ArticleMolecular biology of the cell2014
Alternate pleckstrin homology domain orientations regulate dynamin-catalyzed membrane fission.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Nanoscale dynamics of Dynamin 1 helices reveals squeeze-twist deformation mode critical for membrane fission.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Centronuclear Myopathy Caused by Defective Membrane Remodelling of Dynamin 2 and BIN1 Variants.International journal of molecular sciences · 2022Review
- Light Scattering Techniques to Assess Self-Assembly and Hydrodynamics of Membrane Trafficking Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- NMR identification of a conserved Drp1 cardiolipin-binding motif essential for stress-induced mitochondrial fission.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Flexible pivoting of dynamin pleckstrin homology domain catalyzes fission: insights into molecular degrees of freedom.Molecular biology of the cell · 2021Article
- The CHD Protein, Kismet, is Important for the Recycling of Synaptic Vesicles during Endocytosis.Scientific reports · 2019Article
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- The tilted helix model of dynamin oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mechanistic study of PpIX accumulation using the JFCR39 cell panel revealed a role for dynamin 2-mediated exocytosis.Scientific reports · 2019Article
- Structural Insights into the Mechanism of Dynamin Superfamily Proteins.Trends in cell biology · 2019Review
- Article
- Steric interference from intrinsically disordered regions controls dynamin-related protein 1 self-assembly during mitochondrial fission.Scientific reports · 2018Article
- Mitochondrial dynamics: The dynamin superfamily and execution by collusion.Seminars in cell & developmental biology · 2018Review
- The pleckstrin-homology domain of dynamin is dispensable for membrane constriction and fission.Molecular biology of the cell · 2017Article
- Membrane fission by dynamin: what we know and what we need to know.The EMBO journal · 2016Review
- Identification and function of conformational dynamics in the multidomain GTPase dynamin.The EMBO journal · 2016Article
- Distinct Splice Variants of Dynamin-related Protein 1 Differentially Utilize Mitochondrial Fission Factor as an Effector of Cooperative GTPase Activity.The Journal of biological chemistry · 2016Article
- A high-throughput platform for real-time analysis of membrane fission reactions reveals dynamin function.Nature cell biology · 2015Article
- Cardiolipin's propensity for phase transition and its reorganization by dynamin-related protein 1 form a basis for mitochondrial membrane fission.Molecular biology of the cell · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The self-assembling GTPase dynamin catalyzes endocytic vesicle scission via membrane insertion of its pleckstrin homology (PH) domain. However, the molecular mechanisms underlying PH domain-dependent membrane fission remain obscure. Membrane-curvature-sensing and membrane-curvature-generating properties have been attributed, but it remains to be seen whether the PH domain is involved in either process independent of dynamin self-assembly. Here, using multiple fluorescence spectroscopic and microscopic techniques, we demonstrate that the isolated PH domain does not act to bend membranes but instead senses high membrane curvature through hydrophobic insertion into the membrane bilayer. Furthermore, we use a complementary set of short- and long-distance Förster resonance energy transfer approaches to distinguish PH-domain orientation from proximity at the membrane surface in full-length dynamin. We reveal, in addition to the GTP-sensitive "hydrophobic mode," the presence of an alternate, GTP-insensitive "electrostatic mode" of PH domain-membrane interactions that retains dynamin on the membrane surface during the GTP hydrolysis cycle. Stabilization of this alternate orientation produces dramatic variations in the morphology of membrane-bound dynamin spirals, indicating that the PH domain regulates membrane fission through the control of dynamin polymer dynamics.
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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.