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Expression of PAT‐1/MLDP increases triacylglycerol stores and promotes changes in lipid droplet morphology in a CHO cell model

All cells have specific organelles for the sequestration of neutral lipid stores termed lipid storage droplets (LDs). These organelles have a proteinaceous coating that regulates and marshals the movement and storage of the neutral lipid contents. One cohort of these proteins is the PAT family, named for the perilipins, ADRP, and TIP47. A new member of this family has been identified (termed MLDP or PAT‐1), which shares homology to the other PAT family members at the genomic, nucleotide, and amino acid levels. RT‐PCR and western blot analyses indicate that PAT‐1 is not expressed in CHO cells. When a PAT‐1‐3XFLAG fusion protein is ectopically expressed in CHO cells, the protein targets to LDs, co‐localizes to LDs coated with ADRP, and also targets to smaller structures within the cell. When cells are disrupted and subjected to a sucrose gradient ultracentrifugation, PAT‐1 partitions with both buoyant, ADRP‐coated LDs, as well as a more dense pool. CHO cells expressing PAT‐1 contained 1.5 fold more triacylglycerol stores than control cells. Unlike CHO cells expressing other PAT family members, CHO cells expressing the PAT‐1 fusion contain larger LDs (4 microns compared to 1.5 microns) with one or two droplets predominating in each cell. Based on these data we hypothesize that PAT‐1 plays a role in LD metabolism and organization within the cell.