| http://purl.uniprot.org/citations/25253725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25253725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25253725 | http://www.w3.org/2000/01/rdf-schema#comment | "S-acylation, the attachment of fatty acids onto cysteine residues, regulates protein trafficking and function and is mediated by a family of zDHHC enzymes. The S-acylation of peripheral membrane proteins has been proposed to occur at the Golgi, catalyzed by an S-acylation machinery that displays little substrate specificity. To advance understanding of how S-acylation of peripheral membrane proteins is handled by Golgi zDHHC enzymes, we investigated interactions between a subset of four Golgi zDHHC enzymes and two S-acylated proteins-synaptosomal-associated protein 25 (SNAP25) and cysteine-string protein (CSP). Our results uncover major differences in substrate recognition and S-acylation by these zDHHC enzymes. The ankyrin-repeat domains of zDHHC17 and zDHHC13 mediated strong and selective interactions with SNAP25/CSP, whereas binding of zDHHC3 and zDHHC7 to these proteins was barely detectable. Despite this, zDHHC3/zDHHC7 could S-acylate SNAP25/CSP more efficiently than zDHHC17, whereas zDHHC13 lacked S-acylation activity toward these proteins. Overall the results of this study support a model in which dynamic intracellular localization of peripheral membrane proteins is achieved by highly selective recruitment by a subset of zDHHC enzymes at the Golgi, combined with highly efficient S-acylation by other Golgi zDHHC enzymes."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e14-06-1169"xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e14-06-1169"xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Grefen C."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Grefen C."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Chamberlain L.H."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Chamberlain L.H."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Lemonidis K."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Lemonidis K."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Sanchez-Perez M.C."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Sanchez-Perez M.C."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Gorleku O.A."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/author | "Gorleku O.A."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/pages | "3870-3883"xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/pages | "3870-3883"xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/title | "The Golgi S-acylation machinery comprises zDHHC enzymes with major differences in substrate affinity and S-acylation activity."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/title | "The Golgi S-acylation machinery comprises zDHHC enzymes with major differences in substrate affinity and S-acylation activity."xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/volume | "25"xsd:string |
| http://purl.uniprot.org/citations/25253725 | http://purl.uniprot.org/core/volume | "25"xsd:string |