ReviewThe EMBO journal2011
Let's go bananas: revisiting the endocytic BAR code.
Review in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 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
133 citing papers in PubMed.
- Beyond spherical vesicles: morphological diversity of extracellular vesicles in health and disease.Annals of medicine · 2026Review
- Membrane curvature initiates Cdc42-FBP17-N-WASP clustering and actin nucleation.The EMBO journal · 2026Article
- Genome-Wide Association Reveals Signalling-Linked Infection Tolerance in Hibernating Bats.Pathogens (Basel, Switzerland) · 2026Article
- Database analysis reveals endophilin A expression as a marker of metastasis and prognosis in breast cancer.Discover oncology · 2025Article
- GTP hydrolysis triggers membrane remodeling by AMPH-1.Science advances · 2025Article
- Article
- Insulin receptor tyrosine kinase substrate in health and disease (Review).Molecular medicine reports · 2025Review
- Peripheral membrane protein endophilin B1 probes, perturbs and permeabilizes lipid bilayers.Communications biology · 2025Article
- Prominosomes - a particular class of extracellular vesicles containing prominin-1/CD133?Journal of nanobiotechnology · 2025Review
- Mechanistic divergences of endocytic clathrin-coated vesicle formation in mammals, yeasts and plants.Journal of cell science · 2024Review
- Membrane remodeling by FAM92A1 during brain development regulates neuronal morphology, synaptic function, and cognition.Nature communications · 2024Article
- Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast.Nature communications · 2024Article
- The Regulation of Exosome Generation and Function in Physiological and Pathological Processes.International journal of molecular sciences · 2023Review
- Membrane shapers from two distinct superfamilies cooperate in the development of neuronal morphology.The Journal of cell biology · 2023Article
- Self-assembly of CIP4 drives actin-mediated asymmetric pit-closing in clathrin-mediated endocytosis.Nature communications · 2023Article
- Two-dimensional molecular condensation in cell signaling and mechanosensing.Acta biochimica et biophysica Sinica · 2023Review
- Pacsin 2-dependent N-cadherin internalization regulates the migration behaviour of malignant cancer cells.Journal of cell science · 2023Article
- Review
- GTP-stimulated membrane fission by the N-BAR protein AMPH-1.Traffic (Copenhagen, Denmark) · 2023Article
- Article
73 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Against the odds of membrane resistance, members of the BIN/Amphiphysin/Rvs (BAR) domain superfamily shape membranes and their activity is indispensable for a plethora of life functions. While crystal structures of different BAR dimers advanced our understanding of membrane shaping by scaffolding and hydrophobic insertion mechanisms considerably, especially life-imaging techniques and loss-of-function studies of clathrin-mediated endocytosis with its gradually increasing curvature show that the initial idea that solely BAR domain curvatures determine their functions is oversimplified. Diagonal placing, lateral lipid-binding modes, additional lipid-binding modules, tilde shapes and formation of macromolecular lattices with different modes of organisation and arrangement increase versatility. A picture emerges, in which BAR domain proteins create macromolecular platforms, that recruit and connect different binding partners and ensure the connection and coordination of the different events during the endocytic process, such as membrane invagination, coat formation, actin nucleation, vesicle size control, fission, detachment and uncoating, in time and space, and may thereby offer mechanistic explanations for how coordination, directionality and effectiveness of a complex process with several steps and key players can be achieved.
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.