ArticlePloS one2010
Structural insights into triglyceride storage mediated by fat storage-inducing transmembrane (FIT) protein 2.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 60 citations in OpenAlex.
- Insect Lipids: Structure, Classification and Function.Advances in experimental medicine and biology · 2026Review
- ECM characterization and 3D bioprinted models of NSCLC for investigating stiffness-dependent tumor behavior and drug response.Materials today. Bio · 2025Article
- Interplay between lipid droplets and alpha-synuclein: implication in Parkinson's disease pathogenesis.Frontiers in molecular neuroscience · 2025Review
- Lipid Droplets: Formation, Degradation, and Their Role in Cellular Responses to Flavivirus Infections.Microorganisms · 2024Review
- Dynamic Regulation of Lipid Droplet Biogenesis in Plant Cells and Proteins Involved in the Process.International journal of molecular sciences · 2023Review
- Fat storage-inducing transmembrane proteins: beyond mediating lipid droplet formation.Cellular & molecular biology letters · 2022Review
- The yeastJournal of cell science · 2020Article
- FIT2 is an acyl-coenzyme A diphosphatase crucial for endoplasmic reticulum homeostasis.The Journal of cell biology · 2020Article
- Identification of Potentially Relevant Genes for Excessive Exercise-Induced Pathological Cardiac Hypertrophy in Zebrafish.Frontiers in physiology · 2020Article
- LDAF1 and Seipin Form a Lipid Droplet Assembly Complex.Developmental cell · 2019Article
- Mouse lipogenic proteins promote the co-accumulation of triacylglycerols and sesquiterpenes in plant cells.Planta · 2019Article
- Mice lacking fat storage-inducing transmembrane protein 2 show improved profiles upon pressure overload-induced heart failure.Heliyon · 2019Article
- To Bud or Not to Bud: A Perspective on Molecular Simulations of Lipid Droplet Budding.Frontiers in molecular biosciences · 2019Article
- Fat storage-inducing transmembrane (FIT or FITM) proteins are related to lipid phosphatase/phosphotransferase enzymes.Microbial cell (Graz, Austria) · 2017Article
- The collaborative work of droplet assembly.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Mouse fat storage-inducing transmembrane protein 2 (FIT2) promotes lipid droplet accumulation in plants.Plant biotechnology journal · 2017Article
- SGBS cells as a model of human adipocyte browning: A comprehensive comparative study with primary human white subcutaneous adipocytes.Scientific reports · 2017Article
- Role of Phospholipid Flux during Milk Secretion in the Mammary Gland.Journal of mammary gland biology and neoplasia · 2017Review
- A homozygous FITM2 mutation causes a deafness-dystonia syndrome with motor regression and signs of ichthyosis and sensory neuropathy.Disease models & mechanisms · 2017Article
- Reep1 null mice reveal a converging role for hereditary spastic paraplegia proteins in lipid droplet regulation.Human molecular genetics · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Fat storage-Inducing Transmembrane proteins 1 & 2 (FIT1/FITM1 and FIT2/FITM2) belong to a unique family of evolutionarily conserved proteins localized to the endoplasmic reticulum that are involved in triglyceride lipid droplet formation. FIT proteins have been shown to mediate the partitioning of cellular triglyceride into lipid droplets, but not triglyceride biosynthesis. FIT proteins do not share primary sequence homology with known proteins and no structural information is available to inform on the mechanism by which FIT proteins function. Here, we present the experimentally-solved topological models for FIT1 and FIT2 using N-glycosylation site mapping and indirect immunofluorescence techniques. These methods indicate that both proteins have six-transmembrane-domains with both N- and C-termini localized to the cytosol. Utilizing this model for structure-function analysis, we identified and characterized a gain-of-function mutant of FIT2 (FLL(157-9)AAA) in transmembrane domain 4 that markedly augmented the total number and mean size of lipid droplets. Using limited-trypsin proteolysis we determined that the FLL(157-9)AAA mutant has enhanced trypsin cleavage at K86 relative to wild-type FIT2, indicating a conformational change. Taken together, these studies indicate that FIT2 is a 6 transmembrane domain-containing protein whose conformation likely regulates its activity in mediating lipid droplet formation.
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Registered trials
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.