scholarly journals Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry

10.3791/62107 ◽  
2021 ◽  
Author(s):  
Lucia M. Q. Liao ◽  
Rachel A. V. Gray ◽  
Dale D. O. Martin
Keyword(s):  
Fatty Acid ◽  
Click Chemistry ◽  
Acylated Proteins

scholarly journals Molecular basis of fatty acid selectivity in the zDHHC family of S-acyltransferases revealed by click chemistry

2017 ◽  
Vol 114 (8) ◽  
pp. E1365-E1374 ◽  
Author(s):  
Jennifer Greaves ◽  
Kevin R. Munro ◽  
Stuart C. Davidson ◽  
Matthieu Riviere ◽  
Justyna Wojno ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Click Chemistry ◽  
Mammalian Cells ◽  
Transmembrane Domain ◽  
Acyl Chain ◽  
Fatty Acid Selectivity ◽  
Molecular Determinants ◽  
Chain Acyl ◽  
Domain 3 ◽  
Acylated Proteins

S-acylation is a major posttranslational modification, catalyzed by the zinc finger DHHC domain containing (zDHHC) enzyme family. S-acylated proteins can be modified by different fatty acids; however, very little is known about how zDHHC enzymes contribute to acyl chain heterogeneity. Here, we used fatty acid-azide/alkyne labeling of mammalian cells, showing their transformation into acyl-CoAs and subsequent click chemistry-based detection, to demonstrate that zDHHC enzymes have marked differences in their fatty acid selectivity. This difference in selectivity was apparent even for highly related enzymes, such as zDHHC3 and zDHHC7, which displayed a marked difference in their ability to use C18:0 acyl-CoA as a substrate. Furthermore, we identified isoleucine-182 in transmembrane domain 3 of zDHHC3 as a key determinant in limiting the use of longer chain acyl-CoAs by this enzyme. This study uncovered differences in the fatty acid selectivity profiles of cellular zDHHC enzymes and mapped molecular determinants governing this selectivity.

Sustainable thermoplastic elastomers derived from cellulose, fatty acid and furfural via ATRP and click chemistry

2017 ◽  
Vol 176 ◽  
pp. 83-90 ◽  
Author(s):  
Juan Yu ◽  
Chuanwei Lu ◽  
Chunpeng Wang ◽  
Jifu Wang ◽  
Yimin Fan ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Click Chemistry ◽  
Thermoplastic Elastomers

Discovery of novel free fatty acid receptor 1 agonists bearing triazole core via click chemistry

2016 ◽  
Vol 24 (21) ◽  
pp. 5449-5454 ◽  
Author(s):  
Zheng Li ◽  
Jianyong Yang ◽  
Xuekun Wang ◽  
Huilan Li ◽  
Chunxia Liu ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Click Chemistry ◽  
Acid Receptor ◽  
Free Fatty Acid Receptor ◽  
Fatty Acid Receptor

scholarly journals C. Elegans Fatty Acid Two-Hydroxylase Regulates Intestinal Homeostasis by Affecting Heptadecenoic Acid Production

2018 ◽  
Vol 49 (3) ◽  
pp. 947-960 ◽  
Author(s):  
Yuanbao Li ◽  
Chunxia Wang ◽  
Yikai Huang ◽  
Rong Fu ◽  
Hanxi Zheng ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Click Chemistry ◽  
Protein Transport ◽  
Lipid Analysis ◽  
Fatty Acyl ◽  
Intestinal Cells ◽  
Membrane Structures ◽  
C Elegans ◽  
Apical Side

Background/Aims: The hydroxylation of fatty acids at the C-2 position is the first step of fatty acid α-oxidation and generates sphingolipids containing 2-hydroxy fatty acyl moieties. Fatty acid 2-hydroxylation is catalyzed by Fatty acid 2-hydroxylase (FA2H) enzyme. However, the precise roles of FA2H and fatty acid 2-hydroxylation in whole cell homeostasis still remain unclear. Methods: Here we utilize Caenorhabditis elegans as the model and systemically investigate the physiological functions of FATH-1/C25A1.5, the highly conserved worm homolog for mammalian FA2H enzyme. Immunostaining, dye-staining and translational fusion reporters were used to visualize FATH-1 protein and a variety of subcellular structures. The “click chemistry” method was employed to label 2-OH fatty acid in vivo. Global and tissue-specific RNAi knockdown experiments were performed to inactivate FATH-1 function. Lipid analysis of the fath-1 deficient mutants was achieved by mass spectrometry. Results: C. elegans FATH-1 is expressed at most developmental stages and in most tissues. Loss of fath-1 expression results in severe growth retardation and shortened lifespan. FATH-1 function is crucially required in the intestine but not the epidermis with stereospecificity. The “click chemistry” labeling technique showed that the FATH-1 metabolites are mainly enriched in membrane structures preferable to the apical side of the intestinal cells. At the subcellular level, we found that loss of fath-1 expression inhibits lipid droplets formation, as well as selectively disrupts peroxisomes and apical endosomes. Lipid analysis of the fath-1 deficient animals revealed a significant reduction in the content of heptadecenoic acid, while other major FAs remain unaffected. Feeding of exogenous heptadecenoic acid (C17: 1), but not oleic acid (C18: 1), rescues the global and subcellular defects of fath-1 knockdown worms. Conclusion: Our study revealed that FATH-1 and its catalytic products are highly specific in the context of chirality, C-chain length, spatial distribution, as well as the types of cellular organelles they affect. Such an unexpected degree of specificity for the synthesis and functions of hydroxylated FAs helps to regulate protein transport and fat metabolism, therefore maintaining the cellular homeostasis of the intestinal cells. These findings may help our understanding of FA2H functions across species, and offer potential therapeutical targets for treating FA2H-related diseases.

scholarly journals Two classes of fatty acid acylated proteins exist in eukaryotic cells.

1985 ◽  
Vol 4 (5) ◽  
pp. 1137-1144 ◽  
Author(s):  
A.I. Magee ◽  
S.A. Courtneidge
Keyword(s):  
Fatty Acid ◽  
Eukaryotic Cells ◽  
Acylated Proteins

Tracing Fatty Acid Metabolism by Click Chemistry

2012 ◽  
Vol 7 (12) ◽  
pp. 2004-2011 ◽  
Author(s):  
Christoph Thiele ◽  
Cyrus Papan ◽  
Dominik Hoelper ◽  
Kalina Kusserow ◽  
Anne Gaebler ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Click Chemistry ◽  
Fatty Acid Metabolism ◽  
Acid Metabolism

African swine fever virus fatty acid acylated proteins

Virology ◽  
1991 ◽  
Vol 185 (2) ◽  
pp. 942-945 ◽  
Author(s):  
Begoña Aguado ◽  
Eladio Vañuela ◽  
Antonio Alcamí
Keyword(s):  
Fatty Acid ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Acylated Proteins

scholarly journals Fatty Acid Acylated Proteins of the Halotolerant Alga Dunaliella salina

1989 ◽  
Vol 90 (2) ◽  
pp. 549-552 ◽  
Author(s):  
Martha Stephenson ◽  
Phillip E. Ryals ◽  
Guy A. Thompson
Keyword(s):  
Fatty Acid ◽  
Dunaliella Salina ◽  
Acylated Proteins
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