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Journal articles on the topic 'Treadmilling'

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Published: 4 June 2021
Last updated: 8 February 2022

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1

Rodionov, V. I. "Microtubule Treadmilling in Vivo." Science 275, no. 5297 (January 10, 1997): 215–18. http://dx.doi.org/10.1126/science.275.5297.215.

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2

York, Ashley. "Treadmilling runs bacterial division." Nature Reviews Microbiology 15, no. 4 (April 2017): 193. http://dx.doi.org/10.1038/nrmicro.2017.24.

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3

Perez, Amilcar J., Yann Cesbron, Sidney L. Shaw, Jesus Bazan Villicana, Ho-Ching T. Tsui, Michael J. Boersma, Ziyun A. Ye, et al. "Movement dynamics of divisome proteins and PBP2x:FtsW in cells of Streptococcus pneumoniae." Proceedings of the National Academy of Sciences 116, no. 8 (February 4, 2019): 3211–20. http://dx.doi.org/10.1073/pnas.1816018116.

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Bacterial cell division and peptidoglycan (PG) synthesis are orchestrated by the coordinated dynamic movement of essential protein complexes. Recent studies show that bidirectional treadmilling of FtsZ filaments/bundles is tightly coupled to and limiting for both septal PG synthesis and septum closure in some bacteria, but not in others. Here we report the dynamics of FtsZ movement leading to septal and equatorial ring formation in the ovoid-shaped pathogen, Streptococcus pneumoniae. Conventional and single-molecule total internal reflection fluorescence microscopy (TIRFm) showed that nascent rings of FtsZ and its anchoring and stabilizing proteins FtsA and EzrA move out from mature septal rings coincident with MapZ rings early in cell division. This mode of continuous nascent ring movement contrasts with a failsafe streaming mechanism of FtsZ/FtsA/EzrA observed in a ΔmapZ mutant and another Streptococcus species. This analysis also provides several parameters of FtsZ treadmilling in nascent and mature rings, including treadmilling velocity in wild-type cells and ftsZ(GTPase) mutants, lifetimes of FtsZ subunits in filaments and of entire FtsZ filaments/bundles, and the processivity length of treadmilling of FtsZ filament/bundles. In addition, we delineated the motion of the septal PBP2x transpeptidase and its FtsW glycosyl transferase-binding partner relative to FtsZ treadmilling in S. pneumoniae cells. Five lines of evidence support the conclusion that movement of the bPBP2x:FtsW complex in septa depends on PG synthesis and not on FtsZ treadmilling. Together, these results support a model in which FtsZ dynamics and associations organize and distribute septal PG synthesis, but do not control its rate in S. pneumoniae.
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4

Forer, Arthur. "Does actin produce the force that moves a chromosome to the pole during anaphase?" Canadian Journal of Biochemistry and Cell Biology 63, no. 6 (June 1, 1985): 585–98. http://dx.doi.org/10.1139/o85-077.

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Chromosomes move towards spindle poles because of force produced by chromosomal spindle fibres. I argue that actin is involved in producing this force. Actin is present in chromosomal spindle fibres, with consistent polarity. Physiological experiments using ultraviolet microbeam irradiations suggest that the force is due to an actin and myosin (or myosin-equivalent) system. Other physiological experiments (using inhibitors in "leaky" cells or antibodies injected into cells) that on the face of it would seem to rule out actin and myosin on closer scrutiny do not really do so at all. I argue that in vivo the "on" ends of chromosomal spindle fibre microtubules are at the kinetochores; I discuss the apparent contradiction between this conclusion and those from experiments on microtubules in vitro. From what we know of treadmilling in microtubules in vitro, the poleward movements of irradiation-induced areas of reduced birefringence (arb) can not be explained as treadmilling of microtubules: additional assumptions need to be made for arb movements toward the pole to be due to treadmilling. If arb movement does indeed represent treadmilling along chromosomal spindle fibre microtubules, treadmilling continues throughout anaphase. Thus I suggest that chromosomal spindle fibres shorten in anaphase not because polymerization is stopped at the kinetochore (the on end), as previously assumed, but rather because there is increased depolymerization at the pole (the "off" end).
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5

Arpağ, Göker, Elizabeth J. Lawrence, Veronica J. Farmer, Sarah L. Hall, and Marija Zanic. "Collective effects of XMAP215, EB1, CLASP2, and MCAK lead to robust microtubule treadmilling." Proceedings of the National Academy of Sciences 117, no. 23 (May 26, 2020): 12847–55. http://dx.doi.org/10.1073/pnas.2003191117.

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Microtubule network remodeling is essential for fundamental cellular processes including cell division, differentiation, and motility. Microtubules are active biological polymers whose ends stochastically and independently switch between phases of growth and shrinkage. Microtubule treadmilling, in which the microtubule plus end grows while the minus end shrinks, is observed in cells; however, the underlying mechanisms are not known. Here, we use a combination of computational and in vitro reconstitution approaches to determine the conditions leading to robust microtubule treadmilling. We find that microtubules polymerized from tubulin alone can treadmill, albeit with opposite directionality and order-of-magnitude slower rates than observed in cells. We then employ computational simulations to predict that the combinatory effects of four microtubule-associated proteins (MAPs), namely EB1, XMAP215, CLASP2, and MCAK, can promote fast and sustained plus-end-leading treadmilling. Finally, we experimentally confirm the predictions of our computational model using a multi-MAP, in vitro microtubule dynamics assay to reconstitute robust plus-end-leading treadmilling, consistent with observations in cells. Our results demonstrate how microtubule dynamics can be modulated to achieve a dynamic balance between assembly and disassembly at opposite polymer ends, resulting in treadmilling over long periods of time. Overall, we show how the collective effects of multiple components give rise to complex microtubule behavior that may be used for global network remodeling in cells.
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6

MIHASHI, KOSHIN. "Treadmilling of actin and tubulin." Seibutsu Butsuri 25, no. 2 (1985): 75–83. http://dx.doi.org/10.2142/biophys.25.75.

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7

Naoz, Moshe, Uri Manor, Hirofumi Sakaguchi, Bechara Kachar, and Nir S. Gov. "Protein Localization by Actin Treadmilling and Molecular Motors Regulates Stereocilia Shape and Treadmilling Rate." Biophysical Journal 95, no. 12 (December 2008): 5706–18. http://dx.doi.org/10.1529/biophysj.108.143453.

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8

Waterman-Storer, Clare M., and E. D. Salmon. "Microtubule dynamics: Treadmilling comes around again." Current Biology 7, no. 6 (June 1997): R369—R372. http://dx.doi.org/10.1016/s0960-9822(06)00177-1.

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9

Peglion, Florent, Flora Llense, and Sandrine Etienne-Manneville. "Adherens junction treadmilling during collective migration." Nature Cell Biology 16, no. 7 (June 15, 2014): 639–51. http://dx.doi.org/10.1038/ncb2985.

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10

Fulton, Alice B. "Treadmilling, diffusional exchange and cytoplasmic structures." Journal of Muscle Research and Cell Motility 6, no. 3 (June 1985): 263–73. http://dx.doi.org/10.1007/bf00713169.

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11

Gardet, Agnès, Michelyne Breton, Germain Trugnan, and Serge Chwetzoff. "Role for Actin in the Polarized Release of Rotavirus." Journal of Virology 81, no. 9 (February 14, 2007): 4892–94. http://dx.doi.org/10.1128/jvi.02698-06.

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ABSTRACT Rotaviruses are characterized by polarized release from the apical side of infected enterocytes, and the rotavirus VP4 spike protein specifically binds to the actin network at the apical pole of differentiated enterocytic cells. To determine the functional consequences of this VP4-actin interaction, fluorescence recovery after photobleaching experiments were carried out to measure the diffusional mobility of VP4 associated with the microfilaments. Results show that VP4 binds to barbed ends of microfilaments by using actin treadmilling. Actin treadmilling inhibition results in the loss of rotavirus apical preferential release, suggesting a major role for actin in polarized rotavirus release.
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12

Shaw, S. L. "Sustained Microtubule Treadmilling in Arabidopsis Cortical Arrays." Science 300, no. 5626 (June 13, 2003): 1715–18. http://dx.doi.org/10.1126/science.1083529.

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13

Doubrovinski, K., and K. Kruse. "Self-organization in systems of treadmilling filaments." European Physical Journal E 31, no. 1 (January 2010): 95–104. http://dx.doi.org/10.1140/epje/i2010-10548-8.

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14

Margolis, Robert L., and Leslie Wilson. "Microtubule treadmilling: what goes around comes around." BioEssays 20, no. 10 (December 12, 1998): 830–36. http://dx.doi.org/10.1002/(sici)1521-1878(199810)20:10<830::aid-bies8>3.0.co;2-n.

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15

Ishimoto, Kenta, and Darren G. Crowdy. "Dynamics of a treadmilling microswimmer near a no-slip wall in simple shear." Journal of Fluid Mechanics 821 (May 25, 2017): 647–67. http://dx.doi.org/10.1017/jfm.2017.220.

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Induction of flow is commonly used to control the migration of a microswimmer in a confined system such as a microchannel. The motion of a swimmer, in general, is governed by nonlinear equations due to non-trivial hydrodynamic interactions between the flow and the swimmer near a wall. This paper derives analytical expressions for the equations of motion governing a circular treadmilling swimmer in simple shear near a no-slip wall by combining the reciprocal theorem for Stokes flow with an exact solution for the dragging problem of a cylinder near a wall. We demonstrate that the reduced dynamical system possesses a Hamiltonian structure, which we use to show that the swimmer cannot migrate stably at a constant distance from a wall but only exhibit periodic oscillatory motion along the wall, or to escape from it. A treadmilling swimmer with the lowest two treadmilling modes is investigated in detail by means of a bifurcation analysis of the reduced dynamical system. It is found that the swimming direction of oscillatory motion is clarified by the sign of the Hamiltonian in the absence of flow, and that the induction of the flow suppresses upstream migration but aligns swimmer orientations in downstream migration. These results could inform strategies for the transport and control of micro-organisms and micromachines.
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16

Fields, R. Douglas, and Dipankar J. Dutta. "Treadmilling Model for Plasticity of the Myelin Sheath." Trends in Neurosciences 42, no. 7 (July 2019): 443–47. http://dx.doi.org/10.1016/j.tins.2019.04.002.

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17

Guo, Kunkun, Julian Shillcock, and Reinhard Lipowsky. "Treadmilling of actin filaments via Brownian dynamics simulations." Journal of Chemical Physics 133, no. 15 (October 21, 2010): 155105. http://dx.doi.org/10.1063/1.3497001.

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18

Rothwell, S. W., W. A. Grasser, and D. B. Murphy. "Direct observation of microtubule treadmilling by electron microscopy." Journal of Cell Biology 101, no. 5 (November 1, 1985): 1637–42. http://dx.doi.org/10.1083/jcb.101.5.1637.

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Using an immunoelectron microscopic procedure, we directly observed the concurrent addition and loss of chicken brain tubulin subunits from the opposite ends of microtubules containing erythrocyte tubulin domains. The polarity of growth of the brain tubulin on the ends of erythrocyte microtubules was determined to be similar to growth off the ends of Chlamydomonas axonemes. The flux rate for brain tubulin subunits in vitro was low, approximately 0.9 micron/h. Tubulin subunit flux did not continue through the entire microtubule as expected, but ceased when erythrocyte tubulin domains became exposed, resulting in a metastable configuration that persisted for at least several hours. We attribute this to differences in the critical concentrations of erythrocyte and brain tubulin. The exchange of tubulin subunits into the walls of preformed microtubules other than at their ends was also determined to be insignificant, the exchange rate being less than the sensitivity of the assay, or less than 0.2%/h.
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19

Erlenkämper, C., and K. Kruse. "Treadmilling and length distributions of active polar filaments." Journal of Chemical Physics 139, no. 16 (October 28, 2013): 164907. http://dx.doi.org/10.1063/1.4825248.

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20

Bugyi, Beáta, and Marie-France Carlier. "Control of Actin Filament Treadmilling in Cell Motility." Annual Review of Biophysics 39, no. 1 (April 2010): 449–70. http://dx.doi.org/10.1146/annurev-biophys-051309-103849.

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21

Kachar, Bechara. "Moving Encounters: Actin Treadmilling in the Brush Border." Developmental Cell 50, no. 5 (September 2019): 529–30. http://dx.doi.org/10.1016/j.devcel.2019.08.011.

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22

Selve, Norma, and Albrecht Wegner. "Rate of treadmilling of actin filaments in vitro." Journal of Molecular Biology 187, no. 4 (February 1986): 627–31. http://dx.doi.org/10.1016/0022-2836(86)90341-4.

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23

Wagner, Robert J., Kristen Such, Ethan Hobbs, and Franck J. Vernerey. "Treadmilling and dynamic protrusions in fire ant rafts." Journal of The Royal Society Interface 18, no. 179 (June 2021): 20210213. http://dx.doi.org/10.1098/rsif.2021.0213.

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Fire ants ( Solenopsis invicta ) are exemplary for their formation of cohered, buoyant and dynamic structures composed entirely of their own bodies when exposed to flooded environments. Here, we observe tether-like protrusions that emerge from aggregated fire ant rafts when docked to stationary, vertical rods. Ant rafts comprise a floating, structural network of interconnected ants on which a layer of freely active ants walk. We show here that sustained shape evolution is permitted by the competing mechanisms of perpetual raft contraction aided by the transition of bulk structural ants to the free active layer and outward raft expansion owing to the deposition of free ants into the structural network at the edges, culminating in global treadmilling. Furthermore, we see that protrusions emerge as a result of asymmetries in the edge deposition rate of free ants. Employing both experimental characterization and a model for self-propelled particles in strong confinement, we interpret that these asymmetries are likely to occur stochastically owing to wall accumulation effects and directional motion of active ants when strongly confined by the protrusions' relatively narrow boundaries. Together, these effects may realize the cooperative, yet spontaneous formation of protrusions that fire ants sometimes use for functional exploration and to escape flooded environments.
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24

Wadsworth, P., and E. D. Salmon. "Analysis of the treadmilling model during metaphase of mitosis using fluorescence redistribution after photobleaching." Journal of Cell Biology 102, no. 3 (March 1, 1986): 1032–38. http://dx.doi.org/10.1083/jcb.102.3.1032.

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One recent hypothesis for the mechanism of chromosome movement during mitosis predicts that a continual, uniform, poleward flow or "treadmilling" of microtubules occurs within the half-spindle between the chromosomes and the poles during mitosis (Margolis, R. L., and L. Wilson, 1981, Nature (Lond.), 293:705-711). We have tested this treadmilling hypothesis using fluorescent analog cytochemistry and measurements of fluorescence redistribution after photobleaching to examine microtubule behavior during metaphase of mitosis. Mitotic BSC 1 mammalian tissue culture cells or newt lung epithelial cells were microinjected with brain tubulin labeled with 5-(4,6-dichlorotriazin-2-yl) amino fluorescein (DTAF) to provide a fluorescent tracer of the endogenous tubulin pool. Using a laser microbeam, fluorescence in the half-spindle was photobleached in either a narrow 1.6 micron wide bar pattern across the half-spingle or in a circular area of 2.8 or 4.5 micron diameter. Fluorescence recovery in the spindle fibers, measured using video microscopy or photometric techniques, occurs as bleached DTAF-tubulin subunits within the microtubules are exchanged for unbleached DTAF-tubulin in the cytosol by steady-state microtubule assembly-disassembly pathways. Recovery of 75% of the bleached fluorescence follows first-order kinetics and has an average half-time of 37 sec, at 31-33 degrees C. No translocation of the bleached bar region could be detected during fluorescence recovery, and the rate of recovery was independent of the size of the bleached spot. These results reveal that, for 75% of the half-spindle microtubules, FRAP does not occur by a synchronous treadmilling mechanism.
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25

Nakamura, Masayoshi, Jelmer J. Lindeboom, Marco Saltini, Bela M. Mulder, and David W. Ehrhardt. "SPR2 protects minus ends to promote severing and reorientation of plant cortical microtubule arrays." Journal of Cell Biology 217, no. 3 (January 16, 2018): 915–27. http://dx.doi.org/10.1083/jcb.201708130.

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The cortical microtubule arrays of higher plants are organized without centrosomes and feature treadmilling polymers that are dynamic at both ends. The control of polymer end stability is fundamental for the assembly and organization of cytoskeletal arrays, yet relatively little is understood about how microtubule minus ends are controlled in acentrosomal microtubule arrays, and no factors have been identified that act at the treadmilling minus ends in higher plants. Here, we identify Arabidopsis thaliana SPIRAL2 (SPR2) as a protein that tracks minus ends and protects them against subunit loss. SPR2 function is required to facilitate the rapid reorientation of plant cortical arrays as stimulated by light perception, a process that is driven by microtubule severing to create a new population of microtubules. Quantitative live-cell imaging and computer simulations reveal that minus protection by SPR2 acts by an unexpected mechanism to promote the lifetime of potential SPR2 severing sites, increasing the likelihood of severing and thus the rapid amplification of the new microtubule array.
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26

HERRMANN, K. H., S. V. M. SATYANARAYANA, V. SRIDHAR, and K. P. N. MURTHY. "MONTE CARLO SIMULATION OF ACTIN FILAMENT BASED CELL MOTILITY." International Journal of Modern Physics B 17, no. 29 (November 20, 2003): 5597–611. http://dx.doi.org/10.1142/s0217979203023288.

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Cell motility resulting from actin polymerization is modeled on a two-dimensional square lattice. The treadmilling of actin filaments, formation of lamellipodia, protrusion and motility of the model cell are studied using Monte Carlo simulations. The grid space of the square lattice and the Monte Carlo step are related to length and time scales of the problem. The average velocity computed with this prescription from the simulations shows a remarkable agreement with the experimental velocity of a keratocyte. The model cell captures the essential aspects of treadmilling based motility. The movement of the model cell is diffusive for small times and exhibits a cross over to polymerization driven drift for large times. The studies on the parameter sensitivity of cell velocity indicated that the optimal choice of number of monomers, the number of filaments, the rate of depolymerization and the monomer diffusion leads to large velocities. The cell velocity distribution is found to be Gaussian and is in agreement with some of the experimental work.
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27

Le Clainche, Christophe, and Marie-France Carlier. "Regulation of Actin Assembly Associated With Protrusion and Adhesion in Cell Migration." Physiological Reviews 88, no. 2 (April 2008): 489–513. http://dx.doi.org/10.1152/physrev.00021.2007.

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To migrate, a cell first extends protrusions such as lamellipodia and filopodia, forms adhesions, and finally retracts its tail. The actin cytoskeleton plays a major role in this process. The first part of this review (sect. ii) describes the formation of the lamellipodial and filopodial actin networks. In lamellipodia, the WASP-Arp2/3 pathways generate a branched filament array. This polarized dendritic actin array is maintained in rapid treadmilling by the concerted action of ADF, profilin, and capping proteins. In filopodia, formins catalyze the processive assembly of nonbranched actin filaments. Cell matrix adhesions mechanically couple actin filaments to the substrate to convert the treadmilling into protrusion and the actomyosin contraction into traction of the cell body and retraction of the tail. The second part of this review (sect. iii) focuses on the function and the regulation of major proteins (vinculin, talin, tensin, and α-actinin) that control the nucleation, the binding, and the barbed-end growth of actin filaments in adhesions.
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28

Maly, I. "Self-organization of treadmilling microtubules into a polar array." Trends in Cell Biology 12, no. 10 (October 1, 2002): 462–65. http://dx.doi.org/10.1016/s0962-8924(02)02369-3.

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29

Small, J. Victor. "Getting the actin filaments straight: nucleation-release or treadmilling?" Trends in Cell Biology 5, no. 2 (February 1995): 52–55. http://dx.doi.org/10.1016/s0962-8924(00)88939-4.

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30

Ni, Qin, and Garegin A. Papoian. "Turnover versus treadmilling in actin network assembly and remodeling." Cytoskeleton 76, no. 11-12 (October 9, 2019): 562–70. http://dx.doi.org/10.1002/cm.21564.

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31

Abeyaratne, Rohan, Eric Puntel, and Giuseppe Tomassetti. "Treadmilling stability of a one-dimensional actin growth model." International Journal of Solids and Structures 198 (August 2020): 87–98. http://dx.doi.org/10.1016/j.ijsolstr.2020.04.009.

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32

Narita, Akihiro. "Minimum requirements for the actin-like treadmilling motor system." BioArchitecture 1, no. 5 (September 2011): 205–8. http://dx.doi.org/10.4161/bioa.18115.

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33

Weber, Michele, and Michael Sixt. "MEK signalling tunes actin treadmilling for interstitial lymphocyte migration." EMBO Journal 29, no. 17 (September 1, 2010): 2861–63. http://dx.doi.org/10.1038/emboj.2010.183.

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34

Lyu, Zhixin, David Weiss, and Jie Xiao. "Ftsn Bridges the FtsZ-Treadmilling and Septal Peptidoglycan Synthesis." Biophysical Journal 116, no. 3 (February 2019): 278a. http://dx.doi.org/10.1016/j.bpj.2018.11.1506.

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35

Arpag, Goker, and Marija Zanic. "Dynamic Instability and Treadmilling Coexist for In Vitro Microtubules." Biophysical Journal 116, no. 3 (February 2019): 157a. http://dx.doi.org/10.1016/j.bpj.2018.11.869.

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36

Chaikeeratisak, Vorrapon, Kanika Khanna, Katrina T. Nguyen, Joseph Sugie, MacKennon E. Egan, Marcella L. Erb, Anastasia Vavilina, et al. "Viral Capsid Trafficking along Treadmilling Tubulin Filaments in Bacteria." Cell 177, no. 7 (June 2019): 1771–80. http://dx.doi.org/10.1016/j.cell.2019.05.032.

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37

Loomis, Patricia A., Lili Zheng, Gabriella Sekerková, Benjarat Changyaleket, Enrico Mugnaini, and James R. Bartles. "Espin cross-links cause the elongation of microvillus-type parallel actin bundles in vivo." Journal of Cell Biology 163, no. 5 (December 1, 2003): 1045–55. http://dx.doi.org/10.1083/jcb.200309093.

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The espin actin-bundling proteins, which are the target of the jerker deafness mutation, caused a dramatic, concentration-dependent lengthening of LLC-PK1-CL4 cell microvilli and their parallel actin bundles. Espin level was also positively correlated with stereocilium length in hair cells. Villin, but not fascin or fimbrin, also produced noticeable lengthening. The espin COOH-terminal peptide, which contains the actin-bundling module, was necessary and sufficient for lengthening. Lengthening was blocked by 100 nM cytochalasin D. Espin cross-links slowed actin depolymerization in vitro less than twofold. Elimination of an actin monomer-binding WASP homology 2 domain and a profilin-binding proline-rich domain from espin did not decrease lengthening, but made it possible to demonstrate that actin incorporation was restricted to the microvillar tip and that bundles continued to undergo actin treadmilling at ∼1.5 s−1 during and after lengthening. Thus, through relatively subtle effects on actin polymerization/depolymerization reactions in a treadmilling parallel actin bundle, espin cross-links cause pronounced barbed-end elongation and, thereby, make a longer bundle without joining shorter modules.
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38

Wanger, Michael, Thomas Keiser, Jean-Marc Neuhaus, and Albrecht Wegner. "The actin treadmill." Canadian Journal of Biochemistry and Cell Biology 63, no. 6 (June 1, 1985): 414–21. http://dx.doi.org/10.1139/o85-060.

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Actin filaments can assemble at the barbed end and disassemble simultaneously at the pointed end. Prerequisites for this treadmilling reaction are the structural polarity of actin filaments and tight coupling of the actin assembly reaction and the adenosine triphosphate hydrolysis occurring during actin polymerization. In this article, investigations on the actin treadmill are reviewed.
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39

Panda, Dulal, Gopal Chakrabarti, Jon Hudson, Karli Pigg, Herbert P. Miller, Leslie Wilson, and Richard H. Himes. "Suppression of Microtubule Dynamic Instability and Treadmilling by Deuterium Oxide†." Biochemistry 39, no. 17 (May 2000): 5075–81. http://dx.doi.org/10.1021/bi992217f.

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40

Ramirez-Diaz, Diego A., Daniela A. García-Soriano, Ana Raso, Jonas Mücksch, Mario Feingold, Germán Rivas, and Petra Schwille. "Treadmilling analysis reveals new insights into dynamic FtsZ ring architecture." PLOS Biology 16, no. 5 (May 18, 2018): e2004845. http://dx.doi.org/10.1371/journal.pbio.2004845.

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41

Monteiro, João M., Ana R. Pereira, Nathalie T. Reichmann, Bruno M. Saraiva, Pedro B. Fernandes, Helena Veiga, Andreia C. Tavares, et al. "Peptidoglycan synthesis drives an FtsZ-treadmilling-independent step of cytokinesis." Nature 554, no. 7693 (February 2018): 528–32. http://dx.doi.org/10.1038/nature25506.

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42

Arpag, Goker, Elizabeth Lawrence, and Marija Zanic. "Microtubule Treadmilling Reconstituted with a Minimal-component in vitro System." Biophysical Journal 118, no. 3 (February 2020): 32a. http://dx.doi.org/10.1016/j.bpj.2019.11.353.

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43

Schumacher, Maria A., Tomoo Ohashi, Lauren Corbin, and Harold P. Erickson. "High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP." Acta Crystallographica Section F Structural Biology Communications 76, no. 2 (February 1, 2020): 94–102. http://dx.doi.org/10.1107/s2053230x20001132.

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Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R) state, favored for monomers, to a tense (T) conformation, which is favored upon association into filaments. The R conformation has been observed in numerous monomeric FtsZ crystal structures and the T conformation in Staphylococcus aureus FtsZ crystallized as assembled filaments. However, while Escherichia coli has served as a main model system for the study of the Z-ring and the associated divisome, a structure has not yet been reported for E. coli FtsZ. To address this gap, structures were determined of the E. coli FtsZ mutant FtsZ(L178E) with GDP and GTP bound to 1.35 and 1.40 Å resolution, respectively. The E. coli FtsZ(L178E) structures both crystallized as straight filaments with subunits in the R conformation. These high-resolution structures can be employed to facilitate experimental cell-division studies and their interpretation in E. coli.
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44

Bayley, P. M., M. J. Schilstra, and S. R. Martin. "A simple formulation of microtubule dynamics: quantitative implications of the dynamic instability of microtubule populations in vivo and in vitro." Journal of Cell Science 93, no. 2 (June 1, 1989): 241–54. http://dx.doi.org/10.1242/jcs.93.2.241.

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A simple formulation of microtubule dynamic instability is presented, which is based on the experimental observations by T. Horio and H. Hotani of coexisting, interconverting growing and shrinking microtubules. Employing only three independent, experimentally determined parameters for a given microtubule end, this treatment accounts quantitatively for the principal features of the observed dynamic behaviour of steady-state tubulin microtubules in vitro. Experimental data are readily reproduced for microtubule length redistribution, and for the kinetics of tubulin exchange processes, including pulse-chase properties. The relative importance of dynamic incorporation and that due to treadmilling are assessed. Dynamic incorporation is found to dominate the overall exchange properties; polarized incorporation due to treadmilling generally becomes significant only when the dynamics are largely suppressed. This treatment also permits simulation of certain cellular phenomena, showing how microtubule renucleation can control microtubule growth, by means of changes in microtubule number concentration in a system at constant microtubule mass. A relatively simple extension of the formulation accounts quantitatively for non-steady-state microtubule properties, e.g. dilution-induced rapid disassembly and the oscillatory mode of microtubule assembly. The principles relating dynamic instability and oscillatory behaviour are clearly indicated. Possible mechanisms of the switching of microtubules are briefly discussed.
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45

Chomicki, Guillaume, Raymond Wightman, and Simon R. Turner. "A Specific Class of Short Treadmilling Microtubules Enhances Cortical Microtubule Alignment." Molecular Plant 9, no. 8 (August 2016): 1214–16. http://dx.doi.org/10.1016/j.molp.2016.05.008.

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46

Grego, Sonia, Viviana Cantillana, and E. D. Salmon. "Microtubule Treadmilling in Vitro Investigated by Fluorescence Speckle and Confocal Microscopy." Biophysical Journal 81, no. 1 (July 2001): 66–78. http://dx.doi.org/10.1016/s0006-3495(01)75680-9.

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47

Oelz, Dietmar, and Alex Mogilner. "Actomyosin contraction, aggregation and traveling waves in a treadmilling actin array." Physica D: Nonlinear Phenomena 318-319 (April 2016): 70–83. http://dx.doi.org/10.1016/j.physd.2015.10.005.

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48

Bisson-Filho, Alexandre W., Yen-Pang Hsu, Georgia R. Squyres, Erkin Kuru, Fabai Wu, Calum Jukes, Yingjie Sun, et al. "Treadmilling by FtsZ filaments drives peptidoglycan synthesis and bacterial cell division." Science 355, no. 6326 (February 16, 2017): 739–43. http://dx.doi.org/10.1126/science.aak9973.

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49

Hotani, Hirokazu, and Tetsuya Horio. "Dynamics of microtubules visualized by darkfield microscopy: Treadmilling and dynamic instability." Cell Motility and the Cytoskeleton 10, no. 1-2 (1988): 229–36. http://dx.doi.org/10.1002/cm.970100127.

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50

Crowdy, Darren. "Treadmilling swimmers near a no-slip wall at low Reynolds number." International Journal of Non-Linear Mechanics 46, no. 4 (May 2011): 577–85. http://dx.doi.org/10.1016/j.ijnonlinmec.2010.12.010.

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