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Kinetic Mechanism of Blebbistatin Inhibition of Nonmuscle Myosin IIB†

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Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, Philadelphia, Pennsylvania 19104, and Department of Cell Biology and Institute of Chemistry and Cell Biology, Harvard Medical School, 250 Longwood Avenue, Boston, Massachusetts 02115
Cite this: Biochemistry 2004, 43, 46, 14832–14839
Publication Date (Web):October 28, 2004
https://doi.org/10.1021/bi0490284
Copyright © 2004 American Chemical Society
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    Abstract

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    We examined the effect of blebbistatin on the kinetic properties of nonmuscle myosin IIB subfragment 1 (NMIIB S1). Blebbistatin is a small molecule that affects cell blebbing during the process of cell division, which has been shown to decrease the myosin ATPase activity of a number of myosins [Straight et al. (2003) Science 299, 1743−1747]. The steady-state actin-activated ATPase activity of NMIIB S1 was decreased ∼90% at 40 μM actin in the presence of blebbistatin. Stopped-flow techniques were employed to elucidate the effect of blebbistatin on the various steps of the NMIIB S1 cross-bridge cycle. Blebbistatin did not affect ATP binding and hydrolysis. Binding to actin in the presence of ADP (0.57 ± 0.08 μM-1 s-1) was reduced slightly in the presence of blebbistatin (0.38 ± 0.03 μM-1 s-1), while mantADP dissociation from acto-NMIIB S1 was reduced (∼30%). Pi release was blocked in the presence of blebbistatin. Accordingly, the apparent affinity of NMIIB S1 for actin in the presence of ATP was greatly reduced. Based on the above data, we surmise that blebbistatin inhibits the ATPase activity of NMIIB S1 primarily by blocking entry into the strong binding state; secondarily, it reduces the rate of ADP release. These effects are likely mediated by binding of blebbistatin within the myosin cleft that progressively closes in forming the acto-myosin rigor state.

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    †

     This study was supported by a grant from NIH, No. RO1 AR35661 to H.L.S.

    ‡

     University of Pennsylvania School of Medicine.

    §

     Current address:  Department of Biology, University of North Carolina at Charlotte, 9201 University City Blvd., Charlotte, NC 28223.

    ⊥

     Harvard Medical School.

    ‖

     Current Address:  Department of Biochemistry, Stanford University School of Medicine, B409A, 279 Campus Drive, Stanford, CA 94305-5307

    *

     Corresponding author. Mailing address:  Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, B400 Richards Building, Philadelphia, PA 19104-6085. Phone:  215-898-8726. Fax:  215-573-2273. E-mail:  [email protected].

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    21. Wiebke Ewert, Peter Franz, Georgios Tsiavaliaris, Matthias Preller. Structural and Computational Insights into a Blebbistatin-Bound Myosin•ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke. International Journal of Molecular Sciences 2020, 21 (19) , 7417. https://doi.org/10.3390/ijms21197417
    22. Dietmar J. Manstein, Matthias Preller. Small Molecule Effectors of Myosin Function. 2020, 61-84. https://doi.org/10.1007/978-3-030-38062-5_5
    23. Anna Á. Rauscher, Máté Gyimesi, Mihály Kovács, András Málnási-Csizmadia. Targeting Myosin by Blebbistatin Derivatives: Optimization and Pharmacological Potential. Trends in Biochemical Sciences 2018, 43 (9) , 700-713. https://doi.org/10.1016/j.tibs.2018.06.006
    24. Weikang Ma, Henry Gong, Thomas Irving. Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle. International Journal of Molecular Sciences 2018, 19 (9) , 2643. https://doi.org/10.3390/ijms19092643
    25. Mohammad A. Rahman, Marko Ušaj, Dilson E. Rassier, Alf Månsson. Blebbistatin Effects Expose Hidden Secrets in the Force-Generating Cycle of Actin and Myosin. Biophysical Journal 2018, 115 (2) , 386-397. https://doi.org/10.1016/j.bpj.2018.05.037
    26. Natalie C. Heer, Adam C. Martin. Tension, contraction and tissue morphogenesis. Development 2017, 144 (23) , 4249-4260. https://doi.org/10.1242/dev.151282
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    41. Sarah M. Heissler, Dietmar J. Manstein. Nonmuscle myosin-2: mix and match. Cellular and Molecular Life Sciences 2013, 70 (1) , 1-21. https://doi.org/10.1007/s00018-012-1002-9
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    45. David Van Goor, Callen Hyland, Andrew W. Schaefer, Paul Forscher, . The Role of Actin Turnover in Retrograde Actin Network Flow in Neuronal Growth Cones. PLoS ONE 2012, 7 (2) , e30959. https://doi.org/10.1371/journal.pone.0030959
    46. Fabio C. Minozzo, Lennart Hilbert, Dilson E. Rassier, . Pre-Power-Stroke Cross-Bridges Contribute to Force Transients during Imposed Shortening in Isolated Muscle Fibers. PLoS ONE 2012, 7 (1) , e29356. https://doi.org/10.1371/journal.pone.0029356
    47. M. Preller, D.J. Manstein. 4.8 Myosin Motors: Structural Aspects and Functionality. 2012, 118-150. https://doi.org/10.1016/B978-0-12-374920-8.00410-0
    48. Cathy C Moore. Nonmuscle myosin II regulates migration but not contraction in rat hepatic stellate cells. World Journal of Hepatology 2011, 3 (7) , 184. https://doi.org/10.4254/wjh.v3.i7.184
    49. Stephanie I. Fraley, Christopher M. Hale, Ryan J. Bloom, Alfredo Celedon, Jerry S. H. Lee, Denis Wirtz. Intra- and Extracellular Microrheology of Endothelial Cells in a 3D Matrix. 2011, 69-87. https://doi.org/10.1007/978-1-4419-7835-6_4
    50. Balázs Takács, Neil Billington, Máté Gyimesi, Bálint Kintses, András Málnási-Csizmadia, Peter J. Knight, Mihály Kovács. Myosin complexed with ADP and blebbistatin reversibly adopts a conformation resembling the start point of the working stroke. Proceedings of the National Academy of Sciences 2010, 107 (15) , 6799-6804. https://doi.org/10.1073/pnas.0907585107
    51. Christopher M. Hale, Sean X. Sun, Denis Wirtz, . Resolving the Role of Actoymyosin Contractility in Cell Microrheology. PLoS ONE 2009, 4 (9) , e7054. https://doi.org/10.1371/journal.pone.0007054
    52. Hiroyuki Iwamoto. Evidence for Unique Structural Change of Thin Filaments upon Calcium Activation of Insect Flight Muscle. Journal of Molecular Biology 2009, 390 (1) , 99-111. https://doi.org/10.1016/j.jmb.2009.05.002
    53. Sengen Xu, Howard D. White, Gerald W. Offer, Leepo C. Yu. Stabilization of Helical Order in the Thick Filaments by Blebbistatin: Further Evidence of Coexisting Multiple Conformations of Myosin. Biophysical Journal 2009, 96 (9) , 3673-3681. https://doi.org/10.1016/j.bpj.2009.01.049
    54. Chambers C. Hughes, John B. MacMillan, Susana P. Gaudêncio, William Fenical, James J. La Clair. Ammosamides A and B Target Myosin. Angewandte Chemie International Edition 2009, 48 (4) , 728-732. https://doi.org/10.1002/anie.200804107
    55. Chambers C. Hughes, John B. MacMillan, Susana P. Gaudêncio, William Fenical, James J. La Clair. Ammosamides A and B Target Myosin. Angewandte Chemie 2009, 121 (4) , 742-746. https://doi.org/10.1002/ange.200804107
    56. Zoe M. Goeckeler, Paul C. Bridgman, Robert B. Wysolmerski. Nonmuscle myosin II is responsible for maintaining endothelial cell basal tone and stress fiber integrity. American Journal of Physiology-Cell Physiology 2008, 295 (4) , C994-C1006. https://doi.org/10.1152/ajpcell.00318.2008
    57. Ryan J. Bloom, Jerry P. George, Alfredo Celedon, Sean X. Sun, Denis Wirtz. Mapping Local Matrix Remodeling Induced by a Migrating Tumor Cell Using Three-Dimensional Multiple-Particle Tracking. Biophysical Journal 2008, 95 (8) , 4077-4088. https://doi.org/10.1529/biophysj.108.132738
    58. Fa-Qing Zhao, Raúl Padrón, Roger Craig. Blebbistatin Stabilizes the Helical Order of Myosin Filaments by Promoting the Switch 2 Closed State. Biophysical Journal 2008, 95 (7) , 3322-3329. https://doi.org/10.1529/biophysj.108.137067
    59. Hong Hui Wang, Hideyuki Tanaka, Xiaoran Qin, Tiejun Zhao, Li-Hong Ye, Tuyoshi Okagaki, Takeshi Katayama, Akio Nakamura, Ryoki Ishikawa, Sean E. Thatcher, Gary L. Wright, Kazuhiro Kohama. Blebbistatin inhibits the chemotaxis of vascular smooth muscle cells by disrupting the myosin II-actin interaction. American Journal of Physiology-Heart and Circulatory Physiology 2008, 294 (5) , H2060-H2068. https://doi.org/10.1152/ajpheart.00970.2007
    60. Guillaume T. Charras, Margaret Coughlin, Timothy J. Mitchison, L. Mahadevan. Life and Times of a Cellular Bleb. Biophysical Journal 2008, 94 (5) , 1836-1853. https://doi.org/10.1529/biophysj.107.113605
    61. Cristina Lucas-Lopez, John S. Allingham, Tomas Lebl, Christopher P. A. T. Lawson, Ruth Brenk, James R. Sellers, Ivan Rayment, Nicholas J. Westwood. The small molecule tool (S)-(−)-blebbistatin: novel insights of relevance to myosin inhibitor design. Organic & Biomolecular Chemistry 2008, 6 (12) , 2076. https://doi.org/10.1039/b801223g
    62. Ying Dou, Per Arlock, Anders Arner. Blebbistatin specifically inhibits actin-myosin interaction in mouse cardiac muscle. American Journal of Physiology-Cell Physiology 2007, 293 (3) , C1148-C1153. https://doi.org/10.1152/ajpcell.00551.2006
    63. Colin P. Johnson, Hsin-Yao Tang, Christine Carag, David W. Speicher, Dennis E. Discher. Forced Unfolding of Proteins Within Cells. Science 2007, 317 (5838) , 663-666. https://doi.org/10.1126/science.1139857
    64. G.J. JOHNSON, L.A. LEIS, M.D. KRUMWIEDE, J.G. WHITE. The critical role of myosin IIA in platelet internal contraction. Journal of Thrombosis and Haemostasis 2007, 5 (7) , 1516-1529. https://doi.org/10.1111/j.1538-7836.2007.02611.x
    65. H Lee Sweeney, Hyokeun Park, Alan B Zong, Zhaohui Yang, Paul R Selvin, Steven S Rosenfeld. How myosin VI coordinates its heads during processive movement. The EMBO Journal 2007, 26 (11) , 2682-2692. https://doi.org/10.1038/sj.emboj.7601720
    66. Manli Chuai, Wei Zeng, Xuesong Yang, Veronika Boychenko, James A. Glazier, Cornelis J. Weijer. Cell movement during chick primitive streak formation. Developmental Biology 2006, 296 (1) , 137-149. https://doi.org/10.1016/j.ydbio.2006.04.451
    67. Nelson A. Medeiros, Dylan T. Burnette, Paul Forscher. Myosin II functions in actin-bundle turnover in neuronal growth cones. Nature Cell Biology 2006, 8 (3) , 216-226. https://doi.org/10.1038/ncb1367
    68. Sara Matson, Styliani Markoulaki, Tom Ducibella. Antagonists of Myosin Light Chain Kinase and of Myosin II Inhibit Specific Events of Egg Activation in Fertilized Mouse Eggs1. Biology of Reproduction 2006, 74 (1) , 169-176. https://doi.org/10.1095/biolreprod.105.046409
    69. Wayne Chan, German Calderon, Amy L. Swift, Jamie Moseley, Shaohua Li, Hiroshi Hosoya, Irwin M. Arias, Daniel F. Ortiz. Myosin II Regulatory Light Chain Is Required for Trafficking of Bile Salt Export Protein to the Apical Membrane in Madin-Darby Canine Kidney Cells. Journal of Biological Chemistry 2005, 280 (25) , 23741-23747. https://doi.org/10.1074/jbc.M502767200
    70. John S Allingham, Robert Smith, Ivan Rayment. The structural basis of blebbistatin inhibition and specificity for myosin II. Nature Structural & Molecular Biology 2005, 12 (4) , 378-379. https://doi.org/10.1038/nsmb908
    71. Shi Shu, Xiong Liu, Edward D. Korn. Blebbistatin and blebbistatin-inactivated myosin II inhibit myosin II-independent processes in Dictyostelium. Proceedings of the National Academy of Sciences 2005, 102 (5) , 1472-1477. https://doi.org/10.1073/pnas.0409528102
    72. Mary Anne Conti, Sachiyo Kawamoto, Robert S. Adelstein. Non-Muscle Myosin II. , 223-264. https://doi.org/10.1007/978-1-4020-6519-4_7
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