The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Mechanism of Blebbistatin Inhibition of Myosin II
Open accessAbstract
Blebbistatin is a recently discovered small molecule inhibitor showing high affinity and selectivity toward myosin II. Here we report a detailed investigation of its mechanism of inhibition. Blebbistatin does not compete with nucleotide binding to the skeletal muscle myosin subfragment-1. The inhibitor preferentially binds to the ATPase intermediate with ADP and phosphate bound at the active site, and it slows down phosphate release. Blebbistatin interferes neither with binding of myosin to actin nor with ATP-induced actomyosin dissociation. Instead, it blocks the myosin heads in a products complex with low actin affinity. Blind docking molecular simulations indicate that the productive blebbistatin-binding site of the myosin head is within the aqueous cavity between the nucleotide pocket and the cleft of the actin-binding interface. The property that blebbistatin blocks myosin II in an actin-detached state makes the compound useful both in muscle physiology and in exploring the cellular function of cytoplasmic myosin II isoforms, whereas the stabilization of a specific myosin intermediate confers a great potential in structural studies.
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Cites
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Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor
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Structural Mechanism of Muscle Contraction
Geeves, M. A., & Holmes, K. C. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.687 · Cited by 781
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Efficient docking of peptides to proteins without prior knowledge of the binding site
Hetényi, C., & van der Spoel, D. (2002) · Protein Science · doi:10.1110/ps.0202302 · Cited by 450
Self-citationSpecificity of blebbistatin, an inhibitor of myosin II
Limouze, J., Straight, A. F., Mitchison, T., & Sellers, J. R. (2004) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-004-6060-7 · Cited by 386
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Cited by
Mechanical compression drives cancer cells toward invasive phenotype
Tse, J. M., Cheng, G., Tyrrell, J. A., Wilcox-Adelman, S. A., Boucher, Y., Jain, R. K., & Munn, L. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118910109 · Cited by 631
Tsai, R. K., & Discher, D. E. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708043 · Cited by 486
Feng, X., Arang, N., Rigiracciolo, D. C., Lee, J. S., Yeerna, H., Wang, Z., Lubrano, S., Kishore, A., Pachter, J. A., König, G. M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.009 · Cited by 237
Mechano-modulatory synthetic niches for liver organoid derivation
Sorrentino, G., Rezakhani, S., Yildiz, E., Nuciforo, S., Heim, M. H., Lutolf, M. P., & Schoonjans, K. (2020) · Nature Communications · doi:10.1038/s41467-020-17161-0 · Cited by 224
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Metadata
- Authors
- Kovács, M., Tóth, J., Hetényi, C., Málnási-Csizmadia, A., & Sellers, J. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-08
- Volume
- 279
- Issue
- 34
- Pages
- 35557-35563
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2009582775
- Cited by
- 1,019
- References
- 21
- FWCI
- 13.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kovács, M., Tóth, J., Hetényi, C., Málnási-Csizmadia, A., & Sellers, J. R. (2004). Mechanism of Blebbistatin Inhibition of Myosin II. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m405319200
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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.
