Microscopic analysis of polymerization dynamics with individual actin filaments
Abstract
The polymerization-depolymerization dynamics of actin is a key process in a variety of cellular functions. Many spectroscopic studies have been performed in solution, but studies on single actin filaments have just begun. Here, we show that the time course of polymerization of individual filaments consists of a polymerization phase and a subsequent steady-state phase. During the steady-state phase, a treadmilling process of elongation at the barbed end and shortening at the pointed end occurs, in which both components of the process proceed at approximately the same rate. The time correlation of length fluctuation of the filaments in the steady-state phase showed that the polymerization-depolymerization dynamics follow a diffusion (stochastic) process, which cannot be explained by simple association and dissociation of monomers at both ends of the filaments.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
α-syn GCIs in MSA are insoluble and phosphorylated at serine residue 129.
“α-syn GCIs in MSA are known to be insoluble and phosphorylated at serine residue 129 [17]”
From Novel oligodendroglial alpha synuclein viral vector models of multiple system atrophy: studies in rodents and nonhuman primates (2017) · cites this paper as [17]
Cites
The Regulation of Rabbit Skeletal Muscle Contraction
Spudich, J. A., & Watt, S. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62016-2 · Cited by 4,496 · see citing works
Dynamic instability of microtubule growth
Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337 · see citing works
Mechanics of Motor Proteins and the Cytoskeleton
Howard, & Clark (2002) · Applied Mechanics Reviews · doi:10.1115/1.1451234 · Cited by 2,909 · see citing works
ACTIN AND ACTIN-BINDING PROTEINS. A CRITICAL EVALUATION OF MECHANISMS AND FUNCTIONS
Pollard, T. D., & Cooper, J. A. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005011 · Cited by 1,505 · see citing works
Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., & Yanagida, T. (1995) · Nature · doi:10.1038/374555a0 · Cited by 1,048 · see citing works
Self-citationKouyama, T., & Mihashi, K. (1981) · PubMed · Cited by 805 · see citing works
A theory of linear and helical aggregations of macromolecules
Oosawa, F., & Kasai, M. (1962) · Journal of Molecular Biology · doi:10.1016/s0022-2836(62)80112-0 · Cited by 777 · see citing works
Fluorimetry Study of N‐(1‐Pyrenyl)iodoacetamide‐Labelled F‐Actin
Kouyama, T., & Mihashi, K. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb06167.x · Cited by 722 · see citing works
Head to tail polymerization of actin
Wegner, A. (1976) · Journal of Molecular Biology · doi:10.1016/s0022-2836(76)80100-3 · Cited by 716 · see citing works
Thermodynamics of the polymerization of protein
Oosawa, F., & Asakura, S. (1975) · Cited by 580 · see citing works
Visualization of the dynamic instability of individual microtubules by dark-field microscopy
Horio, T., & Hotani, H. (1986) · Nature · doi:10.1038/321605a0 · Cited by 566 · see citing works
Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
Harada, Y., Sakurada, K., Aoki, T., Thomas, D. D., & Yanagida, T. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80060-9 · Cited by 522 · see citing works
Direct observation of motion of single F-actin filaments in the presence of myosin
Yanagida, T., Nakase, M., Nishiyama, K., & Oosawa, F. (1984) · Nature · doi:10.1038/307058a0 · Cited by 479 · see citing works
Actin Polymerization and ATP Hydrolysis
Korn, E. D., Carlier, M., & Pantaloni, D. (1987) · Science · doi:10.1126/science.3672117 · Cited by 456 · see citing works
Amann, K. J., & Pollard, T. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211556398 · Cited by 263 · see citing works
Woodrum, D. T., Rich, S. A., & Pollard, T. D. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.67.1.231 · Cited by 213 · see citing works
Tightly-bound divalent cation of actin
Estes, J. E., Selden, L. A., Kinosian, H. J., & Gershman, L. C. (1992) · Journal of Muscle Research and Cell Motility · doi:10.1007/bf01766455 · Cited by 137 · see citing works
Direct Measurement of the Torsional Rigidity of Single Actin Filaments
Yasuda, R., Miyata, H., & Kinosita, K. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0571 · Cited by 132 · see citing works
Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules
Pantaloni, D., Carlier, M., Melki, R., Combeau, C., & Valentin-Ranc, C. (1991) · AIP conference proceedings · doi:10.1063/1.40581 · Cited by 129 · see citing works
Uni-Directional Growth of F-Actin
KONDO, H., & Ishiwata, S. (1976) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131043 · Cited by 124 · see citing works
Self-citationRole of Nucleotide Hydrolysis in the Dynamics of Actin Filaments and Microtubules
Carlier, M. (1989) · International review of cytology · doi:10.1016/s0074-7696(08)60629-4 · Cited by 117 · see citing works
On the mechanism of actin monomer-polymer subunit exchange at steady state.
Brenner, S. L., & Korn, E. D. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32530-4 · Cited by 111 · see citing works
Kinetics and Thermodynamics of Phalloidin Binding to Actin Filaments from Three Divergent Species
Cruz, E. M. D. L., & Pollard, T. D. (1996) · Biochemistry · doi:10.1021/bi961047t · Cited by 97 · see citing works
Phallotoxin and actin binding assay by fluorescence enhancement
Huang, Z., Haugland, R. P., You, W., & Haugland, R. P. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90299-m · Cited by 82 · see citing works
Direct demonstration of actin filament annealing in vitro.
Murphy, D. B., Gray, R., GRASSER, W. A., et al. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.6.1947 · Cited by 72 · see citing works
Visualization and force measurement of branching by Arp2/3 complex and N-WASP in actin filament
Fujiwara, I., Suetsugu, S., Uemura, S., Takenawa, T., & Ishiwata, S. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00421-7 · Cited by 53 · see citing works
Self-citationDirectional movement of F-actin in vitro
Honda, H., Nagashima, H., & Asakura, S. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90428-6 · Cited by 47 · see citing works
Polymerization polarity of actin.
Hayashi, T., & Ip, W. (1976) · PubMed · Cited by 29 · see citing works
Molecular Interactions of Actin
(2002) · Results and problems in cell differentiation · doi:10.1007/978-3-540-46558-4 · Cited by 22 · see citing works
Microscopic Analysis of Polymerization and Fragmentation of Individual Actin Filaments
Ishiwata, S., Tadashige, J., 増井, 一., et al. (2001) · Results and problems in cell differentiation · doi:10.1007/978-3-540-46560-7_6 · Cited by 5 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Schulz-Schaeffer, W. J. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0711-0 · Cited by 627 · see citing works
Hyperphosphorylation and insolubility of α‐synuclein in transgenic mouse oligodendrocytes
Kahle, P. J., Neumann, M., Ozmen, L., Müller, V., Jacobsen, H., Spooren, W., Fuss, B., Mallon, B., Macklin, W. B., Fujiwara, H., et al. (2002) · The EMBO Reports · doi:10.1093/embo-reports/kvf109 · Cited by 314 · see citing works
Dzamko, N., Gysbers, A., Perera, G., Bahar, A., Shankar, A., Gao, J., Fu, Y., & Halliday, G. M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1648-8 · Cited by 273 · see citing works
Uchihara, T., & Giasson, B. I. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1485-1 · Cited by 249 · see citing works
Absence of α-synuclein mRNA expression in normal and multiple system atrophy oligodendroglia
Miller, D. W., Johnson, J. M., Solano, S. M., Hollingsworth, Z. R., Standaert, D. G., & Young, A. B. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-005-0378-1 · Cited by 198 · see citing works
Oliveras-Salvá, M., Van der Perren, A., Casadei, N., Stroobants, S., Nuber, S., D’Hooge, R., Van den Haute, C., & Baekelandt, V. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-44 · Cited by 191 · see citing works
Reduced striatal tyrosine hydroxylase in incidental Lewy body disease
Beach, T. G., Adler, C. H., Sue, L. I., Peirce, J. B., Bachalakuri, J., Dalsing-Hernandez, J. E., Lue, L. F., Caviness, J. N., Connor, D. J., Sabbagh, M. N., et al. (2008) · Acta Neuropathologica · doi:10.1007/s00401-007-0313-7 · Cited by 128 · see citing works
Lou, H., Montoya, S. E., Alerte, T. N. M., Wang, J., Wu, J., Peng, X., Hong, C.-S., Friedrich, E. E., Mader, S. A., Pedersen, C. J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100867 · Cited by 115 · see citing works
Does PGC1α/FNDC5/BDNF Elicit the Beneficial Effects of Exercise on Neurodegenerative Disorders?
Jodeiri Farshbaf, M., Ghaedi, K., Megraw, T. L., Curtiss, J., Shirani Faradonbeh, M., Vaziri, P., & Nasr-Esfahani, M. H. (2016) · NeuroMolecular Medicine · doi:10.1007/s12017-015-8370-x · Cited by 101 · see citing works
Neuropathology of mild cognitive impairment
Saito, Y., & Murayama, S. (2007) · Neuropathology · doi:10.1111/j.1440-1789.2007.00806.x · Cited by 92 · see citing works
Regulation of the neurodegenerative process associated to Parkinson's disease by CD4+ T-cells
González, H., Contreras, F., & Pacheco, R. (2015) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-015-9618-9 · Cited by 70 · see citing works
Mandel, R. J., Marmion, D. J., Kirik, D., Chu, Y., Heindel, C., McCown, T., Gray, S. J., & Kordower, J. H. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0451-7 · Cited by 56 · see citing works
Animal modeling an oligodendrogliopathy – multiple system atrophy
Bleasel, J. M., Halliday, G. M., & Kim, W. S. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0279-6 · Cited by 19 · see citing works
- Authors
- Fujiwara, I., Takahashi, S., Tadakuma, H., Funatsu, T., & Ishiwata, S.
- Affiliations
- Waseda University (JP)
- Corresponding author
- Ishiwata, Shin'ichi
- Venue
- Nature Cell Biology
- Published
- 2002-08-19
- Volume
- 4
- Issue
- 9
- Pages
- 666-673
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2117223239
- Cited by
- 420
- References
- 30
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 1 · 2023: 4 · 2022: 7 · 2021: 9 · 2020: 12 · 2019: 11 · 2018: 6 · 2017: 24 · 2016: 28 · 2015: 22 · 2014: 14 · 2013: 15 · 2012: 24
- FWCI
- 6.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Waseda University
- Core Research for Evolutional Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Keywords
- actin polymerization, actin depolymerization, treadmilling, diffusion, polymerization dynamics, steady-state phases
- MeSH terms
- Actins, Animals, Biopolymers, Diffusion, Kinetics, Microscopy, Fluorescence, Models, Biological, Rabbits, Stochastic Processes, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review