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We tested whether the mechanisms of chromosome movement during anaphase in locust (Locusta migratoria L.) spermatocytes might be similar to those described for crane-fly spermatocytes. Actin and myosin have been implicated in anaphase chromosome movements in crane-fly spermatocytes, as indicated by the effects of inhibitors and by the localisations of actin and myosin in spindles. In this study, we tested whether locust spermatocyte spindles also utilise actin and myosin, and whether actin is involved in microtubule flux. Living locust spermatocytes were treated with inhibitors of actin (latrunculin B and cytochalasin D), myosin (BDM), or myosin phosphorylation (Y-27632 and ML-7). We added drugs (individually) during anaphase. Actin inhibitors alter anaphase: chromosomes either completely stop moving, slow, or sometimes accelerate. The myosin inhibitor, BDM, also alters anaphase: in most cases, the chromosomes drastically slow or stop. ML-7, an inhibitor of MLCK, causes chromosomes to stop, slow, or sometimes accelerate, similar to actin inhibitors. Y-27632, an inhibitor of Rho-kinase, drastically slows or stops anaphase chromosome movements. The effects of the drugs on anaphase movement are reversible: most of the half-bivalents resumed movement at normal speed after these drugs were washed out. Actin and myosin were present in the spindles in locations consistent with their possible involvement in force production. Microtubule flux along kinetochore fibres is an actin-dependent process, since LatB completely removes or drastically reduces the gap in microtubule acetylation at the kinetochore. These results suggest that actin and myosin are involved in anaphase chromosome movements in locust spermatocytes.
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http://dx.doi.org/10.1007/s00709-007-0262-y | DOI Listing |
Biophys Rep (N Y)
September 2025
Cellular Signal Transduction in the Cardiovascular System COBRE, University of Nevada Reno, Reno, NV 89557; Department of Nutrition, University of Nevada Reno, Reno, NV 89557. Electronic address:
Skeletal muscle alpha actin (ACTA1) is important for muscle contraction and relaxation, with historical studies focused on ACTA1 mutations in muscle dysfunction. Proteomics reports have consistently observed that actin, including ACTA1, is acetylated at multiple lysine sites. However, few reports have studied the effects of actin acetylation on cellular function, and fewer have examined ACTA1 acetylation on skeletal muscle function.
View Article and Find Full Text PDFEur J Cell Biol
September 2025
The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710049, PR China; Bioinspired Engineering and Biomechanics Center (BEBC), Xi'an Jiaotong University, Xi'an 710049, PR China. Electronic address:
Cell migration toward stiffer or softer environments (durotaxis) underlies processes from development to cancer metastasis, yet the underlying mechanism and its universality remain unclear. To resolve this, we investigated how traction forces and directional persistence dictate cell migration along stiffness gradients. We utilized tunable PEG hydrogels with stiffness gradients of 1-16 kPa and perturbed contractility (blebbistatin, oligomycin), and adhesion (vinculin mutants), in cancer cells exhibiting opposing durotactic biases.
View Article and Find Full Text PDFUnlabelled: As human skeletal muscle cellular and molecular contractile properties are temperature-sensitive, the ability to perform experiments at body temperature (∼37°C) may lead to a better understanding of their responses and potentially their effects upon whole-muscle and whole-body performance. We quantified molecular (myosin-actin cross-bridge mechanics and kinetics) and cellular (specific tension; force divided by cross-sectional area) function in slow-contracting myosin heavy chain (MHC) I and fast-contracting MHC IIA fibers from older adults (n=13, 8 female) at 37°C and compared these to results at 25°C. MHC I fibers were more temperature-sensitive than MHC IIA fibers, showing greater increases in cross-bridge kinetics (MHC I: 4.
View Article and Find Full Text PDFT cell activation is characterized by rapid reorganization of the actin cytoskeleton and cell spreading on the antigen presenting cell. The T cell nucleus occupies a large fraction of the cell volume, and its mechanical properties are likely to act as a key determinant of activation. However, the contribution of nuclear mechanics to T cell spreading and activation is not well understood.
View Article and Find Full Text PDFbioRxiv
August 2025
Department of Bioengineering, Stanford University, Stanford, CA, USA.
Understanding the behaviors of contractile actomyosin systems requires precise spatiotemporal control of filamentous myosin activity. Here, we develop a tool for optical control of contractility by extending the MyLOV family of gearshifting motors to create engineered filamentous myosins that change velocity in response to blue light. We characterize these minifilaments using single-molecule tracking assays, contractility assays in reconstituted actin networks, and imaging of contractile phenotypes in S2 cells.
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