ArticleNature communications2019
Functional recruitment of dynamin requires multimeric interactions for efficient endocytosis.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 36 citations in OpenAlex.
- Functional Specialization of Clathrin-Independent Endocytic Routes: Mechanisms and Cellular Roles.Traffic (Copenhagen, Denmark) · 2026Review
- DNM2 lipid binding drives centronuclear myopathy and represents a potential therapeutic target.JCI insight · 2026Article
- Protein dimerization in 2D vs 3D: Geometric allostery enhances binding affinity.The Journal of chemical physics · 2025Article
- Intersectin1 promotes clathrin-mediated endocytosis by organizing and stabilizing endocytic protein interaction networks.Cell reports · 2024Article
- Dynamin 1xA interacts with Endophilin A1 via its spliced long C-terminus for ultrafast endocytosis.The EMBO journal · 2024Article
- Cryo-EM structures of membrane-bound dynamin in a post-hydrolysis state primed for membrane fission.Developmental cell · 2024Article
- Intersectin1 promotes clathrin-mediated endocytosis by organizing and stabilizing endocytic protein interaction networks.bioRxiv : the preprint server for biology · 2024Article
- Role of the dynamin-related protein 2 family and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana.Journal of cell science · 2024Article
- A mechanism-based theory of cellular and tissue plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Prodrugs of the Archetypal Dynamin Inhibitor Bis-T-22.ChemMedChem · 2022Article
- Cellular and structural insight into dynamin function during endocytic vesicle formation: a tale of 50 years of investigation.Bioscience reports · 2022Review
- Multivalent interactions between molecular components involved in fast endophilin mediated endocytosis drive protein phase separation.Nature communications · 2022Article
- BIN1 modulation in vivo rescues dynamin-related myopathy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- Iron homeostasis and organismal aging.Ageing research reviews · 2021Review
- Receptor tyrosine kinases and cancer: oncogenic mechanisms and therapeutic approaches.Oncogene · 2021Review
- β-arrestin-dependent PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Evolving models for assembling and shaping clathrin-coated pits.The Journal of cell biology · 2020Review
- Imaging endocytic vesicle formation at high spatial and temporal resolutions with the pulsed-pH protocol.Nature protocols · 2020Article
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
During clathrin mediated endocytosis (CME), the concerted action of dynamin and its interacting partners drives membrane scission. Essential interactions occur between the proline/arginine-rich domain of dynamin (dynPRD) and the Src-homology domain 3 (SH3) of various proteins including amphiphysins. Here we show that multiple SH3 domains must bind simultaneously to dynPRD through three adjacent motifs for dynamin's efficient recruitment and function. First, we show that mutant dynamins modified in a single motif, including the central amphiphysin SH3 (amphSH3) binding motif, partially rescue CME in dynamin triple knock-out cells. However, mutating two motifs largely prevents that ability. Furthermore, we designed divalent dynPRD-derived peptides. These ligands bind multimers of amphSH3 with >100-fold higher affinity than monovalent ones in vitro. Accordingly, dialyzing living cells with these divalent peptides through a patch-clamp pipette blocks CME much more effectively than with monovalent ones. We conclude that dynamin drives vesicle scission via multivalent interactions in cells.
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.