ArticleProceedings of the National Academy of Sciences of the United States of America2005
Blebbistatin and blebbistatin-inactivated myosin II inhibit myosin II-independent processes in Dictyostelium.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 107 citations in OpenAlex.
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- Formation and closure of macropinocytic cups in Dictyostelium.Current biology : CB · 2023Article
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- Tuning of Liver Sieve: The Interplay between Actin and Myosin Regulatory Light Chain Regulates Fenestration Size and Number in Murine Liver Sinusoidal Endothelial Cells.International journal of molecular sciences · 2022Article
- The Amoebal Model for Macropinocytosis.Sub-cellular biochemistry · 2022Article
- Non-muscle myosin II regulates aortic stiffness through effects on specific focal adhesion proteins and the non-muscle cortical cytoskeleton.Journal of cellular and molecular medicine · 2021Article
- Using Live-Cell Imaging and Synthetic Biology to Probe Directed Migration inFrontiers in cell and developmental biology · 2021Review
- Dynamics ofFrontiers in cellular and infection microbiology · 2020Article
- Force Spectrum Microscopy Using Mitochondrial Fluctuations of Control and ATP-Depleted Cells.Biophysical journal · 2018Article
- The physiological regulation of macropinocytosis duringJournal of cell science · 2018Article
- Mechanical phenotyping of K562 cells by the Micropipette Aspiration Technique allows identifying mechanical changes induced by drugs.Scientific reports · 2018Article
- Article
- Extracellular matrix stiffness causes systematic variations in proliferation and chemosensitivity in myeloid leukemias.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Active Traction Force Response to Long-Term Cyclic Stretch Is Dependent on Cell Pre-stress.Biophysical journal · 2016Article
- Macrophage engulfment of a cell or nanoparticle is regulated by unavoidable opsonization, a species-specific 'Marker of Self' CD47, and target physical properties.Current opinion in immunology · 2015Review
- Kinetic characterization of the sole nonmuscle myosin-2 from the model organism Drosophila melanogaster.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Blebbistatin, a cell-permeable inhibitor of class-II myosins, was developed to provide a tool for studying the biologic roles of myosin II. Consistent with this use, we find that blebbistatin inhibits three myosin II-dependent processes in Dictyostelium (growth in suspension culture, capping of Con A receptors, and development to fruiting bodies) and does not inhibit growth on plates, which does not require myosin II. As expected, macropinocytosis (myosin I-dependent), contractile vacuole activity (myosin V-dependent), and phagocytosis (myosin VII-dependent), none of which requires myosin II, are not inhibited by blebbistatin in myosin II-null cells, but, unexpectedly, blebbistatin does inhibit macropinocytosis and phagocytosis by cells expressing myosin II. Expression of catalytically inactive myosin II in myosin II-null cells also inhibits macropinocytosis and phagocytosis. Both blebbistatin-inhibited myosin II and catalytically inactive myosin II form cytoplasmic aggregates, which may be why they inhibit myosin II-independent processes, but neither affects the distribution of actin filaments in vegetative cells or actin and myosin distribution in dividing or polarized cells. Blebbistatin also inhibits cell streaming and plaque expansion in myosin II-null cells. Our results are consistent with myosin II being the only Dictyostelium myosin that is inhibited by blebbistatin but also show that blebbistatin-inactivated myosin II inhibits some myosin II-independent processes and that blebbistatin inhibits other activities in the absence of myosin II.
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