| http://purl.uniprot.org/citations/32108178 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32108178 | http://www.w3.org/2000/01/rdf-schema#comment | "Glycine N-myristoylation is an essential acylation modification modulating the functions, stability, and membrane association of diverse cytosolic proteins in human cells. Myristoyl-CoA is the 14-carbon acyl donor of the acyltransferase reaction. Acyl-CoAs of a chain length compatible with the binding site of the N-myristoyltransferase enzymes (NMT) are competitive inhibitors, and the mechanism protecting these enzymes from unwanted acyl-CoA species requires the acyl-CoA binding protein ACBD6. The acyl-CoA binding domain (ACB) and the ankyrin-repeat motifs (ANK) of ACBD6 can perform their functions independently. Interaction of ANK with human NMT2 was necessary and sufficient to provide protection. Fusion of the ANK module to the acyl-CoA binding protein ACBD1 was sufficient to confer the NMT-stimulatory property of ACBD6 to the chimera. The ACB domain is dispensable and sequestration of the competitor was not the basis for NMT2 protection. Acyl-CoAs bound to ACB modulate the function of the ANK module and act as positive effector of the allosteric activation of the enzyme. The functional relevance of homozygous mutations in ACBD6 gene, which have not been associated with a disease so far, is presented. Skin-derived fibroblasts of two unrelated individuals with neurodevelopmental disorder and carrying loss of function mutations in the ACBD6 gene were deficient in protein N-myristoylation. These cells were sensitive to substrate analog competing for myristoyl-CoA binding to NMT. These findings account for the requirement of an ANK-containing acyl-CoA binding protein in the cellular mechanism protecting the NMT enzymes and establish that in human cells, ACBD6 supports the N-myristoylation of proteins."xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0229718"xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/author | "Kuypers F.A."xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/author | "Soupene E."xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/author | "Schatz U.A."xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/author | "Rudnik-Schoneborn S."xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/pages | "e0229718"xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/title | "Requirement of the acyl-CoA carrier ACBD6 in myristoylation of proteins: Activation by ligand binding and protein interaction."xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://purl.uniprot.org/core/volume | "15"xsd:string |
| http://purl.uniprot.org/citations/32108178 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32108178 |
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| http://purl.uniprot.org/uniprot/#_Q9BR61-mappedCitation-32108178 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32108178 |
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