Yeast Srv2 has two distinct functions in actin turnover: its hexameric N-terminal-half enhances cofilin-mediated severing of filaments, while its C-terminal-half catalyzes dissociation of cofilin from ADP-actin monomers and stimulates nucleotide exchange. Here, we dissected the structure and function of mouse CAP1 to better understand its mechanistic relationship to yeast Srv2. Although CAP1 has a shorter N-terminal oligomerization sequence compared with Srv2, we find that the N-terminal-half of CAP1 (N-CAP1) forms hexameric structures with six protrusions, similar to N-Srv2. Further, N-CAP1 autonomously binds to F-actin and decorates the sides and ends of filaments, altering F-actin structure and enhancing cofilin-mediated severing. These activities depend on conserved surface residues on the helical-folded domain. Moreover, N-CAP1 enhances yeast cofilin-mediated severing, and conversely, yeast N-Srv2 enhances human cofilin-mediated severing, highlighting the mechanistic conservation between yeast and mammals. Further, we demonstrate that the C-terminal actin-binding β-sheet domain of CAP1 is sufficient to catalyze nucleotide-exchange of ADP-actin monomers, while in the presence of cofilin this activity additionally requires the WH2 domain. Thus, the structures, activities, and mechanisms of mouse and yeast Srv2/CAP homologs are remarkably well conserved, suggesting that the same activities and mechanisms underlie many of the diverse actin-based functions ascribed to Srv2/CAP homologs in different organisms."xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m114.601765"xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/author | "Goode B.L."xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/author | "Sokolova O."xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/author | "Collins A."xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/author | "Jansen S."xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/author | "Golden L."xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/pages | "30732-30742"xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/title | "Structure and mechanism of mouse cyclase-associated protein (CAP1) in regulating actin dynamics."xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://purl.uniprot.org/core/volume | "289"xsd:string |
| http://purl.uniprot.org/citations/25228691 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25228691 |
| http://purl.uniprot.org/citations/25228691 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25228691 |
| http://purl.uniprot.org/uniprot/#_B1ARS0-mappedCitation-25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/#_P40124-mappedCitation-25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/#_Q3U0U5-mappedCitation-25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/#_Q3UVJ2-mappedCitation-25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/#_Q3UNQ0-mappedCitation-25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/#_P17555-mappedCitation-25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/#_Q3TC53-mappedCitation-25228691 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/P40124 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/Q3TC53 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/25228691 |
| http://purl.uniprot.org/uniprot/Q3UNQ0 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/25228691 |