title: Trans-Golgi proteins participate in the control of lipid droplet and chylomicron formation.
abstract: LDs (lipid droplets) carrying TAG (triacylglycerol) and cholesteryl esters are emerging as dynamic cellular organelles that are generated in nearly every cell. They play a key role in lipid and membrane homoeostasis. Abnormal LD dynamics are associated with the pathophysiology of many metabolic diseases, such as obesity, diabetes, atherosclerosis, fatty liver and even cancer. Chylomicrons, stable droplets also consisting of TAG and cholesterol are generated in the intestinal epithelium to transport exogenous (dietary) lipids after meals from the small intestine to tissues for degradation. Defective chylomicron formation is responsible for inherited lipoprotein deficiencies, including abetalipoproteinaemia, hypobetalipoproteinaemia and chylomicron retention disease. These are disorders sharing characteristics such as fat malabsorption, low levels of circulating lipids and fat-soluble vitamins, failure to thrive in early childhood, ataxic neuropathy and visual impairment. Thus understanding the molecular mechanisms governing the dynamics of LDs and chylomicrons, namely, their biogenesis, growth, maintenance and degradation, will not only clarify their molecular role, but might also provide additional indications to treatment of metabolic diseases. In this review, we highlight the role of two small GTPases [ARFRP1 (ADP-ribosylation factor related protein 1) and ARL1 (ADP-ribosylation factor-like 1)] and their downstream targets acting on the trans-Golgi (Golgins and Rab proteins) on LD and chylomicron formation.
authors.affiliation: Department of Experimental Diabetology, German Institute of Human Nutrition Potsdam-Rehbruecke, D-14558 Nuthetal, Germany.
authors.forename: Deike
authors.initials: D
authors.lastname: Hesse
authors.forename: Alexander
authors.initials: A
authors.lastname: Jaschke
authors.forename: Bomee
authors.initials: B
authors.lastname: Chung
authors.forename: Annette
authors.initials: A
authors.lastname: Schürmann
mesh_terms: D020727:ADP-Ribosylation Factors / Q000235:genetics / Q000378:metabolism*; D017667:Adipocytes / Q000201:enzymology / Q000378:metabolism; D000818:Animals; D001324:Autoantigens / Q000378:metabolism; D001692:Biological Transport; D002914:Chylomicrons / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000201:enzymology / Q000378:metabolism; D000077614:Golgi Matrix Proteins; D006801:Humans; D050356:Lipid Metabolism; D052439:Lipid Metabolism Disorders / Q000201:enzymology / Q000378:metabolism; D008066:Lipolysis; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D025941:Protein Interaction Mapping
chemical_list: D001324:Autoantigens; D002914:Chylomicrons; D000077614:Golgi Matrix Proteins; C450721:Golgi complex autoantigen, 97-kDa; D008565:Membrane Proteins; C097313:ADP-ribosylation factor related proteins; D020727:ADP-Ribosylation Factors; C531986:Arfrp1 protein, mouse