ArticleThe Journal of cell biology1988
Formation of membrane networks in vitro by kinesin-driven microtubule movement.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Thermodynamic uncertainty relation for systems with active Ornstein-Uhlenbeck particles.PNAS nexus · 2025Article
- Review
- Single-molecule in vitro reconstitution assay for kinesin-1-driven membrane dynamics.Biophysical reviews · 2019Review
- Morphology of mitochondria in spatially restricted axons revealed by cryo-electron tomography.PLoS biology · 2018Article
- Vesicle Size Regulates Nanotube Formation in the Cell.Scientific reports · 2016Article
- Dynamic tubulation of mitochondria drives mitochondrial network formation.Cell research · 2015Article
- Characterization and expression pattern of KIFC1-like kinesin gene in the testis of the Macrobrachium nipponense with discussion of its relationship with structure lamellar complex (LCx) and acroframosome (AFS).Molecular biology reports · 2012Article
- Membrane shape as a reporter for applied forces.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Bidirectional membrane tube dynamics driven by nonprocessive motors.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Coalescence of membrane tethers: experiments, theory, and applications.Biophysical journal · 2005Article
- Membrane tube formation from giant vesicles by dynamic association of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Dynein supports motility of endoplasmic reticulum in the fungus Ustilago maydis.Molecular biology of the cell · 2002Article
- Intact lysosome transport and phagosome function despite kinectin deficiency.Molecular and cellular biology · 2001Article
- Brefeldin A-dependent membrane tubule formation reconstituted in vitro is driven by a cell cycle-regulated microtubule motor.Molecular biology of the cell · 2000Article
- Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism.Molecular biology of the cell · 1999Article
- A novel direct interaction of endoplasmic reticulum with microtubules.The EMBO journal · 1998Article
- Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease.The Journal of cell biology · 1998Article
- In vitro reconstitution of microtubule plus end-directed, GTPgammaS-sensitive motility of Golgi membranes.Molecular biology of the cell · 1998Article
- Golgi tubule traffic and the effects of brefeldin A visualized in living cells.The Journal of cell biology · 1997Article
- The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus oocytes.Molecular biology of the cell · 1997Article
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2 authors.
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Abstract
Certain intracellular organelles such as the endoplasmic reticulum (Terasaki, M., L. B. Chen, and K. Fujiwara. 1986. J. Cell Biol. 103:1557-1568) and lysosomes (Swanson, J., A. Bushnell, and S. C. Silverstein. Proc. Natl. Acad. Sci. USA. 84:1921-1925) form tubular networks that are closely aligned with microtubules. Here we describe the formation of polygonal networks composed of interconnected membrane tubules that occurs when a preparation of microtubule affinity-purified squid kinesin is combined with microtubules and ATP on a glass surface. The membrane, which is a minor contaminant in the microtubule affinity-purified kinesin preparation, binds to microtubules translocating along kinesin-coated glass surfaces. Force exerted by kinesin upon the microtubule is transmitted to the membrane and a tubular extension of the membrane is produced. As the membrane tubule elongates, membrane tension exerts an opposing force upon the translocating microtubule that can alter its direction of movement by dissociating or partially dissociating the microtubule from the kinesin-coated surface. Membrane tubules that come in contact appear to fuse with one another, and thus give rise to two-dimensional polygonal networks of tubules that have similar features to endoplasmic reticulum networks in cells. Artificial liposomes composed of dimyristoylphosphatidylcholine and yolk phosphatidylglycerol also form stable tubular structures when subjected to shear forces, but do not interact with microtubules or form polygonal networks, suggesting that such phenomena may require membrane-associated proteins. These findings indicate that kinesin generates sufficient force to form tubular membrane extensions in vitro and suggest that this microtubule-based motility protein may also be responsible for creating tubular membrane networks within cells.
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