ArticleNature communications2017
Role for formin-like 1-dependent acto-myosin assembly in lipid droplet dynamics and lipid storage.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
40 citing papers in PubMed, 71 citations in OpenAlex.
- Matrix stress relaxation drives glioblastoma cell response in viscoelastic biomaterials.Science advances · 2026Article
- Toll-like receptor 4 signaling links cytoskeletal remodeling to lipid accumulation in macrophages.Inflammation and regeneration · 2026Review
- Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026Review
- Dlgap2 deficiency disrupts synaptic homeostasis by promoting ubiquitin-mediated Itsn1 degradation in a valproic acid-induced autism-like model.Scientific reports · 2026Article
- Genomic Insights into Abdominal and Intramuscular Fat Deposition in Chickens and Their Implications for Productivity Traits: A Systematic Review.Animals : an open access journal from MDPI · 2026Review
- Overexpression of Drosophila NUAK or Constitutively-Active Formin-Like Promotes the Formation of Aberrant Myofibrils.Cytoskeleton (Hoboken, N.J.) · 2025Article
- The lipid droplet protein Jabba promotes actin remodeling downstream of prostaglandin signaling duringMolecular biology of the cell · 2025Article
- Cofilin(s) and Mitochondria: Function Beyond Actin Dynamics.International journal of molecular sciences · 2025Review
- Article
- LncRNAInternational journal of molecular sciences · 2024Article
- Lipid droplets inFrontiers in plant science · 2024Article
- Adipose triglyceride lipase promotes prostaglandin-dependent actin remodeling by regulating substrate release from lipid droplets.Development (Cambridge, England) · 2023Article
- Nonmuscle myosin 2 filaments are processive in cells.Biophysical journal · 2023Article
- A dynamic actin cytoskeleton is required to prevent constitutive VDAC-dependent MAPK signalling and aberrant lipid homeostasis.iScience · 2023Article
- Small lipid droplets are rigid enough to indent a nucleus, dilute the lamina, and cause rupture.The Journal of cell biology · 2023Article
- Lipid droplet-associated lncRNA LIPTER preserves cardiac lipid metabolism.Nature cell biology · 2023Article
- Article
- Cellular communication through extracellular vesicles and lipid droplets.Journal of extracellular biology · 2023Review
- Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023Article
- Cholesterol esters form supercooled lipid droplets whose nucleation is facilitated by triacylglycerols.Nature communications · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipid droplets (LDs) are cellular organelles specialized in triacylglycerol (TG) storage undergoing homotypic clustering and fusion. In non-adipocytic cells with numerous LDs this is balanced by poorly understood droplet dissociation mechanisms. We identify non-muscle myosin IIa (NMIIa/MYH-9) and formin-like 1 (FMNL1) in the LD proteome. NMIIa and actin filaments concentrate around LDs, and form transient foci between dissociating LDs. NMIIa depletion results in decreased LD dissociations, enlarged LDs, decreased hydrolysis and increased storage of TGs. FMNL1 is required for actin assembly on LDs in vitro and for NMIIa recruitment to LDs in cells. We propose a novel acto-myosin structure regulating lipid storage: FMNL1-dependent assembly of myosin II-functionalized actin filaments on LDs facilitates their dissociation, thereby affecting LD surface-to-volume ratio and enzyme accessibility to TGs. In neutrophilic leucocytes from MYH9-related disease patients NMIIa inclusions are accompanied by increased lipid storage in droplets, suggesting that NMIIa dysfunction may contribute to lipid imbalance in man.
Indexed as
Identifiers
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.