both the N and C termini are oriented toward the cytosol and have different catalytic roles. A highly conserved motif, 129YFP131, and a hydrophilic segment exclusive to yeast DGAT2 reside in a long endoplasmic reticulum luminal loop following the first transmembrane domain and play an essential role in enzyme catalysis. The strongly conserved residue His195 within the motif HPHG, which may play a role in the active site of DGAT2, is likely embedded in the membrane
gene MaDGAT encodes one transmembrane region in its 5'-end. MaDGAT without the transmembrane region is still functional. Perhaps the N-terminal transmembrane region in MaDGAT functions only to anchor the enzyme to the endoplasmic reticulum
gene MaDGAT encodes one transmembrane region in its 5'-end. MaDGAT without the transmembrane region is still functional. Perhaps the N-terminal transmembrane region in MaDGAT functions only to anchor the enzyme to the endoplasmic reticulum
DGAT-2 is an integral membrane, it has two transmembrane domains separated by a short loop (about 5-8 amino acids) that extends into the endoplasmic reticulum (ER) lumen. The first transmembrane domain contains an ER targeting signal while the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol
an endoplasmic reticulum (ER) retrieval motif responsible for the steady state localization of DGAT2 protein in the ER is identified near the C-terminus of tung tree DGAT2
the interaction of isoform DGAT2 with lipid droplets is dependent on the C-terminus. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, failed to co-localize with lipid droplets when cells are oleate loaded to stimulate triacylglycerol synthesis
DGAT2 is an integral membrane protein with both the N and C terminus oriented toward the cytosol, the loop between the two transmembrane domains of DGAT2is not exposed to the cytosol
DGAT1 (BnaDGAT1) is a polytopic membrane protein in the endoplasmic reticulum (ER) with its N-terminal domain (residues 1-113) localized to the cytoplasm. Structure model of isozyme DGAT1-a transmembrane and cytosolic domains, overview
DGAT1 (BnaDGAT1) is a polytopic membrane protein in the endoplasmic reticulum (ER) with its N-terminal domain (residues 1-113) localized to the cytoplasm. Structure model of isozyme DGAT1-a transmembrane and cytosolic domains, overview
determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration. Comparison of tissue expression patterns of isozymes GmDGAT1A and GmDGAT2D in nodules, roots, stems, leaves, flowers, pods, and seeds
determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration. Comparison of tissue expression patterns of isozymes GmDGAT1A and GmDGAT2D in nodules, roots, stems, leaves, flowers, pods, and seeds
determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration. Comparison of tissue expression patterns of isozymes GmDGAT1A and GmDGAT2D in nodules, roots, stems, leaves, flowers, pods, and seeds
the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol. Although present in the ER, DGAT2 also co-localizes with lipid droplets
the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol. Although present in the ER, DGAT2 also co-localizes with lipid droplets