ArticleBiochemical and biophysical research communications2010
Arabidopsis dynamin-related protein 1A polymers bind, but do not tubulate, liposomes.
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Clathrin-Mediated Endocytosis in Plants: Historical to Modern Advances.Traffic (Copenhagen, Denmark) · 2026Review
- Phosphatidylinositides regulate the cell plate morphology transition during cytokinesis in Arabidopsis.Nature communications · 2025Article
- Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring lipid-protein interactions in plant membranes.Journal of experimental botany · 2024Review
- Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.bioRxiv : the preprint server for biology · 2024Article
- SH3 Domain-Containing Protein 2 Plays a Crucial Role at the Step of Membrane Tubulation during Cell Plate Formation.The Plant cell · 2017Article
- High lipid order of Arabidopsis cell-plate membranes mediated by sterol and DYNAMIN-RELATED PROTEIN1A function.The Plant journal : for cell and molecular biology · 2014Article
- Dynamin-related proteins in plant post-Golgi traffic.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Arabidopsis dynamin-related protein 1A (AtDRP1A) is involved in endocytosis and cell plate maturation in Arabidopsis. Unlike dynamin, AtDRP1A does not have any recognized membrane binding or protein-protein interaction domains. We report that GTPase active AtDRP1A purified from Escherichia coli as a fusion to maltose binding protein forms homopolymers visible by negative staining electron microscopy. These polymers interact with protein-free liposomes whose lipid composition mimics that of the inner leaflet of the Arabidopsis plasma membrane, suggesting that lipid-binding may play a role in AtDRP1A function. However, AtDRP1A polymers do not appear to assemble and disassemble in a dynamic fashion and do not have the ability to tubulate liposomes in vitro, suggesting that additional factors or modifications are necessary for AtDRP1A's in vivo function.
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Registered trials
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