Academic literature on the topic 'Myosin II Superfamily'
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Journal articles on the topic "Myosin II Superfamily"
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Berg, Jonathan S., Bradford C. Powell, and Richard E. Cheney. "A Millennial Myosin Census." Molecular Biology of the Cell 12, no. 4 (April 2001): 780–94. http://dx.doi.org/10.1091/mbc.12.4.780.
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The past decade has seen a remarkable explosion in our knowledge of the size and diversity of the myosin superfamily. Since these actin-based motors are candidates to provide the molecular basis for many cellular movements, it is essential that motility researchers be aware of the complete set of myosins in a given organism. The availability of cDNA and/or draft genomic sequences from humans,Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana,Saccharomyces cerevisiae, Schizosaccharomyces pombe, andDictyostelium discoideum has allowed us to tentatively define and compare the sets of myosin genes in these organisms. This analysis has also led to the identification of several putative myosin genes that may be of general interest. In humans, for example, we find a total of 40 known or predicted myosin genes including two new myosins-I, three new class II (conventional) myosins, a second member of the class III/ninaC myosins, a gene similar to the class XV deafness myosin, and a novel myosin sharing at most 33% identity with other members of the superfamily. These myosins are in addition to the recently discovered class XVI myosin with N-terminal ankyrin repeats and two human genes with similarity to the class XVIII PDZ-myosin from mouse. We briefly describe these newly recognized myosins and extend our previous phylogenetic analysis of the myosin superfamily to include a comparison of the complete or nearly complete inventories of myosin genes from several experimentally important organisms.
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Syamaladevi, Divya P., James A. Spudich, and R. Sowdhamini. "Structural and Functional Insights on the Myosin Superfamily." Bioinformatics and Biology Insights 6 (January 2012): BBI.S8451. http://dx.doi.org/10.4137/bbi.s8451.
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The myosin superfamily is a versatile group of molecular motors involved in the transport of specific biomolecules, vesicles and organelles in eukaryotic cells. The processivity of myosins along an actin filament and transport of intracellular ‘cargo’ are achieved by generating physical force from chemical energy of ATP followed by appropriate conformational changes. The typical myosin has a head domain, which harbors an ATP binding site, an actin binding site, and a light-chain bound ‘lever arm’, followed often by a coiled coil domain and a cargo binding domain. Evolution of myosins started at the point of evolution of eukaryotes, S. cerevisiae being the simplest one known to contain these molecular motors. The coiled coil domain of the myosin classes II, V and VI in whole genomes of several model organisms display differences in the length and the strength of interactions at the coiled coil interface. Myosin II sequences have long-length coiled coil regions that are predicted to have a highly stable dimeric interface. These are interrupted, however, by regions that are predicted to be unstable, indicating possibilities of alternate conformations, associations to make thick filaments, and interactions with other molecules. Myosin V sequences retain intermittent regions of strong and weak interactions, whereas myosin VI sequences are relatively devoid of strong coiled coil motifs. Structural deviations at coiled coil regions could be important for carrying out normal biological function of these proteins.
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Pernier, Julien, and Kristine Schauer. "Does the Actin Network Architecture Leverage Myosin-I Functions?" Biology 11, no. 7 (June 29, 2022): 989. http://dx.doi.org/10.3390/biology11070989.
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The actin cytoskeleton plays crucial roles in cell morphogenesis and functions. The main partners of cortical actin are molecular motors of the myosin superfamily. Although our understanding of myosin functions is heavily based on myosin-II and its ability to dimerize, the largest and most ancient class is represented by myosin-I. Class 1 myosins are monomeric, actin-based motors that regulate a wide spectrum of functions, and whose dysregulation mediates multiple human diseases. We highlight the current challenges in identifying the “pantograph” for myosin-I motors: we need to reveal how conformational changes of myosin-I motors lead to diverse cellular as well as multicellular phenotypes. We review several mechanisms for scaling, and focus on the (re-) emerging function of class 1 myosins to remodel the actin network architecture, a higher-order dynamic scaffold that has potential to leverage molecular myosin-I functions. Undoubtfully, understanding the molecular functions of myosin-I motors will reveal unexpected stories about its big partner, the dynamic actin cytoskeleton.
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Porro, Chiara, Antonio Pennella, Maria Antonietta Panaro, and Teresa Trotta. "Functional Role of Non-Muscle Myosin II in Microglia: An Updated Review." International Journal of Molecular Sciences 22, no. 13 (June 22, 2021): 6687. http://dx.doi.org/10.3390/ijms22136687.
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Myosins are a remarkable superfamily of actin-based motor proteins that use the energy derived from ATP hydrolysis to translocate actin filaments and to produce force. Myosins are abundant in different types of tissues and involved in a large variety of cellular functions. Several classes of the myosin superfamily are expressed in the nervous system; among them, non-muscle myosin II (NM II) is expressed in both neurons and non-neuronal brain cells, such as astrocytes, oligodendrocytes, endothelial cells, and microglia. In the nervous system, NM II modulates a variety of functions, such as vesicle transport, phagocytosis, cell migration, cell adhesion and morphology, secretion, transcription, and cytokinesis, as well as playing key roles during brain development, inflammation, repair, and myelination functions. In this review, we will provide a brief overview of recent emerging roles of NM II in resting and activated microglia cells, the principal regulators of immune processes in the central nervous system (CNS) in both physiological and pathological conditions. When stimulated, microglial cells react and produce a number of mediators, such as pro-inflammatory cytokines, free radicals, and nitric oxide, that enhance inflammation and contribute to neurodegenerative diseases. Inhibition of NM II could be a new therapeutic target to treat or to prevent CNS diseases.
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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 (March 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 cDNA, identified this ∼220 kDa protein as a nonmuscle myosin II. This myosin is also present in axoplasm, as determined by two independent criteria. First, RT-PCR using sequence-specific primers detected the transcript in the stellate ganglion, which contains the cell bodies that give rise to the giant axon. Second, Western blot analysis using nonmuscle myosin II isotype-specific antibodies detected a single ∼220 kDa band in axoplasm. Axoplasm was fractionated through a four-step sucrose gradient after 0.6 M KI treatment, which separates organelles from cytoskeletal components. Of the total nonmuscle myosin II in axoplasm, 43.2% copurified with organelles in the 15% sucrose fraction, while the remainder (56.8%) was soluble and found in the supernatant. This myosin decorates the cytoplasmic surface of 21% of the axoplasmic organelles, as demonstrated by immunogold electron-microscopy. Thus, nonmuscle myosin II is synthesized in the cell bodies of the giant axon, is present in the axon, and is associated with isolated axoplasmic organelles. Therefore, in addition to myosin V, this myosin is likely to be an axoplasmic organelle motor.
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Hofmann, Wilma A., Terezina Johnson, Marcin Klapczynski, Ji-Lao Fan, and Primal de Lanerolle. "From transcription to transport: emerging roles for nuclear myosin IThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (August 2006): 418–26. http://dx.doi.org/10.1139/o06-069.
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Myosins are a superfamily of actin-activated ATPases that, in the cytoplasm, work together with actin as molecular motors. The presence of actin in the nucleus has been known for many years. The demonstration of a nuclear isoform of a myosin, nuclear myosin I (NMI), stimulated a great deal of interest in possible intranuclear motor functions of an acto–NMI complex. NMI has been shown to be involved in transcription by RNA polymerases I and II. In both cases, NMI interacts with the respective polymerase and is critically involved in the basic process of transcription. A recent study on intranuclear long-range chromosome movement has now demonstrated a role for NMI in the translocation of chromosome regions as well. Moreover, this movement is based on an active and directed process that is facilitated by an acto–NMI complex, establishing for the first time a functional role for a motor complex consisting of actin and a myosin in the nucleus.
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Ostap, E. M., and T. D. Pollard. "Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase." Journal of Cell Biology 132, no. 6 (March 15, 1996): 1053–60. http://dx.doi.org/10.1083/jcb.132.6.1053.
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Acanthamoeba myosin-IA and myosin-IB are single-headed molecular motors that may play an important role in membrane-based motility. To better define the types of motility that myosin-IA and myosin IB can support, we determined the rate constants for key steps on the myosin-I ATPase pathway using fluorescence stopped-flow, cold-chase, and rapid-quench techniques. We determined the rate constants for ATP binding, ATP hydrolysis, actomyosin-I dissociation, phosphate release, and ADP release. We also determined equilibrium constants for myosin-I binding to actin filaments, ADP binding to actomyosin-I, and ATP hydrolysis. These rate constants define an ATPase mechanism in which (a) ATP rapidly dissociates actomyosin-I, (b) the predominant steady-state intermediates are in a rapid equilibrium between actin-bound and free states, (c) phosphate release is rate limiting and regulated by heavy-chain phosphorylation, and (d) ADP release is fast. Thus, during steady-state ATP hydrolysis, myosin-I is weakly bound to the actin filament like skeletal muscle myosin-II and unlike the microtubule-based motor kinesin. Therefore, for myosin-I to support processive motility or cortical contraction, multiple myosin-I molecules must be specifically localized to a small region on a membrane or in the actin-rich cell cortex. This conclusion has important implications for the regulation of myosin-I via localization through the unique myosin-I tails. This is the first complete transient kinetic characterization of a member of the myosin superfamily, other than myosin-II, providing the opportunity to obtain insights about the evolution of all myosin isoforms.
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Reddy, Kumar B. "Regulation of αIIbβ3-Signaling by Myomesin Family of Proteins." Blood 110, no. 11 (November 16, 2007): 3893. http://dx.doi.org/10.1182/blood.v110.11.3893.3893.
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Abstract Integrins are the type-I transmembrane proteins. They function as heterodimers of α and β subunits. The platelet integrin αIIbβ3 (GPIIb-IIIa) served as the model system in understanding the signaling across integrin receptors. αIIbβ3 exists in a resting state on circulating platelets and can be activated via several inside-out signaling pathways resulting in binding to its ligands, such as fibrinogen (Fg). The inside-out signaling appears to be regulated by several cytoskeletal and signaling proteins, which directly associate with the cytoplasmic tails of αIIbβ3. We have previously identified skelemin/myomesin-I as the cytoskeletal protein that interacted with the cytoplasmic tail of β3-integrins. Skelemin/myomesin-I is very closely related to two other members: myomesins-II and III. Myomesins I-III, along with other proteins such as titin and myosin light chain kinases, are members of a much larger superfamily of proteins. The hallmark of this family of proteins is the presence of a variable number of fibronectin (Fn)-like and immunoglobulin (Ig)-like motifs. Myomesin-I contains five Fn-motifs flanked by a total of seven Ig-like motifs. The interaction between β3-integrin and myomesin-I occurs via the C-terminal Ig motifs 3–7 of myomsin-I. In order to understand the functional consequence of this interaction between myomesin-I and β3-integrin, we measured the ligand binding properties of αIIbβ3 in a CHO cell model system. We found that expression of Ig motifs 3–7 increased Fg binding to the αIIbβ3, comparable to talin-head domain, used as the positive control. However, the expression of smaller and individual Ig motifs 4 and 5 resulted in still significantly higher Fg-binding to αIIbβ3. Ig motifs from myomesin-II also behaved in a similar fashion. We also found that myomesin-II is ubiquitously expressed in all the cell types tested, including platelets, suggesting myomesin-II is the likely candidate among various myomesin family members for the regulation of signaling across αIIbβ3. Our results suggest that the Ig motifs of the myomesin represent novel domains, which can regulate inside-out signaling across αIIbβ3.
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Sorci, Guglielmo, Francesca Riuzzi, Cataldo Arcuri, Ileana Giambanco, and Rosario Donato. "Amphoterin Stimulates Myogenesis and Counteracts the Antimyogenic Factors Basic Fibroblast Growth Factor and S100B via RAGE Binding." Molecular and Cellular Biology 24, no. 11 (June 1, 2004): 4880–94. http://dx.doi.org/10.1128/mcb.24.11.4880-4894.2004.
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ABSTRACT The receptor for advanced glycation end products (RAGE), a multiligand receptor of the immunoglobulin superfamily, has been implicated in the inflammatory response, diabetic angiopathy and neuropathy, neurodegeneration, cell migration, tumor growth, neuroprotection, and neuronal differentiation. We show here that (i) RAGE is expressed in skeletal muscle tissue and its expression is developmentally regulated and (ii) RAGE engagement by amphoterin (HMGB1), a RAGE ligand, in rat L6 myoblasts results in stimulation of myogenic differentiation via activation of p38 mitogen-activated protein kinase (MAPK), up-regulation of myogenin and myosin heavy chain expression, and induction of muscle creatine kinase. No such effects were detected in myoblasts transfected with a RAGE mutant lacking the transducing domain or myoblasts transfected with a constitutively inactive form of the p38 MAPK upstream kinase, MAPK kinase 6, Cdc42, or Rac-1. Moreover, amphoterin counteracted the antimyogenic activity of the Ca2+-modulated protein S100B, which was reported to inhibit myogenic differentiation via inactivation of p38 MAPK, and basic fibroblast growth factor (bFGF), a known inhibitor of myogenic differentiation, in a manner that was inversely related to the S100B or bFGF concentration and directly related to the extent of RAGE expression. These data suggest that RAGE and amphoterin might play an important role in myogenesis, accelerating myogenic differentiation via Cdc42-Rac-1-MAPK kinase 6-p38 MAPK.
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Xuan, Mei-Fu, Zhao-Bo Luo, Jun-Xia Wang, Qing Guo, Sheng-Zhong Han, Song-Shan Jin, Jin-Dan Kang, and Xi-Jun Yin. "Shift from slow- to fast-twitch muscle fibres in skeletal muscle of newborn heterozygous and homozygous myostatin-knockout piglets." Reproduction, Fertility and Development 31, no. 10 (2019): 1628. http://dx.doi.org/10.1071/rd19103.
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Myostatin (MSTN) is a member of the transforming growth factor-β superfamily that negatively regulates skeletal muscle development. A lack of MSTN induces muscle hypertrophy and increases formation of fast-twitch (Type II) muscle fibres. This study investigated muscle development in newborn heterozygous (MSTN+/−) and homozygous (MSTN−/−) MSTN-knockout piglets. Detailed morphological and gene and protein expression analyses were performed of the biceps femoris, semitendinosus and diaphragm of MSTN+/−, MSTN−/− and wild-type (WT) piglets. Haematoxylin–eosin staining revealed that the cross-sectional area of muscle fibres was significantly larger in MSTN-knockout than WT piglets. ATPase staining demonstrated that the percentage of Type IIb and IIa muscle fibres was significantly higher in MSTN−/− and MSTN+/− piglets respectively than in WT piglets. Western blotting showed that protein expression of myosin heavy chain-I was reduced in muscles of MSTN-knockout piglets. Quantitative reverse transcription–polymerase chain reaction revealed that, compared with WT piglets, myogenic differentiation factor (MyoD) mRNA expression in muscles was 1.3- to 2-fold higher in MSTN+/− piglets and 1.8- to 3.5-fold higher MSTN−/− piglets (P<0.05 and P<0.01 respectively). However, expression of myocyte enhancer factor 2C (MEF2C) mRNA in muscles was significantly lower in MSTN+/− than WT piglets (P<0.05). MSTN plays an important role in skeletal muscle development and regulates muscle fibre type by modulating the gene expression of MyoD and MEF2C in newborn piglets.
Conference papers on the topic "Myosin II Superfamily"
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Egan, Paul F., Philip R. LeDuc, Jonathan Cagan, and Christian Schunn. "A Design Exploration of Genetically Engineered Myosin Motors." In ASME 2011 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2011. http://dx.doi.org/10.1115/detc2011-48568.
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As technology advances, there is an increasing need to reliably output mechanical work at smaller scales. At the nanoscale, one of the most promising routes is utilizing biomolecular motors such as myosin proteins commonly found in cells. Myosins convert chemical energy into mechanical energy and are strong candidates for use as components of artificial nanodevices and multi-scale systems. Isoforms of the myosin superfamily of proteins are fine-tuned for specific cellular tasks such as intracellular transport, cell division, and muscle contraction. The modular structure that all myosins share makes it possible to genetically engineer them for fine-tuned performance in specific applications. In this study, a parametric analysis is conducted in order to explore the design space of Myosin II isoforms. The crossbridge model for myosin mechanics is used as a basis for a parametric study. The study sweeps commonly manipulated myosin performance variables and explores novel ways of tuning their performance. The analysis demonstrates the extent that myosin designs are alterable. Additionally, the study informs the biological community of gaps in experimentally tabulated myosin design parameters. The study lays the foundation for further progressing the design and optimization of individual myosins, a pivotal step in the eventual utilization of custom-built biomotors for a broad range of innovative nanotechnological devices.