ArticleProceedings of the National Academy of Sciences of the United States of America2020
The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- A Case of Familial Chylomicronemia Syndrome Caused by a Novel Homozygous GPIHBP1 Mutation Successfully Treated with the Selective PPARα Modulator Pemafibrate.Journal of atherosclerosis and thrombosis · 2026Article
- Lipoprotein lipase requires a flexible lid and stable C-terminal, both maintained by ApoC-II peptide binding.bioRxiv : the preprint server for biology · 2025Article
- Cryogenic electron tomography reveals helical organization of lipoprotein lipase in storage vesicles.Science advances · 2025Article
- Review
- Targeting host-specific metabolic pathways-opportunities and challenges for anti-infective therapy.Frontiers in molecular biosciences · 2024Review
- Lipoprotein lipase as a target for obesity/diabetes related cardiovascular disease.Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques · 2024Review
- Macromolecular Interactions of Lipoprotein Lipase (LPL).Sub-cellular biochemistry · 2024Review
- Dynamic interplay between sortilin and syndecan-1 contributes to prostate cancer progression.Scientific reports · 2023Article
- Lipoprotein Lipase Activity Does Not Differ in the Serum Environment of Vegans and Omnivores.Nutrients · 2023Article
- The mechanisms to dispose of misfolded proteins in the endoplasmic reticulum of adipocytes.Nature communications · 2023Article
- Structure of dimeric lipoprotein lipase reveals a pore adjacent to the active site.Nature communications · 2023Article
- Combined action of albumin and heparin regulates lipoprotein lipase oligomerization, stability, and ligand interactions.PloS one · 2023Article
- A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Characterization of lipoprotein lipase storage vesicles in 3T3-L1 adipocytes.Journal of cell science · 2022Article
- Current Diagnosis and Management of Primary Chylomicronemia.Journal of atherosclerosis and thrombosis · 2021Review
- Article
- Lipoprotein Lipase and Its Regulators: An Unfolding Story.Trends in endocrinology and metabolism: TEM · 2021Review
- GPIHBP1 and ANGPTL4 Utilize Protein Disorder to Orchestrate Order in Plasma Triglyceride Metabolism and Regulate Compartmentalization of LPL Activity.Frontiers in cell and developmental biology · 2021Review
- The structural basis for monoclonal antibody 5D2 binding to the tryptophan-rich loop of lipoprotein lipase.Journal of lipid research · 2020Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Lipases are enzymes necessary for the proper distribution and utilization of lipids in the human body. Lipoprotein lipase (LPL) is active in capillaries, where it plays a crucial role in preventing dyslipidemia by hydrolyzing triglycerides from packaged lipoproteins. Thirty years ago, the existence of a condensed and inactive LPL oligomer was proposed. Although recent work has shed light on the structure of the LPL monomer, the inactive oligomer remained opaque. Here we present a cryo-EM reconstruction of a helical LPL oligomer at 3.8-Å resolution. Helix formation is concentration-dependent, and helices are composed of inactive dihedral LPL dimers. Heparin binding stabilizes LPL helices, and the presence of substrate triggers helix disassembly. Superresolution fluorescent microscopy of endogenous LPL revealed that LPL adopts a filament-like distribution in vesicles. Mutation of one of the helical LPL interaction interfaces causes loss of the filament-like distribution. Taken together, this suggests that LPL is condensed into its inactive helical form for storage in intracellular vesicles.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.