differential permeabilization experiments indicate that their N- and C-termini are oriented towards the cytosol. GPAT8 possesses a divergent type of dilysine motif -KK-COOH which only functions effectively when additional upstream residues are included to provide the proper protein context
differential permeabilization experiments indicate that their N- and C-termini are oriented towards the cytosol. GPAT9 possesses a hydrophobic pentapeptide motif (-f-X-X-K/R/D/E-f-, where f are large hydrophobic amino acid residues)
exogenously expressed protein. Isoform GPAT2 protein has two transmembrane segments and the N-terminal and C-terminal regions face the cytoplasm. The enzymatically active motifs I-III of the GPAT2 protein face the cytosol, while motif IV is within the membrane
subcellular localization of Gat1p and Gat2p are compared using fluorescence microscopy and subcellular fractionation using equilibrium density gradients. Gat1p and Gat2p overlap mostly in their localization and are microsomal GPATs, localized to both perinuclear and cortical endoplasmic reticula in actively proliferating cells
mtGPAT1 has two transmembrane domains (TMDs) (aa 472493 and aa 576592) with both the N- and C-termini facing the cytosol and a loop (aa 494575) facing the intermembrane space
GPAT1 possesses a conserved acyltransferase domain and two transmembrane domains, with the N- and C-terminal domains facing the cytosol, and forms a stem loop structure in the mitochondrial intermembrane space. The active site of acyltransferase is close to the N-terminal domain toward the cytosol, while the C-terminal domain is suggested to have a regulatory function
GPAT1 possesses a conserved acyltransferase domain and two transmembrane domains, with the N- and C-terminal domains facing the cytosol, and forms a stem loop structure in the mitochondrial intermembrane space. The active site of acyltransferase is close to the N-terminal domain toward the cytosol, while the C-terminal domain is suggested to have a regulatory function
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane
analysis of subcellular localization of GPAT isozymes, overview. Isozymes GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, and isozymes GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane