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Relevant bibliographies by topics / Nonmucle Myosin IIs (NM-IIs)

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Academic literature on the topic 'Nonmucle Myosin IIs (NM-IIs)'

Author: Grafiati

Published: 7 September 2023

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Journal articles on the topic "Nonmucle Myosin IIs (NM-IIs)"

1

Lee, Kyoung Hwan, Guidenn Sulbarán, Shixin Yang, et al. "Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals." Proceedings of the National Academy of Sciences 115, no. 9 (2018): E1991—E2000. http://dx.doi.org/10.1073/pnas.1715247115.

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Electron microscope studies have shown that the switched-off state of myosin II in muscle involves intramolecular interaction between the two heads of myosin and between one head and the tail. The interaction, seen in both myosin filaments and isolated molecules, inhibits activity by blocking actin-binding and ATPase sites on myosin. This interacting-heads motif is highly conserved, occurring in invertebrates and vertebrates, in striated, smooth, and nonmuscle myosin IIs, and in myosins regulated by both Ca2+ binding and regulatory light-chain phosphorylation. Our goal was to determine how ear

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2

Dey, Sumit K., Raman K. Singh, Shyamtanu Chattoraj, et al. "Differential role of nonmuscle myosin II isoforms during blebbing of MCF-7 cells." Molecular Biology of the Cell 28, no. 8 (2017): 1034–42. http://dx.doi.org/10.1091/mbc.e16-07-0524.

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Bleb formation has been correlated with nonmuscle myosin II (NM-II) activity. Whether three isoforms of NM-II (NM-IIA, -IIB and -IIC) have the same or differential roles in bleb formation is not well understood. Here we report that ectopically expressed, GFP-tagged NM-II isoforms exhibit different types of membrane protrusions, such as multiple blebs, lamellipodia, combinations of both, or absence of any such protrusions in MCF-7 cells. Quantification suggests that 50% of NM-IIA-GFP–, 29% of NM-IIB-GFP–, and 19% of NM-IIC1-GFP–expressing MCF-7 cells show multiple bleb formation, compared with

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3

Wang, Aibing, Neil Billington, Robert S. Adelstein, and James R. Sellers. "Expression and Characterization of Full Length Nonmuscle Myosin IIs." Biophysical Journal 100, no. 3 (2011): 594a. http://dx.doi.org/10.1016/j.bpj.2010.12.3425.

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4

Lin, Yu-Hung, Yen-Yi Zhen, Kun-Yi Chien, et al. "LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell migration." Molecular Biology of the Cell 28, no. 8 (2017): 1054–65. http://dx.doi.org/10.1091/mbc.e15-04-0218.

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Nonmuscle myosin II (NM-II) is an important motor protein involved in cell migration. Incorporation of NM-II into actin stress fiber provides a traction force to promote actin retrograde flow and focal adhesion assembly. However, the components involved in regulation of NM-II activity are not well understood. Here we identified a novel actin stress fiber–associated protein, LIM and calponin-homology domains 1 (LIMCH1), which regulates NM-II activity. The recruitment of LIMCH1 into contractile stress fibers revealed its localization complementary to actinin-1. LIMCH1 interacted with NM-IIA, but

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5

Saha, Shekhar, Sumit K. Dey, Provas Das, and Siddhartha S. Jana. "Increased expression of nonmuscle myosin IIs is associated with 3MC-induced mouse tumor." FEBS Journal 278, no. 21 (2011): 4025–34. http://dx.doi.org/10.1111/j.1742-4658.2011.08306.x.

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6

Yuen, Samantha L., Ozgur Ogut, and Frank V. Brozovich. "Nonmuscle myosin is regulated during smooth muscle contraction." American Journal of Physiology-Heart and Circulatory Physiology 297, no. 1 (2009): H191—H199. http://dx.doi.org/10.1152/ajpheart.00132.2009.

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The participation of nonmuscle myosin in force maintenance is controversial. Furthermore, its regulation is difficult to examine in a cellular context, as the light chains of smooth muscle and nonmuscle myosin comigrate under native and denaturing electrophoresis techniques. Therefore, the regulatory light chains of smooth muscle myosin (SM-RLC) and nonmuscle myosin (NM-RLC) were purified, and these proteins were resolved by isoelectric focusing. Using this method, intact mouse aortic smooth muscle homogenates demonstrated four distinct RLC isoelectric variants. These spots were identified as

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7

Pleines, Irina, and Bernhard Nieswandt. "RhoA/ROCK guides NMII on the way to MK polyploidy." Blood 128, no. 26 (2016): 3025–26. http://dx.doi.org/10.1182/blood-2016-11-746685.

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A unique feature of megakaryocyte maturation is the switch from mitosis to replication of DNA without cell division, a process termed endomitosis. In this issue of Blood, Roy et al elegantly demonstrate that RhoA/ROCK signaling is critical for the differential activity and localization of nonmuscle myosin (NM) IIA and IIB isoforms at the megakaryocyte cleavage furrow, a key step in the induction of endomitosis.1

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8

Breckenridge, Mark T., Natalya G. Dulyaninova, and Thomas T. Egelhoff. "Multiple Regulatory Steps Control Mammalian Nonmuscle Myosin II Assembly in Live Cells." Molecular Biology of the Cell 20, no. 1 (2009): 338–47. http://dx.doi.org/10.1091/mbc.e08-04-0372.

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To better understand the mechanism controlling nonmuscle myosin II (NM-II) assembly in mammalian cells, mutant NM-IIA constructs were created to allow tests in live cells of two widely studied models for filament assembly control. A GFP-NM-IIA construct lacking the RLC binding domain (ΔIQ2) destabilizes the 10S sequestered monomer state and results in a severe defect in recycling monomers during spreading, and from the posterior to the leading edge during polarized migration. A GFP-NM-IIA construct lacking the nonhelical tailpiece (Δtailpiece) is competent for leading edge assembly, but overas

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9

Osagie, Oloruntoba Ismail, Zhigui Li, Shijun Mi, Jennifer T. Aguilan, and Gloria S. Huang. "ARID1A interacts with nonmuscle myosin IIA to regulate cancer cell motility." Journal of Clinical Oncology 37, no. 15_suppl (2019): e17036-e17036. http://dx.doi.org/10.1200/jco.2019.37.15_suppl.e17036.

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e17036 Background: ARID1A (BAF250A), a member of the SWI/SNF chromatin remodeling complex, is one of the most frequently mutated genes in human cancer. Here we report the discovery of a novel protein-protein interaction between ARID1A and the actin-binding motor protein, non-muscle myosin IIA (NM IIA) encoded by the myosin heavy chain 9 ( MYH9). Methods: The ARID1A immunoprecipitated protein complex was separated by gel electrophoresis followed by analysis of the peptide digested gel bands by C18-Reversed Phase chromatography using an Ultimate 3000 RSLCnano System (Thermo Scientific) equipped

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10

Liu, Xiong, Neil Billington, Shi Shu, et al. "Effect of ATP and regulatory light-chain phosphorylation on the polymerization of mammalian nonmuscle myosin II." Proceedings of the National Academy of Sciences 114, no. 32 (2017): E6516—E6525. http://dx.doi.org/10.1073/pnas.1702375114.

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Addition of 1 mM ATP substantially reduces the light scattering of solutions of polymerized unphosphorylated nonmuscle myosin IIs (NM2s), and this is reversed by phosphorylation of the regulatory light chain (RLC). It has been proposed that these changes result from substantial depolymerization of unphosphorylated NM2 filaments to monomers upon addition of ATP, and filament repolymerization upon RLC-phosphorylation. We now show that the differences in myosin monomer concentration of RLC-unphosphorylated and -phosphorylated recombinant mammalian NM2A, NM2B, and NM2C polymerized in the presence

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