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Journal articles on the topic 'Actin Based Motor Proteins'

Author: Grafiati

Published: 7 September 2023

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1

Ciocanel, Maria-Veronica, Aravind Chandrasekaran, Carli Mager, Qin Ni, Garegin A. Papoian, and Adriana Dawes. "Simulated actin reorganization mediated by motor proteins." PLOS Computational Biology 18, no. 4 (2022): e1010026. http://dx.doi.org/10.1371/journal.pcbi.1010026.

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Cortical actin networks are highly dynamic and play critical roles in shaping the mechanical properties of cells. The actin cytoskeleton undergoes significant reorganization in many different contexts, including during directed cell migration and over the course of the cell cycle, when cortical actin can transition between different configurations such as open patched meshworks, homogeneous distributions, and aligned bundles. Several types of myosin motor proteins, characterized by different kinetic parameters, have been involved in this reorganization of actin filaments. Given the limitations

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2

Brown, Susan S. "Cooperation Between Microtubule- and Actin-Based Motor Proteins." Annual Review of Cell and Developmental Biology 15, no. 1 (1999): 63–80. http://dx.doi.org/10.1146/annurev.cellbio.15.1.63.

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3

Wolgemuth, Charles W., and Sean X. Sun. "Active random forces can drive differential cellular positioning and enhance motor-driven transport." Molecular Biology of the Cell 31, no. 20 (2020): 2283–88. http://dx.doi.org/10.1091/mbc.e19-11-0629.

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Chabrillat, Marion L., Claire Wilhelm, Christina Wasmeier, Elena V. Sviderskaya, Daniel Louvard, and Evelyne Coudrier. "Rab8 Regulates the Actin-based Movement of Melanosomes." Molecular Biology of the Cell 16, no. 4 (2005): 1640–50. http://dx.doi.org/10.1091/mbc.e04-09-0770.

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Rab GTPases have been implicated in the regulation of specific microtubule- and actin-based motor proteins. We devised an in vitro motility assay reconstituting the movement of melanosomes on actin bundles in the presence of ATP to investigate the role of Rab proteins in the actin-dependent movement of melanosomes. Using this assay, we confirmed that Rab27 is required for the actin-dependent movement of melanosomes, and we showed that a second Rab protein, Rab8, also regulates this movement. Rab8 was partially associated with mature melanosomes. Expression of Rab8Q67L perturbed the cellular di

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Titus, M. A., H. M. Warrick, and J. A. Spudich. "Multiple actin-based motor genes in Dictyostelium." Cell Regulation 1, no. 1 (1989): 55–63. http://dx.doi.org/10.1091/mbc.1.1.55.

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Dictyostelium cells, devoid of conventional myosin, display a variety of motile activities, consistent with the presence of other molecular motors. The Dictyostelium genome was probed at low stringency with a gene fragment containing the conserved conventional myosin head domain sequences to identify other actin-based motors that may play a role in the observed motility of these mutant cells. One gene (abmA) has been characterized and encodes a polypeptide of approximately 135 kDa with a head region homologous to other myosin head sequences and a tail region that is not predicted to form eithe

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Koonce, Michael P. "13 Plus 1: A 30-Year Perspective on Microtubule-Based Motility in Dictyostelium." Cells 9, no. 3 (2020): 528. http://dx.doi.org/10.3390/cells9030528.

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Individual gene analyses of microtubule-based motor proteins in Dictyostelium discoideum have provided a rough draft of its machinery for cytoplasmic organization and division. This review collates their activities and looks forward to what is next. A comprehensive approach that considers the collective actions of motors, how they balance rates and directions, and how they integrate with the actin cytoskeleton will be necessary for a complete understanding of cellular dynamics.

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Kumpula, Esa-Pekka, and Inari Kursula. "Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?" Acta Crystallographica Section F Structural Biology Communications 71, no. 5 (2015): 500–513. http://dx.doi.org/10.1107/s2053230x1500391x.

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Apicomplexan parasites are the causative agents of notorious human and animal diseases that give rise to considerable human suffering and economic losses worldwide. The most prominent parasites of this phylum are the malaria-causingPlasmodiumspecies, which are widespread in tropical and subtropical regions, andToxoplasma gondii, which infects one third of the world's population. These parasites share a common form of gliding motility which relies on an actin–myosin motor. The components of this motor and the actin-regulatory proteins in Apicomplexa have unique features compared with all other

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Müller, Kei W., Anna M. Birzle, and Wolfgang A. Wall. "Beam finite-element model of a molecular motor for the simulation of active fibre networks." Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences 472, no. 2185 (2016): 20150555. http://dx.doi.org/10.1098/rspa.2015.0555.

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Molecular motors are proteins that excessively increase the efficiency of subcellular transport processes. They allow for cell division, nutrient transport and even macroscopic muscle movement. In order to understand the effect of motors in large biopolymer networks, e.g. the cytoskeleton, we require a suitable model of a molecular motor. In this contribution, we present such a model based on a geometrically exact beam finite-element formulation. We discuss the numerical model of a non-processive motor such as myosin II, which interacts with actin filaments. Based on experimental data and insp

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9

Vandenboom, Rene. "The Myofibrillar Complex and Fatigue: A Review." Canadian Journal of Applied Physiology 29, no. 3 (2004): 330–56. http://dx.doi.org/10.1139/h04-022.

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The basis for all biological movement is the conversion of chemical energy to mechanical energy by different classes of motor proteins. In skeletal muscle this motor protein is myosin II, a thick filament-based molecule that harnesses the free energy furnished by ATP hydrolysis to perform mechanical work against actin proteins of the thin filament. The cyclic attachment and detachment of myosin with actin that generates muscle force and shortening is Ca2+ regulated. Intense muscle activity may lead to metabolically induced inhibitions to the function of these myofibrillar proteins when Ca2+ re

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10

McQuarrie, Irvine G., and Linda M. Lund. "INTRA-AXONAL MYOSIN AND ACTIN IN NERVE REGENERATION." Neurosurgery 65, suppl_4 (2009): A93—A96. http://dx.doi.org/10.1227/01.neu.0000338593.76635.32.

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Abstract A FOCUSED REVIEW of sciatic nerve regeneration in the rat model, based on research conducted by the authors, is presented. We examine structural proteins carried distally in the axon by energy-requiring motor enzymes, using protein chemistry and molecular biology techniques in combination with immunohistochemistry. Relevant findings from other laboratories are cited and discussed. The general conclusion is that relatively large amounts of actin and tubulin are required to construct a regenerating axon and that these materials mainly originate in the parent axon. The motor enzymes that

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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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Wu, Hao, Jing Zhou, Tianhui Zhu, Ivan Cohen, and Jason Dictenberg. "A kinesin adapter directly mediates dendritic mRNA localization during neural development in mice." Journal of Biological Chemistry 295, no. 19 (2020): 6605–28. http://dx.doi.org/10.1074/jbc.ra118.005616.

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Motor protein-based active transport is essential for mRNA localization and local translation in animal cells, yet how mRNA granules interact with motor proteins remains poorly understood. Using an unbiased yeast two–hybrid screen for interactions between murine RNA-binding proteins (RBPs) and motor proteins, here we identified protein interaction with APP tail-1 (PAT1) as a potential direct adapter between zipcode-binding protein 1 (ZBP1, a β-actin RBP) and the kinesin-I motor complex. The amino acid sequence of mouse PAT1 is similar to that of the kinesin light chain (KLC), and we found that

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Goodson, H. V., B. L. Anderson, H. M. Warrick, L. A. Pon, and J. A. Spudich. "Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton." Journal of Cell Biology 133, no. 6 (1996): 1277–91. http://dx.doi.org/10.1083/jcb.133.6.1277.

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The organization of the actin cytoskeleton plays a critical role in cell physiology in motile and nonmotile organisms. Nonetheless, the function of the actin based motor molecules, members of the myosin superfamily, is not well understood. Deletion of MYO3, a yeast gene encoding a "classic" myosin I, has no detectable phenotype. We used a synthetic lethality screen to uncover genes whose functions might overlap with those of MYO3 and identified a second yeast myosin 1 gene, MYO5. MYO5 shows 86 and 62% identity to MYO3 across the motor and non-motor regions. Both genes contain an amino terminal

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Meinecke, Christoph R., Georg Heldt, Thomas Blaudeck, et al. "Nanolithographic Fabrication Technologies for Network-Based Biocomputation Devices." Materials 16, no. 3 (2023): 1046. http://dx.doi.org/10.3390/ma16031046.

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Network-based biocomputation (NBC) relies on accurate guiding of biological agents through nanofabricated channels produced by lithographic patterning techniques. Here, we report on the large-scale, wafer-level fabrication of optimized microfluidic channel networks (NBC networks) using electron-beam lithography as the central method. To confirm the functionality of these NBC networks, we solve an instance of a classical non-deterministic-polynomial-time complete (“NP-complete”) problem, the subset-sum problem. The propagation of cytoskeletal filaments, e.g., molecular motor-propelled microtubu

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15

Balabanian, Linda, Abdullah R. Chaudhary, and Adam G. Hendricks. "Traffic control inside the cell: microtubule-based regulation of cargo transport." Biochemist 40, no. 2 (2018): 14–17. http://dx.doi.org/10.1042/bio04002014.

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The cell relies on an intricate system of molecular highways and motors to transport proteins, organelles and other vesicular cargoes to their proper locations. Microtubules, long filaments that form a network throughout the cell, act as highways. The motor proteins kinesin and dynein associate with cargoes and transport them along microtubules. Rather than simply acting as passive tracks, microtubules contain signals that regulate kinesin and dynein to target cargoes to specific locations in the cell. These signals include the organization of the microtubule network, chemical modifications th

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Phillips, J. C. "Self-organized networks: Darwinian evolution of dynein rings, stalks, and stalk heads." Proceedings of the National Academy of Sciences 117, no. 14 (2020): 7799–802. http://dx.doi.org/10.1073/pnas.1920840117.

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Cytoskeletons are self-organized networks based on polymerized proteins: actin, tubulin, and driven by motor proteins, such as myosin, kinesin, and dynein. Their positive Darwinian evolution enables them to approach optimized functionality (self-organized criticality). Dynein has three distinct titled subunits, but how these units connect to function as a molecular motor is mysterious. Dynein binds to tubulin through two coiled coil stalks and a stalk head. The energy used to alter the head binding and propel cargo along tubulin is supplied by ATP at a ring 1,500 amino acids away. Here, we sho

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17

Kallio, Juha Pekka, and Inari Kursula. "Recombinant production, purification and crystallization of theToxoplasma gondiicoronin WD40 domain." Acta Crystallographica Section F Structural Biology Communications 70, no. 4 (2014): 517–21. http://dx.doi.org/10.1107/s2053230x14005196.

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Toxoplasma gondiiis one of the most widely spread parasitic organisms in the world. Together with other apicomplexan parasites, it utilizes a special actin–myosin motor for its cellular movement, called gliding motility. This actin-based process is regulated by a small set of actin-binding proteins, which in Apicomplexa comprises only 10–15 proteins, compared with >150 in higher eukaryotes. Coronin is a highly conserved regulator of the actin cytoskeleton, but its functions, especially in parasites, have remained enigmatic. Coronins consist of an N-terminal actin-binding β-propeller WD40 do

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18

Pertici, Irene, Giulio Bianchi, Lorenzo Bongini, Vincenzo Lombardi, and Pasquale Bianco. "A Myosin II-Based Nanomachine Devised for the Study of Ca2+-Dependent Mechanisms of Muscle Regulation." International Journal of Molecular Sciences 21, no. 19 (2020): 7372. http://dx.doi.org/10.3390/ijms21197372.

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The emergent properties of the array arrangement of the molecular motor myosin II in the sarcomere of the striated muscle, the generation of steady force and shortening, can be studied in vitro with a synthetic nanomachine made of an ensemble of eight heavy-meromyosin (HMM) fragments of myosin from rabbit psoas muscle, carried on a piezoelectric nanopositioner and brought to interact with a properly oriented actin filament attached via gelsolin (a Ca2+-regulated actin binding protein) to a bead trapped by dual laser optical tweezers. However, the application of the original version of the nano

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19

Doran, Matthew H., and William Lehman. "The Central Role of the F-Actin Surface in Myosin Force Generation." Biology 10, no. 12 (2021): 1221. http://dx.doi.org/10.3390/biology10121221.

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Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and cell motility. Once polymerized from G-actin, F-actin forms the central core of muscle-thin filaments and acts as molecular tracks for myosin-based motor activity. The ATP-dependent cross-bridge cycle of myosin attachment and detachment drives the sliding of myosin thick filaments past thin filament

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20

Lee, Beth. "Myosins in Osteoclast Formation and Function." Biomolecules 8, no. 4 (2018): 157. http://dx.doi.org/10.3390/biom8040157.

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Skeletal quantity and quality are determined by processes of bone modeling and remodeling, which are undertaken by cells that build and resorb bone as they respond to mechanical, hormonal, and other external and internal signals. As the sole bone resorptive cell type, osteoclasts possess a remarkably dynamic actin cytoskeleton that drives their function in this enterprise. Actin rearrangements guide osteoclasts’ capacity for precursor fusion during differentiation, for migration across bone surfaces and sensing of their composition, and for generation of unique actin superstructures required f

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Vale, Ronald D., Ryan Case, Elena Sablin, Cindy Hart, and Robert Fletterick. "Searching for kinesin's mechanical amplifier." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1396 (2000): 449–57. http://dx.doi.org/10.1098/rstb.2000.0586.

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Kinesin, a microtubule–based motor, and myosin, an actin–based motor, share a similar core structure, indicating that they arose from a common ancestor. However, kinesin lacks the long lever–arm domain that is believed to drive the myosin power stroke. Here, we present evidence that a much smaller region of ca . 10–40 amino acids serves as a mechanical element for kinesin motor proteins. These ‘neck regions’ are class conserved and have distinct structures in plus–end and minus–end–directed kinesin motors. Mutagenesis studies also indicate that the neck regions are involved in coupling ATP hyd

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22

Zakrzewski, Przemysław, Maria Jolanta Rędowicz, Folma Buss, and Marta Lenartowska. "Loss of myosin VI expression affects acrosome/acroplaxome complex morphology during mouse spermiogenesis†." Biology of Reproduction 103, no. 3 (2020): 521–33. http://dx.doi.org/10.1093/biolre/ioaa071.

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Abstract During spermiogenesis in mammals, actin filaments and a variety of actin-binding proteins are involved in the formation and function of highly specialized testis-specific structures. Actin-based motor proteins, such as myosin Va and VIIa, play a key role in this complex process of spermatid transformation into mature sperm. We have previously demonstrated that myosin VI (MYO6) is also expressed in mouse testes. It is present in actin-rich structures important for spermatid development, including one of the earliest events in spermiogenesis—acrosome formation. Here, we demonstrate usin

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Furuta, Akane, Misako Amino, Maki Yoshio, Kazuhiro Oiwa, Hiroaki Kojima, and Ken'ya Furuta. "Creating biomolecular motors based on dynein and actin-binding proteins." Nature Nanotechnology 12, no. 3 (2016): 233–37. http://dx.doi.org/10.1038/nnano.2016.238.

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Teves, Maria, Eduardo Roldan, Diego Krapf, Jerome Strauss III, Virali Bhagat, and Paulene Sapao. "Sperm Differentiation: The Role of Trafficking of Proteins." International Journal of Molecular Sciences 21, no. 10 (2020): 3702. http://dx.doi.org/10.3390/ijms21103702.

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Sperm differentiation encompasses a complex sequence of morphological changes that takes place in the seminiferous epithelium. In this process, haploid round spermatids undergo substantial structural and functional alterations, resulting in highly polarized sperm. Hallmark changes during the differentiation process include the formation of new organelles, chromatin condensation and nuclear shaping, elimination of residual cytoplasm, and assembly of the sperm flagella. To achieve these transformations, spermatids have unique mechanisms for protein trafficking that operate in a coordinated fashi

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Ghulam, Ali, Rahu Sikander, Dhani Bux Talpur, et al. "IDENTIFYING MOLECULAR FUNCTIONS OF DYNEIN MOTOR PROTEINS USING EXTREME GRADIENT BOOSTING ALGORITHM WITH MACHINE LEARNING." Journal of Mountain Area Research 8 (November 29, 2022): 1. http://dx.doi.org/10.53874/jmar.v8i0.166.

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The majority of cytoplasmic proteins and vesicles move actively primarily to dynein motor proteins, which are the cause of muscle contraction. Moreover, identifying how dynein are used in cells will rely on structural knowledge. Cytoskeletal motor proteins have different molecular roles and structures, and they belong to three superfamilies of dynamin, actin and myosin. Loss of function of specific molecular motor proteins can be attributed to a number of human diseases, such as Charcot-Charcot-Dystrophy and kidney disease. It is crucial to create a precise model to identify dynein motor prote

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Coffman, Valerie C., Aaron H. Nile, I.-Ju Lee, Huayang Liu, and Jian-Qiu Wu. "Roles of Formin Nodes and Myosin Motor Activity in Mid1p-dependent Contractile-Ring Assembly during Fission Yeast Cytokinesis." Molecular Biology of the Cell 20, no. 24 (2009): 5195–210. http://dx.doi.org/10.1091/mbc.e09-05-0428.

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Two prevailing models have emerged to explain the mechanism of contractile-ring assembly during cytokinesis in the fission yeast Schizosaccharomyces pombe: the spot/leading cable model and the search, capture, pull, and release (SCPR) model. We tested some of the basic assumptions of the two models. Monte Carlo simulations of the SCPR model require that the formin Cdc12p is present in >30 nodes from which actin filaments are nucleated and captured by myosin-II in neighboring nodes. The force produced by myosin motors pulls the nodes together to form a compact contractile ring. Live microsco

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Evangelista, Marie, Bert M. Klebl, Amy H. Y. Tong, et al. "A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex." Journal of Cell Biology 148, no. 2 (2000): 353–62. http://dx.doi.org/10.1083/jcb.148.2.353.

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Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followed by an acidic domain. The myosin-I SH3 domain interacted with both Bee1p and Vrp1p, yeast homologues of human WASP and WIP, adapter proteins that link actin assembly and signaling molecules. The myosin-I acidic domain interacted with Arp2/3 complex subunits, Arc40p and Arc19p

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ROMET-LEMONNE, GUILLAUME, EMMANUELE HELFER, VINCENT DELATOUR, et al. "BIOMIMETIC SYSTEMS SHED LIGHT ON ACTIN-BASED MOTILITY DOWN TO THE MOLECULAR SCALE." Biophysical Reviews and Letters 04, no. 01n02 (2009): 5–15. http://dx.doi.org/10.1142/s1793048009000909.

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Cell motility, one of the modular activities of living cells, elicits the response of the cell to extra-cellular signals, to move directionally, feed, divide or transport materials. The combined actions of molecular motors and re-modeling of the cytoskeleton generate forces and movement. Here we describe mechanistic approaches of force and movement produced by site-directed assembly of actin filaments. The insight derived from a biochemical analysis of the protein machineries involved in "actin-based motile processes" like cell protrusions, invaginations, organelle propulsion, is used to build

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He, Jiayi, Yixing Qiu, Lei Tan, et al. "Understanding the key functions of Myosins in viral infection." Biochemical Society Transactions 50, no. 1 (2022): 597–607. http://dx.doi.org/10.1042/bst20211239.

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Myosins, a class of actin-based motor proteins existing in almost any organism, are originally considered only involved in driving muscle contraction, reshaping actin cytoskeleton, and anchoring or transporting cargoes, including protein complexes, organelles, vesicles. However, accumulating evidence reveals that myosins also play vital roles in viral infection, depending on viral species and infection stages. This review systemically summarizes the described various myosins, the performed functions, and the involved mechanisms or molecular pathways during viral infection. Meanwhile, the exist

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30

Coluccio, L. M. "Myosin I." American Journal of Physiology-Cell Physiology 273, no. 2 (1997): C347—C359. http://dx.doi.org/10.1152/ajpcell.1997.273.2.c347.

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The class I myosins are single-headed, actin-binding, mechanochemical “motor” proteins with heavy chains in the molecular mass range of 110-130 kDa; they do not form filaments. Each myosin I heavy chain is associated with one to six light chains that bind to specific motifs known as IQ domains. In vertebrate myosin I isoforms, the light chain is calmodulin, which is thought to regulate motor activity. Proteins similar to calmodulin are associated with myosin I isoforms from lower eukaryotes. Some myosin I isoforms from lower eukaryotes are regulated by phosphorylation; however, the phosphoryla

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Lee, Min Joung, Yunseon Jang, Jeongsu Han, et al. "Endothelial-specific Crif1 deletion induces BBB maturation and disruption via the alteration of actin dynamics by impaired mitochondrial respiration." Journal of Cerebral Blood Flow & Metabolism 40, no. 7 (2020): 1546–61. http://dx.doi.org/10.1177/0271678x19900030.

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Cerebral endothelial cells (ECs) require junctional proteins to maintain blood–brain barrier (BBB) integrity, restricting toxic substances and controlling peripheral immune cells with a higher concentration of mitochondria than ECs of peripheral capillaries. The mechanism underlying BBB disruption by defective mitochondrial oxidative phosphorylation (OxPhos) is unclear in a mitochondria-related gene-targeted animal model. To assess the role of EC mitochondrial OxPhos function in the maintenance of the BBB, we developed an EC-specific CR6-interactin factor1 ( Crif1) deletion mouse. We clearly o

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Cornfine, Susanne, Mirko Himmel, Petra Kopp, et al. "The kinesin KIF9 and reggie/flotillin proteins regulate matrix degradation by macrophage podosomes." Molecular Biology of the Cell 22, no. 2 (2011): 202–15. http://dx.doi.org/10.1091/mbc.e10-05-0394.

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Podosomes are actin-based matrix contacts in a variety of cell types, most notably monocytic cells, and are characterized by their ability to lyse extracellular matrix material. Besides their dependence on actin regulation, podosomes are also influenced by microtubules and microtubule-dependent transport processes. Here we describe a novel role for KIF9, a previously little-characterized member of the kinesin motor family, in the regulation of podosomes in primary human macrophages. We find that small interfering RNA (siRNA)/short-hairpin RNA–induced knockdown of KIF9 significantly affects bot

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Stødkilde, Lene, Johan Palmfeldt, Line Nilsson, et al. "Proteomic identification of early changes in the renal cytoskeleton in obstructive uropathy." American Journal of Physiology-Renal Physiology 306, no. 12 (2014): F1429—F1441. http://dx.doi.org/10.1152/ajprenal.00244.2013.

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Bilateral ureteral obstruction (BUO) is associated with renal damage and impaired ability to concentrate urine and is known to induce alterations in an array of kidney proteins. The aim of this study was to identify acute proteomic alterations induced by BUO. Rats were subjected to BUO for 2, 6, or 24 h. Mass spectrometry-based proteomics was performed on the renal inner medulla, and protein changes in the obstructed group were identified. Significant changes were successfully identified for 109 proteins belonging to different biological classes. Interestingly, proteins belonging to the cytosk

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DeGiorgis, Joseph A., Thomas S. Reese, and Elaine L. Bearer. "Association of a Nonmuscle Myosin II with Axoplasmic Organelles." Molecular Biology of the Cell 13, no. 3 (2002): 1046–57. http://dx.doi.org/10.1091/mbc.01-06-0315.

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Association of motor proteins with organelles is required for the motors to mediate transport. Because axoplasmic organelles move on actin filaments, they must have associated actin-based motors, most likely members of the myosin superfamily. To gain a better understanding of the roles of myosins in the axon we used the giant axon of the squid, a powerful model for studies of axonal physiology. First, a ∼220 kDa protein was purified from squid optic lobe, using a biochemical protocol designed to isolate myosins. Peptide sequence analysis, followed by cloning and sequencing of the full-length c

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Munchow, S., C. Sauter, and R. P. Jansen. "Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins." Journal of Cell Science 112, no. 10 (1999): 1511–18. http://dx.doi.org/10.1242/jcs.112.10.1511.

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Asymmetric distribution of messenger RNAs is a widespread mechanism to localize synthesis of specific protein to distinct sites in the cell. Although not proven yet there is considerable evidence that mRNA localisation is an active process that depends on the activity of cytoskeletal motor proteins. To date, the only motor protein with a specific role in mRNA localisation is the budding yeast type V myosin Myo4p. Myo4p is required for the localisation of ASH1 mRNA, encoding a transcriptional repressor that is essential for differential expression of the HO gene and mating type switching in bud

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Zakrzewski, Przemysław, Anna Suwińska, Robert Lenartowski, Maria Jolanta Rędowicz, Folma Buss, and Marta Lenartowska. "Myosin VI maintains the actin-dependent organization of the tubulobulbar complexes required for endocytosis during mouse spermiogenesis†‡." Biology of Reproduction 102, no. 4 (2020): 863–75. http://dx.doi.org/10.1093/biolre/ioz232.

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Abstract Myosin VI (MYO6) is an actin-based motor that has been implicated in a wide range of cellular processes, including endocytosis and the regulation of actin dynamics. MYO6 is crucial for actin/membrane remodeling during the final step of Drosophila spermatogenesis, and MYO6-deficient males are sterile. This protein also localizes to actin-rich structures involved in mouse spermiogenesis. Although loss of MYO6 in Snell’s waltzer knock-out (KO) mice causes several defects and shows reduced male fertility, no studies have been published to address the role of MYO6 in sperm development in m

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Tabakaeva, Oksana, та Anton Tabakaev. "Proteins Features of the Far Eastern Region Bivalve Mollusk Mactra Сhinensis". Food Industry 5, № 1 (2020): 65–70. http://dx.doi.org/10.29141/2500-1922-2020-5-1-8.

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Bivalve mollusk are protein raw materials, their soft tissues are characterized by a hard-rubbery consistency due to its proteins characteristics and should be considered when processing into food. The proteins fractional composition study of different groups (water-soluble, myofibrillar, and stroma) is an urgent task, since it is possible to justify the processing technology based on the obtained data. The article presents the fractional composition study results of the water-soluble proteins and peptides, the molecular mass distribution of the separate components of myofibrillary proteins an

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Diefenbach, Thomas J., Vaughan M. Latham, Dean Yimlamai, Canwen A. Liu, Ira M. Herman, and Daniel G. Jay. "Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone." Journal of Cell Biology 158, no. 7 (2002): 1207–17. http://dx.doi.org/10.1083/jcb.200202028.

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The myosin family of motor proteins is implicated in mediating actin-based growth cone motility, but the roles of many myosins remain unclear. We previously implicated myosin 1c (M1c; formerly myosin Iβ) in the retention of lamellipodia (Wang et al., 1996). Here we address the role of myosin II (MII) in chick dorsal root ganglion neuronal growth cone motility and the contribution of M1c and MII to retrograde F-actin flow using chromophore-assisted laser inactivation (CALI). CALI of MII reduced neurite outgrowth and growth cone area by 25%, suggesting a role for MII in lamellipodial expansion.

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Casoni, Filippo, Manuela Basso, Tania Massignan, et al. "Protein Nitration in a Mouse Model of Familial Amyotrophic Lateral Sclerosis." Journal of Biological Chemistry 280, no. 16 (2005): 16295–304. http://dx.doi.org/10.1074/jbc.m413111200.

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Multiple mechanisms have been proposed to contribute to amyotrophic lateral sclerosis (ALS) pathogenesis, including oxidative stress. Early evidence of a role for oxidative damage was based on the finding, in patients and murine models, of high levels of markers, such as free nitrotyrosine (NT). However, no comprehensive study on the protein targets of nitration in ALS has been reported. We found an increased level of NT immunoreactivity in spinal cord protein extracts of a transgenic mouse model of familial ALS (FALS) at a presymptomatic stage of the disease compared with age-matched controls

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Lu, Ling, Yuh-Ru Julie Lee, Ruiqin Pan, Julin N. Maloof, and Bo Liu. "An Internal Motor Kinesin Is Associated with the Golgi Apparatus and Plays a Role in Trichome Morphogenesis in Arabidopsis." Molecular Biology of the Cell 16, no. 2 (2005): 811–23. http://dx.doi.org/10.1091/mbc.e04-05-0400.

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Members of the kinesin superfamily are microtubule-based motor proteins that transport molecules/organelles along microtubules. We have identified similar internal motor kinesins, Kinesin-13A, from the cotton Gossypium hirsutum and Arabidopsis thaliana. Their motor domains share high degree of similarity with those of internal motor kinesins of animals and protists in the MCAK/Kinesin13 subfamily. However, no significant sequence similarities were detected in sequences outside the motor domain. In Arabidopsis plants carrying the T-DNA knockout kinesin-13a-1 and kinesin-13a-2 mutations at the K

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Marchelletta, Ronald R., Damon T. Jacobs, Joel E. Schechter, Richard E. Cheney, and Sarah F. Hamm-Alvarez. "The class V myosin motor, myosin 5c, localizes to mature secretory vesicles and facilitates exocytosis in lacrimal acini." American Journal of Physiology-Cell Physiology 295, no. 1 (2008): C13—C28. http://dx.doi.org/10.1152/ajpcell.00330.2007.

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We investigated the role of the actin-based myosin motor, myosin 5c (Myo5c) in vesicle transport in exocrine secretion. Lacrimal gland acinar cells (LGAC) are the major source for the regulated secretion of proteins from the lacrimal gland into the tear film. Confocal fluorescence and immunogold electron microscopy revealed that Myo5c was associated with secretory vesicles in primary rabbit LGAC. Upon stimulation of secretion with the muscarinic agonist, carbachol, Myo5c was also detected in association with actin-coated fusion intermediates. Adenovirus-mediated expression of green fluorescent

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Pollard, Thomas D., and E. Michael Ostap. "The Chemical Mechanism of Myosin-I: Implications for Actin-based Motility and the Evolution of the Myosin Family of Motor Proteins." Cell Structure and Function 21, no. 5 (1996): 351–56. http://dx.doi.org/10.1247/csf.21.351.

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Barvitenko, Nadezhda, Muhammad Aslam, Alfons Lawen, et al. "Two Motors and One Spring: Hypothetic Roles of Non-Muscle Myosin II and Submembrane Actin-Based Cytoskeleton in Cell Volume Sensing." International Journal of Molecular Sciences 22, no. 15 (2021): 7967. http://dx.doi.org/10.3390/ijms22157967.

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Changes in plasma membrane curvature and intracellular ionic strength are two key features of cell volume perturbations. In this hypothesis we present a model of the responsible molecular apparatus which is assembled of two molecular motors [non-muscle myosin II (NMMII) and protrusive actin polymerization], a spring [a complex between the plasma membrane (PM) and the submembrane actin-based cytoskeleton (smACSK) which behaves like a viscoelastic solid] and the associated signaling proteins. We hypothesize that this apparatus senses changes in both the plasma membrane curvature and the ionic st

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Karpov, Pavel, Aleksey Raevsky, Maxim Korablyov, and Yaroslav Blume. "Identification of Plant Homologues of Dual Specificity Yak1-Related Kinases." Computational Biology Journal 2014 (December 8, 2014): 1–14. http://dx.doi.org/10.1155/2014/909268.

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Currently, Dual Specificity YAK1-Related Kinases (MNB/DYRK) were found in slime molds, protista, fungi, and animals, but the existence of plant homologues is still unclear. In the present study, we have identified 14 potential plant homologues with the previously unknown functions, based on the strong sequence similarity. The results of bioinformatics analysis revealed their correspondence to DYRK1A, DYRK1B, DYRK3, and DYRK4. For two plant homologues of animal DYRK1A from Physcomitrella patens and Arabidopsis thaliana spatial structures of catalytic domains were predicted, as well as their com

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Stoffler, H. E., U. Honnert, C. A. Bauer, et al. "Targeting of the myosin-I myr 3 to intercellular adherens type junctions induced by dominant active Cdc42 in HeLa cells." Journal of Cell Science 111, no. 18 (1998): 2779–88. http://dx.doi.org/10.1242/jcs.111.18.2779.

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Myr 3, a member of the myosin-I family from rat, is shown in this study to be localized at adherens-type intercellular junctions in epithelial and nonepithelial tissues. Formation of intercellular junctions and the accompanying recruitment of myr 3 to these junctions involves signaling by the Rho subfamily of small GTP-binding proteins. This conclusion is based on studies with HtTA-1 HeLa cells that were induced by overexpression of constitutively active Cdc42Hs to form typical adherens-type intercellular junctions enriched in cadherins (N-cadherin), beta-catenin, filamentous actin and myr 3.

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Raposo, Graça, Marie-Neige Cordonnier, Danièle Tenza, et al. "Association of Myosin I Alpha with Endosomes and Lysosomes in Mammalian Cells." Molecular Biology of the Cell 10, no. 5 (1999): 1477–94. http://dx.doi.org/10.1091/mbc.10.5.1477.

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Myosin Is, which constitute a ubiquitous monomeric subclass of myosins with actin-based motor properties, are associated with plasma membrane and intracellular vesicles. Myosin Is have been proposed as key players for membrane trafficking in endocytosis or exocytosis. In the present paper we provide biochemical and immunoelectron microscopic evidence indicating that a pool of myosin I alpha (MMIα) is associated with endosomes and lysosomes. We show that the overproduction of MMIα or the production of nonfunctional truncated MMIα affects the distribution of the endocytic compartments. We also s

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Månsson, Alf. "Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction." International Journal of Molecular Sciences 21, no. 21 (2020): 8399. http://dx.doi.org/10.3390/ijms21218399.

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Muscle contraction results from cyclic interactions between myosin II motors and actin with two sets of proteins organized in overlapping thick and thin filaments, respectively, in a nearly crystalline lattice in a muscle sarcomere. However, a sarcomere contains a huge number of other proteins, some with important roles in muscle contraction. In particular, these include thin filament proteins, troponin and tropomyosin; thick filament proteins, myosin binding protein C; and the elastic protein, titin, that connects the thin and thick filaments. Furthermore, the order and 3D organization of the

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Geva, Polina, Konstantin Komoshvili, and Stella Liberman-Aronov. "Two- and Three-Dimensional Tracking of MFA2 mRNA Molecules in Mating Yeast." Cells 9, no. 10 (2020): 2151. http://dx.doi.org/10.3390/cells9102151.

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Intracellular mRNA transport contributes to the spatio-temporal regulation of mRNA function and localized translation. In the budding yeast, Saccharomyces cerevisiae, asymmetric mRNA transport localizes ~30 specific mRNAs including those encoding polarity and secretion factors, to the bud tip. The underlying process involves RNA-binding proteins (RBPs), molecular motors, processing bodies (PBs), and the actin cytoskeleton. Recently, pheromone a-factor expression in mating yeast was discovered to depend on proper localization of its mRNA, MFA2 mRNAs in conjunction with PBs cluster at the shmoo

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Blanc, Florian, Tatiana Isabet, Hannah Benisty, H. Lee Sweeney, Marco Cecchini, and Anne Houdusse. "An intermediate along the recovery stroke of myosin VI revealed by X-ray crystallography and molecular dynamics." Proceedings of the National Academy of Sciences 115, no. 24 (2018): 6213–18. http://dx.doi.org/10.1073/pnas.1711512115.

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Myosins form a class of actin-based, ATPase motor proteins that mediate important cellular functions such as cargo transport and cell motility. Their functional cycle involves two large-scale swings of the lever arm: the force-generating powerstroke, which takes place on actin, and the recovery stroke during which the lever arm is reprimed into an armed configuration. Previous analyses of the prerecovery (postrigor) and postrecovery (prepowerstroke) states predicted that closure of switch II in the ATP binding site precedes the movement of the converter and the lever arm. Here, we report on a

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Jacobs, Damon T., Roberto Weigert, Kyle D. Grode, Julie G. Donaldson, and Richard E. Cheney. "Myosin Vc Is a Molecular Motor That Functions in Secretory Granule Trafficking." Molecular Biology of the Cell 20, no. 21 (2009): 4471–88. http://dx.doi.org/10.1091/mbc.e08-08-0865.

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Class V myosins are actin-based motor proteins that have critical functions in organelle trafficking. Of the three class V myosins expressed in mammals, relatively little is known about Myo5c except that it is abundant in exocrine tissues. Here we use MCF-7 cells to identify the organelles that Myo5c associates with, image the dynamics of Myo5c in living cells, and test the functions of Myo5c. Endogenous Myo5c localizes to two distinct compartments: small puncta and slender tubules. Myo5c often exhibits a highly polarized distribution toward the leading edge in migrating cells and is clearly d

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