ArticleTraffic (Copenhagen, Denmark)2009
Hydrophobic and basic domains target proteins to lipid droplets.
Article in Traffic (Copenhagen, Denmark), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 77 citations in OpenAlex.
- Lipid Droplet-Localized Spindle Apparatus Coiled-Coil Protein 1 Regulates Lipid Droplet Distribution.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- Navigating lipid droplet proteins - part II: molecular mechanisms underlying ER-to-lipid droplet protein partitioning.Biochemical Society transactions · 2025Review
- Promiscuous class II-binding SARS-CoV-2-nuc derived vaccine-peptide induced extensive conventional, innate and unconventional T cell responses.Frontiers in immunology · 2025Article
- Identification of motifs and mechanisms for lipid droplet targeting of the lipolytic inhibitors G0S2 and HIG2.Journal of cell science · 2022Article
- Co-translational biogenesis of lipid droplet integral membrane proteins.Journal of cell science · 2022Article
- The Chlamydia trachomatis inclusion membrane protein CT006 associates with lipid droplets in eukaryotic cells.PloS one · 2022Article
- ANKRD22 is an N-myristoylated hairpin-like monotopic membrane protein specifically localized to lipid droplets.Scientific reports · 2021Article
- The C-Terminus of Perilipin 3 Shows Distinct Lipid Binding at Phospholipid-Oil-Aqueous Interfaces.Membranes · 2021Article
- Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation.Nature communications · 2021Article
- A Role for Caveolin-3 in the Pathogenesis of Muscular Dystrophies.International journal of molecular sciences · 2020Review
- Characterization of essential domains in HSD17B13 for cellular localization and enzymatic activity.Journal of lipid research · 2020Article
- Protein Quality Control and Lipid Droplet Metabolism.Annual review of cell and developmental biology · 2020Review
- Caveolin-1 function at the plasma membrane and in intracellular compartments in cancer.Cancer metastasis reviews · 2020Review
- Dynamics and functions of lipid droplets.Nature reviews. Molecular cell biology · 2019Review
- Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Harnessing yeast organelles for metabolic engineering.Nature chemical biology · 2017Review
- Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species.Journal of lipid research · 2016Article
- Spatial control of lipid droplet proteins by the ERAD ubiquitin ligase Doa10.The EMBO journal · 2016Article
- Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets.Trends in cell biology · 2016Review
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 3 countries.
Funding
Abstract
In recent years, progress in the study of the lateral organization of the plasma membrane has led to the proposal that mammalian cells use two different organelles to store lipids: intracellular lipid droplets (LDs) and plasma membrane caveolae. Experimental evidence suggests that caveolin (CAV) may act as a sensitive lipid-organizing molecule that physically connects these two lipid-storing organelles. Here, we determine the sequences necessary for efficient sorting of CAV to LDs. We show that targeting is a process cooperatively mediated by two motifs. CAV's central hydrophobic domain (Hyd) anchors CAV to the endoplasmic reticulum (ER). Next, positively charged sequences (Pos-Seqs) mediate sorting of CAVs into LDs. Our findings were confirmed by identifying an equivalent, non-conserved but functionally interchangeable Pos-Seq in ALDI, a bona fide LD-resident protein. Using this information, we were able to retarget a cytosolic protein and convert it to an LD-resident protein. Further studies suggest three requirements for targeting via this mechanism: the positive charge of the Pos-Seq, physical proximity between Pos-Seq and Hyd and a precise spatial orientation between both motifs. The study uncovers remarkable similarities with the signals that target proteins to the membrane of mitochondria and peroxisomes.
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What OpenQuestion holds
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.