ArticleProceedings of the National Academy of Sciences of the United States of America2017
Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
- The multiple sclerosis drug fingolimod induces pore-like membrane defects, contributing to its antimicrobial activity.The Journal of biological chemistry · 2026Article
- Mitochondrial Voltage-Dependent Anion Channel: From a Passive Pore to a Cellular Hub Through Protein Complexation.International journal of molecular sciences · 2026Review
- Logarithmic Binding and Stretched-Exponential Kinetics in Peripheral Protein Interactions with Lipid Membrane Surfaces.The journal of physical chemistry letters · 2026Article
- Multiple Sclerosis Drug Fingolimod Exhibits Antibacterial Activity through Bacterial Membrane Permeabilization.bioRxiv : the preprint server for biology · 2026Article
- Complex Structural Examination of Protein-Lipid Interactions with Neutron Scattering Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Global and local effects in lipid-mediated interactions between peripheral and integral membrane proteins.Frontiers in molecular biosciences · 2025Review
- Article
- Phospholipid Membrane Interactions of Model Ac-WL-X-LL-OH Peptides Investigated by Solid-State Nuclear Magnetic Resonance.Membranes · 2024Article
- Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel.International journal of molecular sciences · 2024Article
- Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein-VDAC complexation as a potential therapeutic target for Parkinson's disease treatment.Cellular and molecular life sciences : CMLS · 2022Article
- Specific interactions of peripheral membrane proteins with lipids: what can molecular simulations show us?Bioscience reports · 2022Article
- Functional Roles of αApplied and environmental microbiology · 2021Article
- Large scale model lipid membrane movement induced by a cation switch.Journal of colloid and interface science · 2021Article
- Regulation of Mitochondrial Respiration by VDAC Is Enhanced by Membrane-Bound Inhibitors with Disordered Polyanionic C-Terminal Domains.International journal of molecular sciences · 2021Review
- Information gain from isotopic contrast variation in neutron reflectometry on protein-membrane complex structures.Journal of applied crystallography · 2020Article
- Accurate background correction in neutron reflectometry studies of soft condensed matter films in contact with fluid reservoirs.Journal of applied crystallography · 2020Article
- Advances in Translational Nanotechnology: Challenges and Opportunities.Applied sciences (Basel, Switzerland) · 2020Article
- Neutron scattering for STRUCTURAL BIOLOGY: Modern neutron sources illuminate the complex functions of living systems.Physics today · 2020Article
- Membrane perforation by the pore-forming toxin pneumolysin.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
Dimeric tubulin, an abundant water-soluble cytosolic protein known primarily for its role in the cytoskeleton, is routinely found to be associated with mitochondrial outer membranes, although the structure and physiological role of mitochondria-bound tubulin are still unknown. There is also no consensus on whether tubulin is a peripheral membrane protein or is integrated into the outer mitochondrial membrane. Here the results of five independent techniques-surface plasmon resonance, electrochemical impedance spectroscopy, bilayer overtone analysis, neutron reflectometry, and molecular dynamics simulations-suggest that α-tubulin's amphipathic helix H10 is responsible for peripheral binding of dimeric tubulin to biomimetic "mitochondrial" membranes in a manner that differentiates between the two primary lipid headgroups found in mitochondrial membranes, phosphatidylethanolamine and phosphatidylcholine. The identification of the tubulin dimer orientation and membrane-binding domain represents an essential step toward our understanding of the complex mechanisms by which tubulin interacts with integral proteins of the mitochondrial outer membrane and is important for the structure-inspired design of tubulin-targeting agents.
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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.