THESIS
2021
1 online resource (vi, 59 pages) : illustrations (some color)
Abstract
In eukaryotic cells, excess fatty acids are primarily stored in lipid droplets as triacylglycerol (TAG). A series of proteins catalyze the synthesis of TAG in the endoplasmic reticulum (ER). Although the essential enzymes involved in TAG synthesis have been well-defined, it is still unknown whether additional proteins can promote TAG synthesis. Here, I report that the conserved transmembrane proteins TMEM120A and TMEM120B promote TAG synthesis. Loss of TMEM120A, TMEM120B, or both of them disrupts the differentiation of OP9 cells into adipocytes in vitro. In contrast, over-expression of TMEM120A promotes lipid droplet expansion in several cell lines upon exogenous fatty acid supplementation. TMEM120A overexpression also increases the sensitivity of mammalian cells to the simultaneous tre...[
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In eukaryotic cells, excess fatty acids are primarily stored in lipid droplets as triacylglycerol (TAG). A series of proteins catalyze the synthesis of TAG in the endoplasmic reticulum (ER). Although the essential enzymes involved in TAG synthesis have been well-defined, it is still unknown whether additional proteins can promote TAG synthesis. Here, I report that the conserved transmembrane proteins TMEM120A and TMEM120B promote TAG synthesis. Loss of TMEM120A, TMEM120B, or both of them disrupts the differentiation of OP9 cells into adipocytes in vitro. In contrast, over-expression of TMEM120A promotes lipid droplet expansion in several cell lines upon exogenous fatty acid supplementation. TMEM120A overexpression also increases the sensitivity of mammalian cells to the simultaneous treatment of fatty acids and TAG synthesis inhibitors, which causes cell death. My results suggest that the TMEM120 protein family is required for adipocyte differentiation, and TMEM120A contributes to TAG synthesis.
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