http://purl.uniprot.org/citations/26604221 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26604221 | http://www.w3.org/2000/01/rdf-schema#comment | "Cardiolipin (also known as PDL6) is an indispensable lipid required for mitochondrial respiration that is generated through de novo synthesis and remodeling. Here, the cardiolipin remodeling enzyme, acyl-CoA:lysocardiolipin-acyltransferase-1 (Alcat1; SwissProt ID, Q6UWP7) is destabilized in epithelia by lipopolysaccharide (LPS) impairing mitochondrial function. Exposure to LPS selectively decreased levels of carbon 20 (C20)-containing cardiolipin molecular species, whereas the content of C18 or C16 species was not significantly altered, consistent with decreased levels of Alcat1. Alcat1 is a labile protein that is lysosomally degraded by the ubiquitin E3 ligase Skp-Cullin-F-box containing the Fbxo28 subunit (SCF-Fbxo28) that targets Alcat1 for monoubiquitylation at residue K183. Interestingly, K183 is also an acetylation-acceptor site, and acetylation conferred stability to the enzyme. Histone deacetylase 2 (HDAC2) interacted with Alcat1, and expression of a plasmid encoding HDAC2 or treatment of cells with LPS deacetylated and destabilized Alcat1, whereas treatment of cells with a pan-HDAC inhibitor increased Alcat1 levels. Alcat1 degradation was partially abrogated in LPS-treated cells that had been silenced for HDAC2 or treated with MLN4924, an inhibitor of Cullin-RING E3 ubiquitin ligases. Thus, LPS increases HDAC2-mediated Alcat1 deacetylation and facilitates SCF-Fbxo28-mediated disposal of Alcat1, thus impairing mitochondrial integrity."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.176701"xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Jiang J."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Li J."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Lee J.S."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Zhao Y."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Das S."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Ray P."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Ray A."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Zou C."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Xiong S."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Chen B.B."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Kagan V.E."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Tyurina Y.Y."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Mallampalli R.K."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Shiva S."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Manni M.L."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/author | "Synan M.J."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/pages | "51-64"xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/title | "LPS impairs oxygen utilization in epithelia by triggering degradation of the mitochondrial enzyme Alcat1."xsd:string |
http://purl.uniprot.org/citations/26604221 | http://purl.uniprot.org/core/volume | "129"xsd:string |