ArticleProceedings of the National Academy of Sciences of the United States of America2003
Membrane tube formation from giant vesicles by dynamic association of motor proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed.
- Organelle Membrane Extensions in Mammalian Cells.Biology · 2023Review
- Interaction of Hyaluronan Acid with Some Proteins in Aqueous Solution as Studied by NMR.Membranes · 2023Article
- Biomembranes undergo complex, non-axisymmetric deformations governed by Kirchhoff-Love kinematicsand revealed by a three-dimensional computational framework.Proceedings. Mathematical, physical, and engineering sciences · 2021Article
- The Mechanics and Thermodynamics of Tubule Formation in Biological Membranes.The Journal of membrane biology · 2021Review
- Non-Equilibrium Large-Scale Membrane Transformations Driven by MinDE Biochemical Reaction Cycles.Angewandte Chemie (International ed. in English) · 2021Article
- On the Role of Curved Membrane Nanodomains, and Passive and Active Skeleton Forces in the Determination of Cell Shape and Membrane Budding.International journal of molecular sciences · 2021Article
- Rapid formation of human immunodeficiency virus-like particles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mechanisms of Motor-Independent Membrane Remodeling Driven by Dynamic Microtubules.Current biology : CB · 2020Article
- Probing force in living cells with optical tweezers: from single-molecule mechanics to cell mechanotransduction.Biophysical reviews · 2019Review
- Force sharing and force generation by two teams of elastically coupled molecular motors.Scientific reports · 2019Article
- A novel fluorescence microscopic approach to quantitatively analyse protein-induced membrane remodelling.Journal of biosciences · 2018Review
- Fluorescence microscopy applied to intracellular transport by microtubule motors.Journal of biosciences · 2018Review
- Guided by curvature: shaping cells by coupling curved membrane proteins and cytoskeletal forces.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Opposing Kinesin and Myosin-I Motors Drive Membrane Deformation and Tubulation along Engineered Cytoskeletal Networks.Current biology : CB · 2018Article
- Nanoscale invaginations of the nuclear envelope: Shedding new light on wormholes with elusive function.Nucleus (Austin, Tex.) · 2017Review
- Lateral Tension-Induced Penetration of Particles into a Liposome.Materials (Basel, Switzerland) · 2017Article
- Article
- Use of the supported membrane tube assay system for real-time analysis of membrane fission reactions.Nature protocols · 2017Article
- Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein.Biochimica et biophysica acta · 2016Review
- Complex instability of axially compressed tubular lipid membrane with controlled spontaneous curvature.The European physical journal. E, Soft matter · 2015Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tubular morphology of intracellular membranous compartments is actively maintained through interactions with motor proteins and the cytoskeleton. Moving along cytoskeletal elements, motor proteins exert forces on the membranes to which they are attached, resulting in the formation of membrane tubes and tubular networks. To study the formation of membrane tubes by motor proteins, we developed an in vitro assay consisting of purified kinesin proteins directly linked to the lipids of giant unilamellar vesicles. When the vesicles are brought into contact with a network of immobilized microtubules, membrane tubes and tubular networks are formed. Through systematic variation of the kinesin concentration and membrane composition we study the mechanism involved. We show that a threshold concentration of motor proteins is needed and that a low membrane tension facilitates tube formation. Forces involved in tube formation were measured directly with optical tweezers and are shown to depend only on the tension and bending rigidity of the membrane. The forces were found to be higher than can be generated by individual motor proteins, indicating that multiple motors were working together to pull tubes. We propose a simple mechanism by which individual motor proteins can dynamically associate into clusters that provide the force needed for the formation of tubes, explaining why, in contrast to earlier findings [Roux, A., Cappello, G., Cartaud, J., Prost, J., Goud, B. & Bassereau, P. (2002) Proc. Natl. Acad. Sci. USA 99, 5394-5399], motor proteins do not need to be physically linked to each other to be able to pull tubes.
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