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ProteomicsA bioorthogonal chemical reporter for fatty acid synthase-dependent protein acylation
Mammalian fatty acid synthase (FASN) is a lipogenic enzyme that catalyzes the formation of the long chain saturated fatty acid palmitate from acetyl and malonyl CoA in the presence of NADPH. Mammalian cells acquire fatty acids through dietary sources or through FASN. Although most mammalian cells ex...
ORGANISM(S): Homo sapiens (Human) 
2022-02-15 | PXD028244 | Pride
Fatty acid synthase N-myristoylation Protein acylation Click chemistry S-palmitoylation 
ProteomicsDirect analysis of IFITM3 S-fatty-acylation, part 2
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and anothe...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008401 | Pride
Ifitm3 S-fatty-acylation Site identification S-palmitoylation 
ProteomicsDirect analysis of IFITM3 S-fatty-acylation, part 1
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and another ...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008400 | Pride
Post translational modifications Modification site identification S-fatty-acylation Ifitm3 S-palmitoylation 
ProteomicsSelection of the length of fatty acyl chain and of the acylation site by the acyltransferase governs activation of RTX toxins
Numerous proteins synthesized in cells ranging from bacteria to humans have to be posttranslationally acylated to become biologically active. Bacterial Repeats in ToXin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo a posttranslational acyl...
ORGANISM(S): Escherichia coli Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2020-05-20 | PXD018859 | Pride
Fatty acyl Rtx toxin Acyltransferase Acylation Cytotoxicity 
ProteomicsQuantitative proteomics characterization of proteins modified by very long chain fatty acids (VLCFAs) under necroptosis
Necroptosis is a caspase-independent form of regulated cell death that is characterized by membrane permeabilization and rupture. This membrane rupture is responsible for the inflammatory properties of necroptosis and is critical for disease states involving this process. In efforts to understand ho...
ORGANISM(S): Homo sapiens (Human) 
2021-05-25 | PXD022527 | Pride
Ionstar proteomics acylation necroptosis 
ProteomicsDirect identification of protein S-palmitoylation sites
S-fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryot...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008399 | Pride
S-palmitoylation Site identification S-fatty-acylation 
ProteomicsLysine long-chain fatty acylation regulates the TEAD transcription factor
TEAD transcription factors are responsible for the transcriptional output of Hippo signalling1,2. TEAD activity is primarily regulated by phosphorylation of its coactivators YAP and TAZ3,4. In addition, cysteine palmitoylation has recently been shown to regulate TEAD activity5,6. Here, we report lys...
ORGANISM(S): Homo sapiens (Human) 
2023-03-19 | PXD033939 | Pride
Tead acylation 
UnknownMetabolic transitions regulate global protein fatty acylation.
Not available
S-EPMC10808961 | biostudies-literature
UnknownLysine Fatty Acylation: Regulatory Enzymes, Research Tools, and Biological Function.
Not available
S-EPMC8339906 | biostudies-literature
UnknownBioorthogonal pro-metabolites for profiling short chain fatty acylation.
Not available
S-EPMC5885804 | biostudies-literature
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