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Journal articles on the topic 'Myosine-X'

Author: Grafiati

Published: 25 May 2024

Last updated: 31 July 2025

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1

Berg, J. S., B. H. Derfler, C. M. Pennisi, D. P. Corey, and R. E. Cheney. "Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin." Journal of Cell Science 113, no. 19 (2000): 3439–51. http://dx.doi.org/10.1242/jcs.113.19.3439.

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Myosin-X is the founding member of a novel class of unconventional myosins characterized by a tail domain containing multiple pleckstrin homology domains. We report here the full-length cDNA sequences of human and bovine myosin-X as well as the first characterization of this protein's distribution and biochemical properties. The 235 kDa myosin-X contains a head domain with &lt;45% protein sequence identity to other myosins, three IQ motifs, and a predicted stalk of coiled coil. Like several other unconventional myosins and a plant kinesin, myosin-X contains both a myosin tail homology 4 (M

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2

Novakovic, Valerie A., and Gary E. Gilbert. "Procoagulant activities of skeletal and cardiac muscle myosin depend on contaminating phospholipid." Blood 136, no. 21 (2020): 2469–72. http://dx.doi.org/10.1182/blood.2020005930.

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Abstract Recent reports indicate that suspended skeletal and cardiac myosin, such as might be released during injury, can act as procoagulants by providing membrane-like support for factors Xa and Va in the prothrombinase complex. Further, skeletal myosin provides membrane-like support for activated protein C. This raises the question of whether purified muscle myosins retain procoagulant phospholipid through purification. We found that lactadherin, a phosphatidyl-l-serine–binding protein, blocked &gt;99% of prothrombinase activity supported by rabbit skeletal and by bovine cardiac myosin.

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3

Rogers, Michael S., and Emanuel E. Strehler. "The Tumor-sensitive Calmodulin-like Protein Is a Specific Light Chain of Human Unconventional Myosin X." Journal of Biological Chemistry 276, no. 15 (2001): 12182–89. http://dx.doi.org/10.1074/jbc.m010056200.

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Human calmodulin-like protein (CLP) is an epithelial-specific Ca2+-binding protein whose expression is strongly down-regulated in cancers. Like calmodulin, CLP is thought to regulate cellular processes via Ca2+-dependent interactions with specific target proteins. Using gel overlays, we identified a ∼210-kDa protein binding specifically and in a Ca2+-dependent manner to CLP, but not to calmodulin. Yeast two-hybrid screening yielded a CLP-interacting clone encoding the three light chain binding IQ motifs of human “unconventional” myosin X. Pull-down experiments showed CLP binding to the IQ doma

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4

Naydenov, Nayden, Susana Lechuga, Emina Huang, and Andrei Ivanov. "Myosin Motors: Novel Regulators and Therapeutic Targets in Colorectal Cancer." Cancers 13, no. 4 (2021): 741. http://dx.doi.org/10.3390/cancers13040741.

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Colorectal cancer (CRC) remains the third most common cause of cancer and the second most common cause of cancer deaths worldwide. Clinicians are largely faced with advanced and metastatic disease for which few interventions are available. One poorly understood aspect of CRC involves altered organization of the actin cytoskeleton, especially at the metastatic stage of the disease. Myosin motors are crucial regulators of actin cytoskeletal architecture and remodeling. They act as mechanosensors of the tumor environments and control key cellular processes linked to oncogenesis, including cell di

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5

Brown, Lisa D., and Marie E. Cantino. "Immunocytochemical Localization of Myosin Light Chains in the Abdominal Superficial Flexor Muscles of the American Lobster, Homarus Americanus." Microscopy and Microanalysis 4, S2 (1998): 1118–19. http://dx.doi.org/10.1017/s143192760002571x.

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Myosin is composed of two high-molecular weight heavy chains and four low-molecular weight hght chains. In both vertebrate and invertebrate skeletal muscle, each myosin heavy chain is associated with two myosin light chains. In skeletal muscle myosins studied by X-ray diffraction, each myosin heavy chain binds one of each of two distinct classes of hght chains. Thus, while isoform distributions may vary within and between fibers, the spatial distribution of each class of light chain should be uniform within the A band and between sarcomeres and fibers. Since no such study exists for crustacean

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6

Squire, John. "Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview." International Journal of Molecular Sciences 20, no. 22 (2019): 5715. http://dx.doi.org/10.3390/ijms20225715.

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Muscular contraction is a fundamental phenomenon in all animals; without it life as we know it would be impossible. The basic mechanism in muscle, including heart muscle, involves the interaction of the protein filaments myosin and actin. Motility in all cells is also partly based on similar interactions of actin filaments with non-muscle myosins. Early studies of muscle contraction have informed later studies of these cellular actin-myosin systems. In muscles, projections on the myosin filaments, the so-called myosin heads or cross-bridges, interact with the nearby actin filaments and, in a m

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7

Dillmann, W. H. "Methyl palmoxirate increases Ca2+-myosin ATPase activity and changes myosin isoenzyme distribution in the diabetic rat heart." American Journal of Physiology-Endocrinology and Metabolism 248, no. 5 (1985): E602—E606. http://dx.doi.org/10.1152/ajpendo.1985.248.5.e602.

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Previous studies have shown that in rats diabetes mellitus leads to a decrease in cardiac ventricle myosin V1 and an increase in myosin V3 levels. Insulin administration reverts myosin isoenzyme distribution to normal levels. It is currently unclear whether the effects of insulin on myosin isoenzyme distribution are a direct effect of the hormone or are mediated through insulin-induced alterations in cardiac metabolism. To gain further insight into this question diabetic rats received methyl palmoxirate, a potent inhibitor of long-chain fatty acid oxidation. Administration of 25 mg methyl palm

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8

Courson, David S., and Richard E. Cheney. "Myosin-X and disease." Experimental Cell Research 334, no. 1 (2015): 10–15. http://dx.doi.org/10.1016/j.yexcr.2015.03.014.

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9

Almagro, Sébastien, Claire Durmort, Adeline Chervin-Pétinot, et al. "The Motor Protein Myosin-X Transports VE-Cadherin along Filopodia To Allow the Formation of Early Endothelial Cell-Cell Contacts." Molecular and Cellular Biology 30, no. 7 (2010): 1703–17. http://dx.doi.org/10.1128/mcb.01226-09.

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ABSTRACT Vascular endothelium (VE), the monolayer of endothelial cells that lines the vascular tree, undergoes damage at the basis of some vascular diseases. Its integrity is maintained by VE-cadherin, an adhesive receptor localized at cell-cell junctions. Here, we show that VE-cadherin is also located at the tip and along filopodia in sparse or subconfluent endothelial cells. We observed that VE-cadherin navigates along intrafilopodial actin filaments. We found that the actin motor protein myosin-X is colocalized and moves synchronously with filopodial VE-cadherin. Immunoprecipitation and pul

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10

Ikebe, Mitsuo, Osamu Sato, and Tsuyoshi Sakai. "Myosin X and Cytoskeletal Reorganization." Applied Microscopy 48, no. 2 (2018): 33–42. http://dx.doi.org/10.9729/am.2018.48.2.33.

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11

Iwano, Sayaka, Ayaka Satou, Shigeru Matsumura, Naoyuki Sugiyama, Yasushi Ishihama, and Fumiko Toyoshima. "PCTK1 Regulates Integrin-Dependent Spindle Orientation via Protein Kinase A Regulatory Subunit KAP0 and Myosin X." Molecular and Cellular Biology 35, no. 7 (2015): 1197–208. http://dx.doi.org/10.1128/mcb.01017-14.

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Integrin-dependent cell-extracellular matrix (ECM) adhesion is a determinant of spindle orientation. However, the signaling pathways that couple integrins to spindle orientation remain elusive. Here, we show that PCTAIRE-1 kinase (PCTK1), a member of the cyclin-dependent kinases (CDKs) whose function is poorly characterized, plays an essential role in this process. PCTK1 regulates spindle orientation in a kinase-dependent manner. Phosphoproteomic analysis together with an RNA interference screen revealed that PCTK1 regulates spindle orientation through phosphorylation of Ser83 on KAP0, a regul

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12

Vuillez, J. P., M. D. Brunet, E. Borrel, et al. "Place du dosage immunoradiométrique de la chaîne lourde de la myosine en chirurgie coronarienne." Immuno-analyse & Biologie Spécialisée 11, no. 1 (1996): 38–42. http://dx.doi.org/10.1016/0923-2532(96)88389-x.

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13

Berg, Jonathan S., and Richard E. Cheney. "Myosin-X is an unconventional myosin that undergoes intrafilopodial motility." Nature Cell Biology 4, no. 3 (2002): 246–50. http://dx.doi.org/10.1038/ncb762.

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14

Knupp, Morris, and Squire. "The Interacting Head Motif Structure Does Not Explain the X-Ray Diffraction Patterns in Relaxed Vertebrate (Bony Fish) Skeletal Muscle and Insect (Lethocerus) Flight Muscle." Biology 8, no. 3 (2019): 67. http://dx.doi.org/10.3390/biology8030067.

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Unlike electron microscopy, which can achieve very high resolution but to date can only be used to study static structures, time-resolved X-ray diffraction from contracting muscles can, in principle, be used to follow the molecular movements involved in force generation on a millisecond timescale, albeit at moderate resolution. However, previous X-ray diffraction studies of resting muscles have come up with structures for the head arrangements in resting myosin filaments that are different from the apparently ubiquitous interacting head motif (IHM) structures found by single particle analysis

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15

Holmes, K. C., D. R. Trentham, R. Simmons, et al. "X-ray diffraction studies of the contractile mechanism in single muscle fibres." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 359, no. 1452 (2004): 1883–93. http://dx.doi.org/10.1098/rstb.2004.1557.

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The molecular mechanism of muscle contraction was investigated in intact muscle fibres by X–ray diffraction. Changes in the intensities of the axial X–ray reflections produced by imposing rapid changes in fibre length establish the average conformation of the myosin heads during active isometric contraction, and show that the heads tilt during the elastic response to a change in fibre length and during the elementary force generating process: the working stroke. X–ray interference between the two arrays of myosin heads in each filament allows the axial motions of the heads following a sudden d

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16

Cheney, Richard E. "Dynamics of Myosin-X in Filopodia." Biophysical Journal 100, no. 3 (2011): 2a. http://dx.doi.org/10.1016/j.bpj.2010.11.064.

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17

Prosser, Haydn M., Agnieszka K. Rzadzinska, Karen P. Steel, and Allan Bradley. "Mosaic Complementation Demonstrates a Regulatory Role for Myosin VIIa in Actin Dynamics of Stereocilia." Molecular and Cellular Biology 28, no. 5 (2007): 1702–12. http://dx.doi.org/10.1128/mcb.01282-07.

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ABSTRACT We have developed a bacterial artificial chromosome transgenesis approach that allowed the expression of myosin VIIa from the mouse X chromosome. We demonstrated the complementation of the Myo7a null mutant phenotype producing a fine mosaic of two types of sensory hair cells within inner ear epithelia of hemizygous transgenic females due to X inactivation. Direct comparisons between neighboring auditory hair cells that were different only with respect to myosin VIIa expression revealed that mutant stereocilia are significantly longer than those of their complemented counterparts. Myos

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18

Kerber, M. L., and R. E. Cheney. "Myosin-X: a MyTH-FERM myosin at the tips of filopodia." Journal of Cell Science 124, no. 22 (2011): 3733–41. http://dx.doi.org/10.1242/jcs.023549.

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19

Hayden, S. M., J. S. Wolenski, and M. S. Mooseker. "Binding of brush border myosin I to phospholipid vesicles." Journal of Cell Biology 111, no. 2 (1990): 443–51. http://dx.doi.org/10.1083/jcb.111.2.443.

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The actin filament core within each microvillus of the intestinal epithelial cell is attached laterally to the plasma membrane by brush border (BB) myosin I, a protein-calmodulin complex belonging to the myosin I class of actin-based mechanoenzymes. In this report, the binding of BB myosin I to pure phospholipid vesicles was examined and characterized. BB myosin I demonstrated saturable binding to liposomes composed of anionic phospholipids, but did not associate with liposomes composed of only neutral phospholipids. The binding of BB myosin I to phosphatidylserine and phosphatidylglycerol ves

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20

de Lanerolle, P. "cAMP, myosin dephosphorylation, and isometric relaxation of airway smooth muscle." Journal of Applied Physiology 64, no. 2 (1988): 705–9. http://dx.doi.org/10.1152/jappl.1988.64.2.705.

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The temporal relationships among increases in adenosine 3',5'-cyclic monophosphate (cAMP) levels, myosin dephosphorylation, and relaxation were investigated to clarify the mechanisms of airway muscle relaxation. Canine tracheal muscles isometrically contracted (82% of maximum force) with 10(-6) M methacholine were relaxed by adding either 4 x 10(-7) M atropine or 4 x 10(-5) M forskolin. Atropine had no effect on cAMP levels; myosin phosphorylation and force, however, decayed at the same rates and these two parameters returned to their basal pre-methacholine levels within 5 min. Forskolin treat

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21

Zepeda-Bastida, Armando, Natalia Chiquete-Felix, Juan Ocampo-López, Salvador Uribe-Carvajal, and Adela Mújica. "Possible participation of calmodulin in the decondensation of nuclei isolated from guinea pig spermatozoa." Zygote 18, no. 3 (2009): 217–29. http://dx.doi.org/10.1017/s0967199409990220.

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SummaryThe guinea pig spermatozoid nucleus contains actin, myosin, spectrin and cytokeratin. Also, it has been reported that phalloidin and/or 2,3-butanedione monoxime retard the sperm nuclear decondensation caused by heparin, suggesting a role for F-actin and myosin in nuclear stability. The presence of an F-actin/myosin dynamic system in these nuclei led us to search for proteins usually related to this system. In guinea pig sperm nuclei we detected calmodulin, F-actin, the myosin light chain and an actin-myosin complex. To define whether calmodulin participates in nuclear-dynamics, the effe

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22

Malhotra, A., P. Buttrick, and J. Scheuer. "Effects of sex hormones on development of physiological and pathological cardiac hypertrophy in male and female rats." American Journal of Physiology-Heart and Circulatory Physiology 259, no. 3 (1990): H866—H871. http://dx.doi.org/10.1152/ajpheart.1990.259.3.h866.

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Previous studies have demonstrated a role for sex hormones in maintaining normal heart weight and myosin isoenzyme balance in the rat. To determine if sex hormones were necessary to elicit cardiac adaptations to the chronic loads of swimming or hypertension, female rats were gonadectomized (X) and then exposed either to a chronic swimming program (Sw) or to renal hypertension for 8-10 wk. Because gonadectomy in females increased heart and body weight, separate groups of food-restricted sedentary and Sw gonadectomized females (XFR) were included. Swimming resulted in significant increases in bo

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23

Skubiszak, Ludmila, and Leszek Kowalczyk. "The vertebrate skeletal muscle thick filaments are not three-stranded. Reinterpretation of some experimental data." Acta Biochimica Polonica 49, no. 4 (2002): 841–53. http://dx.doi.org/10.18388/abp.2002_3744.

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Computer simulation of mass distribution within the model and Fourier transforms of images depicting mass distribution are explored for verification of two alternative modes of the myosin molecule arrangement within the vertebrate skeletal muscle thick filaments. The model well depicting the complete bipolar structure of the thick filament and revealing a true threefold-rotational symmetry is a tube covered by two helices with a pitch of 2 x 43 nm due to arrangement of the myosin tails along a helical path and grouping of all myosin heads in the crowns rotated by 240 degrees and each containin

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24

Sugi, Haruo, Maki Yamaguchi, Tetsuo Ohno, Hiroshi Okuyama, and Naoto Yagi. "X-ray Diffraction Studies on the Structural Origin of Dynamic Tension Recovery Following Ramp-Shaped Releases in High-Ca Rigor Muscle Fibers." International Journal of Molecular Sciences 21, no. 4 (2020): 1244. http://dx.doi.org/10.3390/ijms21041244.

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It is generally believed that during muscle contraction, myosin heads (M) extending from myosin filament attaches to actin filaments (A) to perform power stroke, associated with the reaction, A-M-ADP-Pi → A-M + ADP + Pi, so that myosin heads pass through the state of A-M, i.e., rigor A-M complex. We have, however, recently found that: (1) an antibody to myosin head, completely covering actin-binding sites in myosin head, has no effect on Ca2+-activated tension in skinned muscle fibers; (2) skinned fibers exhibit distinct tension recovery following ramp-shaped releases (amplitude, 0.5% of Lo; c

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25

Liu, Katy C., Damon T. Jacobs, Brian D. Dunn, Alan S. Fanning, and Richard E. Cheney. "Myosin-X functions in polarized epithelial cells." Molecular Biology of the Cell 23, no. 9 (2012): 1675–87. http://dx.doi.org/10.1091/mbc.e11-04-0358.

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Myosin-X (Myo10) is an unconventional myosin that localizes to the tips of filopodia and has critical functions in filopodia. Although Myo10 has been studied primarily in nonpolarized, fibroblast-like cells, Myo10 is expressed in vivo in many epithelia-rich tissues, such as kidney. In this study, we investigate the localization and functions of Myo10 in polarized epithelial cells, using Madin-Darby canine kidney II cells as a model system. Calcium-switch experiments demonstrate that, during junction assembly, green fluorescent protein–Myo10 localizes to lateral membrane cell–cell contacts and

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26

Homma, Kazuaki, Junya Saito, Reiko Ikebe, and Mitsuo Ikebe. "Motor Function and Regulation of Myosin X." Journal of Biological Chemistry 276, no. 36 (2001): 34348–54. http://dx.doi.org/10.1074/jbc.m104785200.

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27

Ma, Weikang, Henry Gong, and Thomas Irving. "Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle." International Journal of Molecular Sciences 19, no. 9 (2018): 2643. http://dx.doi.org/10.3390/ijms19092643.

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Transgenic mouse models have been important tools for studying the relationship of genotype to phenotype for human diseases, including those of skeletal muscle. We show that mouse skeletal muscle can produce high quality X-ray diffraction patterns establishing the mouse intact skeletal muscle X-ray preparation as a potentially powerful tool to test structural hypotheses in health and disease. A notable feature of the mouse model system is the presence of residual myosin layer line intensities in contracting mouse muscle patterns. This provides an additional tool, along with the I1,1/I1,0 inten

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28

Milligan, R. A. "Structure and Action of Molecular Tracks and Motors." Microscopy and Microanalysis 4, S2 (1998): 456–57. http://dx.doi.org/10.1017/s1431927600022406.

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Molecular motors belonging to the myosin and kinesin superfamilies utilize ATP to move along their respective F-actin and microtubule tracks. The track-motor complexes have not been amenable to crystallization, so x-ray crystallographic investigations have focused on structure determinations of the individual proteins. Although providing detailed descriptions of the structure of each protein, this approach cannot reveal the geometry of interaction of the proteins nor the conformational changes which occur during the mechanochemical cycle. To obtain this information, we use cryoelectron microsc

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29

Chatterjee, M., and M. Tejada. "Phorbol ester-induced contraction in chemically skinned vascular smooth muscle." American Journal of Physiology-Cell Physiology 251, no. 3 (1986): C356—C361. http://dx.doi.org/10.1152/ajpcell.1986.251.3.c356.

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We studied the contractile response to phorbol esters and its relationship to myosin light chain phosphorylation in intact and Triton X-100-skinned porcine carotid preparations. Muscle contraction was activated by phorbol 12,13-dibutyrate (PDBu) and phorbol 12,13-didecanoate (PDD). Dose-dependent contractions to PDBu were obtained both in the intact and skinned preparations. The maximal values of stress in response to PDBu were 1.11 +/- 0.10 X 10(5) N/m2 (n = 7) in the intact and 5.72 +/- 0.59 X 10(4) N/m2 (n = 10) in the skinned muscles. The skinned tissues responded to PDD, which has been sh

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30

Whittaker, M., and R. Milligan. "Thin filament structure and activation." Proceedings, annual meeting, Electron Microscopy Society of America 47 (August 6, 1989): 976–77. http://dx.doi.org/10.1017/s0424820100156869.

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Skeletal muscle contraction is triggered by the release of calcium ions from the sarcoplasmic reticulum of the myofibrils. Troponin and tropomyosin in the thin (actin-containing) filaments act together as the transducer of this signal. Evidence from reconstruction of electron images of negatively stained samples and from x-ray diffraction studies of intact myofibrils (e.g. 2) have led to the steric blocking model of regulation by the tropomyosin troponin complex. In this model, tropomyosin is believed to occupy a defined location on the myosin binding site in the absence of calcium. When calci

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31

Eakins, Felicity, Jeffrey J. Harford, Carlo Knupp, Manfred Roessle, and John M. Squire. "Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths." International Journal of Molecular Sciences 19, no. 7 (2018): 2091. http://dx.doi.org/10.3390/ijms19072091.

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At a resting sarcomere length of approximately 2.2 µm bony fish muscles put into rigor in the presence of BDM (2,3-butanedione monoxime) to reduce rigor tension generation show the normal arrangement of myosin head interactions with actin filaments as monitored by low-angle X-ray diffraction. However, if the muscles are put into rigor using the same protocol but stretched to 2.5 µm sarcomere length, a markedly different structure is observed. The X-ray diffraction pattern is not just a weaker version of the pattern at full overlap, as might be expected, but it is quite different. It is compati

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32

Flood, Veronica H., Tricia L. Slobodianuk, Daniel Keesler, et al. "von Willebrand factor binding to myosin assists in coagulation." Blood Advances 4, no. 1 (2020): 174–80. http://dx.doi.org/10.1182/bloodadvances.2019000533.

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Abstract von Willebrand factor (VWF) binds to platelets and collagen as a means of facilitating coagulation at sites of injury. Recent evidence has shown that myosin can serve as a surface for thrombin generation and binds to activated factor V and factor X. We studied whether VWF can also bind myosin as a means of bringing factor VIII (FVIII) to sites of clot formation. A myosin-binding assay was developed using skeletal muscle myosin to measure VWF binding, and plasma-derived and recombinant VWF containing molecular disruptions at key VWF sites were tested. Competition assays were performed

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33

Homma, Kazuaki, and Mitsuo Ikebe. "Myosin X Is a High Duty Ratio Motor." Journal of Biological Chemistry 280, no. 32 (2005): 29381–91. http://dx.doi.org/10.1074/jbc.m504779200.

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34

Lu, Q., F. Ye, Z. Wei, Z. Wen, and M. Zhang. "Antiparallel coiled-coil-mediated dimerization of myosin X." Proceedings of the National Academy of Sciences 109, no. 43 (2012): 17388–93. http://dx.doi.org/10.1073/pnas.1208642109.

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35

FARUQI, A. R., R. A. CROSS, and J. KENDRICK-JONES. "Small angle X-ray scattering studies on myosin." Journal of Cell Science 1991, Supplement 14 (1991): 23–26. http://dx.doi.org/10.1242/jcs.1991.supplement_14.5.

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36

Watanabe, Tomonobu M., Hiroshi Tokuo, Kohsuke Gonda, Hideo Higuchi, and Mitsuo Ikebe. "The Dynamics for Myosin-X Induced Filopodia Protrusion." Biophysical Journal 98, no. 3 (2010): 725a—726a. http://dx.doi.org/10.1016/j.bpj.2009.12.3976.

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37

Sato, Osamu, Satoshi Komatsu, Tomonobu M. Watanabe, Kazuaki Homma, and Mitsuo Ikebe. "Single Molecule Movement of Full-Length Myosin X." Biophysical Journal 102, no. 3 (2012): 570a. http://dx.doi.org/10.1016/j.bpj.2011.11.3103.

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38

Watanabe, Tomonobu M., Hiroshi Tokuo, Kohsuke Gonda, Hideo Higuchi, and Mitsuo Ikebe. "Myosin-X Induces Filopodia by Multiple Elongation Mechanism." Journal of Biological Chemistry 285, no. 25 (2010): 19605–14. http://dx.doi.org/10.1074/jbc.m109.093864.

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39

Verkhovsky, A. B., and G. G. Borisy. "Non-sarcomeric mode of myosin II organization in the fibroblast lamellum." Journal of Cell Biology 123, no. 3 (1993): 637–52. http://dx.doi.org/10.1083/jcb.123.3.637.

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The organization of myosin in the fibroblast lamellum was studied by correlative fluorescence and electron microscopy after a novel procedure to reveal its underlying morphology. An X-rhodamine analog of conventional smooth muscle myosin (myosin II) that colocalized after microinjection with endogenous myosin was used to trace myosin distribution in living fibroblasts. Then, the same cells were examined by EM of platinum replicas. To visualize the structural arrangement of myosin, other cytoskeletal fibrillar structures had to be removed: microtubules were depolymerized by nocodazole treatment

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40

Chang, Audrey N., Ning Gao, Zhenan Liu та ін. "The dominant protein phosphatase PP1c isoform in smooth muscle cells, PP1cβ, is essential for smooth muscle contraction". Journal of Biological Chemistry 293, № 43 (2018): 16677–86. http://dx.doi.org/10.1074/jbc.ra118.003083.

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Contractile force development of smooth muscle is controlled by balanced kinase and phosphatase activities toward the myosin regulatory light chain (RLC). Numerous biochemical and pharmacological studies have investigated the specificity and regulatory activity of smooth muscle myosin light-chain phosphatase (MLCP) bound to myosin filaments and comprised of the regulatory myosin phosphatase target subunit 1 (MYPT1) and catalytic protein phosphatase 1cβ (PP1cβ) subunits. Recent physiological and biochemical evidence obtained with smooth muscle tissues from a conditional MYPT1 knockout suggests

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41

Knupp and Squire. "Myosin Cross-Bridge Behaviour in Contracting Muscle—The T1 Curve of Huxley and Simmons (1971) Revisited." International Journal of Molecular Sciences 20, no. 19 (2019): 4892. http://dx.doi.org/10.3390/ijms20194892.

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The stiffness of the myosin cross-bridges is a key factor in analysing possible scenarios to explain myosin head changes during force generation in active muscles. The seminal study of Huxley and Simmons (1971: Nature 233: 533) suggested that most of the observed half-sarcomere instantaneous compliance (=1/stiffness) resides in the myosin heads. They showed with a so-called T1 plot that, after a very fast release, the half-sarcomere tension reduced to zero after a step size of about 60Å (later with improved experiments reduced to 40Å). However, later X-ray diffraction studies showed that myosi

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42

Ma, Weikang, Marcus Henze, Robert L. Anderson, et al. "The Super-Relaxed State and Length Dependent Activation in Porcine Myocardium." Circulation Research 129, no. 6 (2021): 617–30. http://dx.doi.org/10.1161/circresaha.120.318647.

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Rationale: Myofilament length-dependent activation (LDA) is the key underlying mechanism of cardiac heterometric autoregulation, commonly referred as the Frank-Starling Law of the heart. Although alterations in LDA are common in cardiomyopathic states, the precise structural and biochemical mechanisms underlying LDA remain unknown. Objective: Here, we examine the role of structural changes in the thick filament during diastole, in particular changes in the availability of myosin heads, in determining both calcium sensitivity and maximum contractile force during systole in permeabilized porcine

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Perz-Edwards, Robert J., Thomas C. Irving, Bruce A. J. Baumann, et al. "X-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle." Proceedings of the National Academy of Sciences 108, no. 1 (2010): 120–25. http://dx.doi.org/10.1073/pnas.1014599107.

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Stretch activation is important in the mechanical properties of vertebrate cardiac muscle and essential to the flight muscles of most insects. Despite decades of investigation, the underlying molecular mechanism of stretch activation is unknown. We investigated the role of recently observed connections between myosin and troponin, called “troponin bridges,” by analyzing real-time X-ray diffraction “movies” from sinusoidally stretch-activated Lethocerus muscles. Observed changes in X-ray reflections arising from myosin heads, actin filaments, troponin, and tropomyosin were consistent with the h

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Niciforovic, Ana, Marija Radojcic, and Bratoljub Milosavljevic. "Gamma-radiation induced agglomeration of chicken muscle myosin and actine." Journal of the Serbian Chemical Society 69, no. 12 (2004): 999–1004. http://dx.doi.org/10.2298/jsc0412999n.

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Radiolytic behaviour of themajor vertebrate muscle proteins: fibrillarmyosin (molar mass, Mm = 520,000 g/mol) and filament forming actin (Mm = 42,050 g/mol) was studied using a SDS-polyacrylamide gel electrophoresis and quantified by high precision laser-densitometry. In order to study the OH radical contribution to the radiation damage, purified chicken myosin and actin (4 ?M) were prepared in N2O saturated solution and irradiated with 1?3 kGy at 60Co gamma source. With respect to changes in the molecular mass, the only observed myosin and actin damage was dose dependent agglomeration of prot

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Baker, T. S., and D. A. Winkelmann. "Methodology for determining the three-dimensional crystal structure of myosin Sl from electron microscopy of orthogonal thin sections." Proceedings, annual meeting, Electron Microscopy Society of America 44 (August 1986): 26–29. http://dx.doi.org/10.1017/s0424820100141895.

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Detailed knowledge of the structure of myosin is essential for understanding the mechanism of muscle contraction. The discovery of conditions for crystallizing the head of myosin (Sl = subfragment 1) has led to systematic studies of the SI structure by x-ray crystallography and electron microscopy. We describe the method used to determine the structure of the myosin Sl molecule by electron microscopy (Fig. 3). This method involved independently reconstructing the three-dimensional density of several thin sections obtained from oriented crystals and then combining these reconstructions to produ

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Winkelmann, Donald A. "Structure of Myosin Subfragment-1 from Electron Microscopy and Crystallography." Proceedings, annual meeting, Electron Microscopy Society of America 46 (1988): 156–57. http://dx.doi.org/10.1017/s0424820100102869.

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The primary role of the interaction of actin and myosin is the generation of force and motion as a direct consequence of the cyclic interaction of myosin crossbridges with actin filaments. Myosin is composed of six polypeptides: two heavy chains of molecular weight 220,000 daltons and two pairs of light chains of molecular weight 17,000-23,000. The C-terminal portions of the myosin heavy chains associate to form an α-helical coiled-coil rod which is responsible for myosin filament formation. The N-terminal portion of each heavy chain associates with two different light chains to form a globula

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Taylor, Kenneth A., Hamidreza Rahmani, Robert J. Edwards, and Michael K. Reedy. "Insights into Actin-Myosin Interactions within Muscle from 3D Electron Microscopy." International Journal of Molecular Sciences 20, no. 7 (2019): 1703. http://dx.doi.org/10.3390/ijms20071703.

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Much has been learned about the interaction between myosin and actin through biochemistry, in vitro motility assays and cryo-electron microscopy (cryoEM) of F-actin, decorated with myosin heads. Comparatively less is known about actin-myosin interactions within the filament lattice of muscle, where myosin heads function as independent force generators and thus most measurements report an average signal from multiple biochemical and mechanical states. All of the 3D imaging by electron microscopy (EM) that has revealed the interplay of the regular array of actin subunits and myosin heads within

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Evans, L. L., A. J. Lee, P. C. Bridgman, and M. S. Mooseker. "Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport." Journal of Cell Science 111, no. 14 (1998): 2055–66. http://dx.doi.org/10.1242/jcs.111.14.2055.

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Myosin-V has been linked to actin-based organelle transport by a variety of genetic, biochemical and localization studies. However, it has yet to be determined whether myosin-V functions as an organelle motor. To further investigate this possibility, we conducted a biochemical and functional analysis of organelle-associated brain myosin-V. Using the initial fractionation steps of an established protocol for the purification of brain myosin-V, we isolated a population of brain microsomes that is approx. fivefold enriched for myosin-V, and is similarly enriched for synaptic vesicle proteins. As

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Melo, Hugo Christiano Soares, and Milton Vieira Coelho. "A new method to precipitate myosin V from rat brain soluble fraction." Acta Biochimica Polonica 54, no. 3 (2007): 575–81. http://dx.doi.org/10.18388/abp.2007_3231.

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Myosin can be precipitated from soluble fraction under different assay conditions. This paper describes a new method for precipitating myosin V from rat brain soluble fraction. Brains were homogenized in 50 mM imidazole/HCl buffer, pH 8.0, containing 10 mM EDTA/EGTA, 250 mM sucrose, 1 mM DTT and 1 mM benzamidine, centrifuged at 45000 x g for 40 min and the supernatant was frozen at -20 degrees C. Forty-eight hours later, the supernatant was thawed, centrifuged at 45000 x g for 40 min and the precipitate was washed in 20 mM imidazole buffer pH 8.0. SDS/PAGE analysis showed four polypeptides in

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Wagner, M. C., and B. A. Molitoris. "ATP depletion alters myosin I beta cellular location in LLC-PK1 cells." American Journal of Physiology-Cell Physiology 272, no. 5 (1997): C1680—C1690. http://dx.doi.org/10.1152/ajpcell.1997.272.5.c1680.

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The brush border (BB) of the proximal tubule cell (PTC) requires dynamic membrane events for function. The actin cytoskeleton is necessary for structure and function in this region. ATP depletion disrupts both structure and function. In this report, myosin 1 beta location in LLC-PK1 cells was followed during ATP depletion and repletion using immunofluorescence and Western blot techniques. Myosin I beta colocalized with F-actin in the microvilli and cell periphery, but no colocalization was observed with stress fibers. ATP depletion increased the apical F-actin, and myosin I beta was colocalize

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