Diacylglycerol acyltransferase-2 contains a c-terminal sequence that interacts with lipid droplets
| Autor: | Shanna L. Banman, S. Stone, Pamela J. McFie |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
endocrine system Gene Expression Protein Sorting Signals Endoplasmic Reticulum N-Acetylglucosaminyltransferases complex mixtures Diglycerides 03 medical and health sciences Genes Reporter Lipid droplet Chlorocebus aethiops Animals Humans Amino Acid Sequence Diacylglycerol O-Acyltransferase Molecular Biology Triglycerides Diacylglycerol kinase Chemistry Endoplasmic reticulum technology industry and agriculture Biological Transport Lipid Droplets Cell Biology Lipid Metabolism Subcellular localization eye diseases Monoacylglycerol lipase Luminescent Proteins Protein Transport Transmembrane domain HEK293 Cells 030104 developmental biology Acyltransferase COS Cells Biophysics lipids (amino acids peptides and proteins) mCherry |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1863:1068-1081 |
| ISSN: | 1388-1981 |
| DOI: | 10.1016/j.bbalip.2018.06.008 |
| Popis: | Diacylglycerol acyltranferase-2 (DGAT2) is a resident protein of the endoplasmic reticulum that catalyzes the synthesis of triacylglycerol. When lipid droplet formation is stimulated by incubating cells with fatty acids, DGAT2 becomes concentrated around the surface of cytosolic lipid droplets. Using confocal microscopy and directed mutagenesis, we have identified a 17-amino acid sequence in the C-terminal region of DGAT2 that is necessary and sufficient for targeting DGAT2 to lipid droplets. When this region was deleted, DGAT2 remained in the ER and did not target to lipid droplets. Fusing this sequence to mCherry directed the fluorescent reporter to lipid droplets. Similarly, when the corresponding region of monoacylglycerol acyltransferase-2 (MGAT2) was replaced with this sequence, MGAT2 was also targeted to lipid droplets. Lastly, we demonstrated that DGAT2 in ER membranes is continuous with lipid droplets. We propose a new model whereby DGAT2 remains in the ER during lipid droplet formation via it's transmembrane domains and interacts with nascent lipid droplets via its C-terminal lipid droplet interacting domain as they expand. |
| Databáze: | OpenAIRE |
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