ArticleScientific reports2019
Crosstalk between protein N-glycosylation and lipid metabolism in Saccharomyces cerevisiae.
Article in Scientific reports, 2019. 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, 19 citations in OpenAlex.
- Endoplasmic Reticulum Stress in Neurodegenerative Diseases.Journal of dementia and alzheimer's disease · 2024Article
- Functional, transcriptomic, and lipidomic studies of theMicrobiology spectrum · 2024Article
- Loss of Opi3 causes a lipid imbalance that influences the virulence traits ofFrontiers in cellular and infection microbiology · 2024Article
- Metabolomic profile of acute myeloid leukaemia parallels of prognosis and response to therapy.Scientific reports · 2023Article
- The ER chaperone, BIP protects Microglia from ER stress-mediated Apoptosis in Hyperglycemia.Neurochemistry international · 2023Article
- miR-27b targets MAIP1 to mediate lipid accumulation in cultured human and mouse hepatic cells.Communications biology · 2023Article
- Perspectives on Retinal Dolichol Metabolism, and Visual Deficits in Dolichol Metabolism-Associated Inherited Disorders.Advances in experimental medicine and biology · 2023Review
- Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease.Progress in molecular and subcellular biology · 2021Article
- Loss of ERAD bridging factor UBX2 modulates lipid metabolism and leads to ER stress-associated apoptosis during cadmium toxicity in Saccharomyces cerevisiae.Current genetics · 2020Article
- Disruption in phosphate transport affects membrane lipid and lipid droplet homeostasis in Saccharomyces cerevisiae.Journal of bioenergetics and biomembranes · 2020Article
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic reticulum (ER) is a multi functional organelle and plays a crucial role in protein folding and lipid biosynthesis. The SEC59 gene encodes dolichol kinase, required for protein glycosylation in the ER. The mutation of sec59-1 caused a protein N-glycosylation defect mediated ER stress resulting in increased levels of phospholipid, neutral lipid and sterol, whereas growth was reduced. In the sec59-1∆ cell, the N-glycosylation of vacuolar carboxy peptidase-Y (CPY) was significantly reduced; whereas the ER stress marker Kar2p and unfolded protein response (UPR) were significantly increased. Increased levels of Triacylglycerol (TAG), sterol ester (SE), and lipid droplets (LD) could be attributed to up-regulation of DPP1, LRO1, and ARE2 in the sec 59-1∆ cell. Also, the diacylglycerol (DAG), sterol (STE), and free fatty acids (FFA) levels were significantly increased, whereas the genes involved in peroxisome biogenesis and Pex3-EGFP levels were reduced when compared to the wild-type. The microarray data also revealed increased expression of genes involved in phospholipid, TAG, fatty acid, sterol synthesis, and phospholipid transport resulting in dysregulation of lipid homeostasis in the sec59-1∆ cell. We conclude that SEC59 dependent N-glycosylation is required for lipid homeostasis, peroxisome biogenesis, and ER protein quality control.
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