ArticlePloS one2017
Molecular identification of transmembrane protein 68 as an endoplasmic reticulum-anchored and brain-specific protein.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Global deletion of the triglyceride-synthesizing enzyme TMEM68 disrupts hepatic lipid homeostasis in mice.Journal of physiology and biochemistry · 2026Article
- Zebrafish are resilient to the loss of major diacylglycerol acyltransferase enzymes.The Journal of biological chemistry · 2024Article
- The acyltransferase transmembrane protein 68 regulates breast cancer cell proliferation by modulating triacylglycerol metabolism.Lipids in health and disease · 2024Article
- Genetic associations with dementia-related proteinopathy: Application of item response theory.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- DIESL fuels a DGAT-independent triglyceride synthesis pathway.Life metabolism · 2023Article
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- Chromosome-level genome assembly and population genomics of Mongolian racerunner (Eremias argus) provide insights into high-altitude adaptation in lizards.BMC biology · 2023Article
- Transmembrane Protein 68 Functions as an MGAT and DGAT Enzyme for Triacylglycerol Biosynthesis.International journal of molecular sciences · 2023Article
- KIAA1363 affects retinyl ester turnover in cultured murine and human hepatic stellate cells.Journal of lipid research · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acyltransferases catalyze essential reactions in the buildup and remodeling of glycerophospholipids and contribute to the maintenance and diversity of cellular membranes. Transmembrane protein 68 (TMEM68) is an evolutionarily conserved protein of unknown function, that forms a distinct subgroup within the glycerophospholipid acyltransferase family. In the current study we expressed murine TMEM68 for the first time in mammalian cells to characterize its subcellular localization, topology, and possible biological function(s). We show that TMEM68 is an integral membrane protein and orients both, the N- and C-terminus towards the cytosol. Live cell imaging demonstrated that TMEM68 is localized mainly at the endoplasmic reticulum (ER), but not at cellular lipid droplets (LDs). The positioning of TMEM68 at the ER was dependent on its first transmembrane domain (TMD), which by itself was sufficient to target cytosolic green fluorescence protein (GFP) to the ER. In contrast, a second TMD was dispensable for ER localization of TMEM68. Finally, we found that among multiple murine tissues the expression level of TMEM68 transcripts was highest in brain. We conclude that TMEM68 is an integral ER membrane protein and a putative acyltransferase involved in brain glycerolipid metabolism.
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