The DOI matches its Crossref record.
Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
Abstract
Cofilin, a 21 000 molecular weight protein of porcine brain, reacts stoichiometrically with actin in a 1:1 molar ratio. Upon binding of cofilin, the fluorescence of pyrene-labeled actin under polymerizing conditions is changed into the monomer form, irrespective of whether cofilin is added to actin before or after polymerization. Cofilin decreases the viscosity of actin filaments but increases the light-scattering intensity of the filaments. The centrifugation assay and the DNase I inhibition assay demonstrate that cofilin binds to actin filaments in a 1:1 molar ratio of cofilin to actin monomer in the filament and that cofilin increases the monomeric actin to a limited extent (up to 1.1-1.5 microM monomer) in the presence of physiological concentrations of Mg2+ and KCl. Cofilin is also able to bind to monomeric actin, as demonstrated by gel filtration. Electron microscopy showed that actin filaments are shortened and slightly thickened in the presence of cofilin. No bundle formation was observed in the presence of various concentrations of cofilin. The gel point assay using an actin cross-linking protein and the nucleation assay also suggested that cofilin shortens the actin filaments and hence increases the filament number. Cofilin blocks the binding of tropomyosin to actin filaments. Tropomyosin is dissociated from actin filaments by the binding of cofilin to actin filaments. Cofilin was found to inhibit the superprecipitation of actin-myosin mixtures as well as the actin-activated myosin ATPase. All these results suggest that cofilin is a new type of actin-associated protein.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Carlier, M.-F., Laurent, V., Santolini, J., Melki, R., Didry, D., Xia, G.-X., Hong, Y., Chua, N.-H., & Pantaloni, D. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.6.1307 · Cited by 1,049
Tropomyosin-Based Regulation of the Actin Cytoskeleton in Time and Space
Gunning, P., O’neill, G., & Hardeman, E. (2008) · Physiological Reviews · doi:10.1152/physrev.00001.2007 · Cited by 478
Reactivation of Phosphorylated Actin Depolymerizing Factor and Identification of the Regulatory Site
Agnew, B. J., Minamide, L. S., & Bamburg, J. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17582 · Cited by 377
Ins and outs of ADF/cofilin activity and regulation
Van Troys, M., Huyck, L., Leyman, S., Dhaese, S., Vandekerkhove, J., & Ampe, C. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.04.001 · Cited by 329
Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.
Koyasu, S., Nishida, E., Kadowaki, T., Matsuzaki, F., Iida, K., Harada, F., Kasuga, M., Sakai, H., & Yahara, I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8054 · Cited by 329
Self-citationRole of actin cytoskeleton in dendritic spine morphogenesis
Sekino, Y., Kojima, N., & Shirao, T. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.04.029 · Cited by 294
Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
Hawkins, M., Pope, B., Maciver, S. K., & Weeds, A. G. (1993) · Biochemistry · doi:10.1021/bi00089a014 · Cited by 277
Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells.
Nishida, E., Iida, K., Yonezawa, N., Koyasu, S., Yahara, I., & Sakai, H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5262 · Cited by 275
Self-citationF-Actin Cytoskeleton Network Self-Organization Through Competition and Cooperation
Kadzik, R. S., Homa, K. E., & Kovar, D. R. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-032320-094706 · Cited by 120
Distribution among tissues and intracellular localization of cofilin, a 21kDa actin-binding protein.
Yonezawa, N., Nishida, E., Koyasu, S., Maekawa, S., Ohta, Y., Yahara, I., & Sakai, H. (1987) · Cell Structure and Function · doi:10.1247/csf.12.443 · Cited by 60
Self-citationThe actin remodeling protein cofilin is crucial for thymic αβ but not γδ T-cell development
Seeland, I., Xiong, Y., Orlik, C., Deibel, D., Prokosch, S., Küblbeck, G., Jahraus, B., De Stefano, D., Moos, S., Kurschus, F. C., et al. (2018) · PLOS Biology · doi:10.1371/journal.pbio.2005380 · Cited by 12
Metadata
- Authors
- Nishida, E., Maekawa, S., & Sakai, H.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1984-10-01
- Volume
- 23
- Issue
- 22
- Pages
- 5307-5313
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1963892030
- Cited by
- 313
- References
- 0
- FWCI
- 2.93
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
