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

Author: Grafiati

Published: 7 September 2023

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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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11

Halder, Debdatta, Shekhar Saha, Raman K. Singh, et al. "Nonmuscle myosin IIA and IIB differentially modulate migration and alter gene expression in primary mouse tumorigenic cells." Molecular Biology of the Cell 30, no. 12 (2019): 1463–76. http://dx.doi.org/10.1091/mbc.e18-12-0790.

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Though many cancers are known to show up-regulation of nonmuscle myosin (NM) IIA and IIB, the mechanism by which NMIIs aid in cancer development remains unexplored. Here we demonstrate that tumor-generating, fibroblast-like cells isolated from 3-methylcholanthrene (3MC)-induced murine tumor exhibit distinct phospho-dependent localization of NMIIA and NMIIB at the perinuclear area and tip of the filopodia and affect cell migration differentially. While NMIIA-KD affects protrusion dynamics and increases cell directionality, NMIIB-KD lowers migration speed and increases filopodial branching. Stra

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12

Du, Min, Guozheng Wang, Igor L. Barsukov, Stephane R. Gross, Richard Smith, and Philip S. Rudland. "Direct interaction of metastasis-inducing S100P protein with tubulin causes enhanced cell migration without changes in cell adhesion." Biochemical Journal 477, no. 6 (2020): 1159–78. http://dx.doi.org/10.1042/bcj20190644.

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Overexpression of S100P promotes breast cancer metastasis in animals and elevated levels in primary breast cancers are associated with poor patient outcomes. S100P can differentially interact with nonmuscle myosin (NM) isoforms (IIA &gt; IIC &gt; IIB) leading to the redistribution of actomyosin filaments to enhance cell migration. Using COS-7 cells which do not naturally express NMIIA, S100P is now shown to interact directly with α,β-tubulin in vitro and in vivo with an equilibrium Kd of 2–3 × 10−7 M. The overexpressed S100P is located mainly in nuclei and microtubule organising centre

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13

Chen, Xin, Yun-Qian Gao, Yan-Yan Zheng, et al. "The intragenic microRNA miR199A1 in the dynamin 2 gene contributes to the pathology of X-linked centronuclear myopathy." Journal of Biological Chemistry 295, no. 26 (2020): 8656–67. http://dx.doi.org/10.1074/jbc.ra119.010839.

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Mutations in the myotubularin 1 (MTM1) gene can cause the fatal disease X-linked centronuclear myopathy (XLCNM), but the underlying mechanism is incompletely understood. In this report, using an Mtm1−/y disease model, we found that expression of the intragenic microRNA miR-199a-1 is up-regulated along with that of its host gene, dynamin 2 (Dnm2), in XLCNM skeletal muscle. To assess the role of miR-199a-1 in XLCNM, we crossed miR-199a-1−/− with Mtm1−/y mice and found that the resultant miR-199a-1-Mtm1 double-knockout mice display markers of improved health, as evidenced by lifespans prolonged b

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14

Weißenbruch, Kai, Justin Grewe, Marc Hippler, et al. "Distinct roles of nonmuscle myosin II isoforms for establishing tension and elasticity during cell morphodynamics." eLife 10 (August 10, 2021). http://dx.doi.org/10.7554/elife.71888.

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Nonmuscle myosin II (NM II) is an integral part of essential cellular processes, including adhesion and migration. Mammalian cells express up to three isoforms termed NM IIA, B, and C. We used U2OS cells to create CRISPR/Cas9-based knockouts of all three isoforms and analyzed the phenotypes on homogenously coated surfaces, in collagen gels, and on micropatterned substrates. In contrast to homogenously coated surfaces, a structured environment supports a cellular phenotype with invaginated actin arcs even in the absence of NM IIA-induced contractility. A quantitative shape analysis of cells on

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15

Sanger, Joseph W., Jushuo Wang, Jennifer White, and Jean M. Sanger. "Distribution and dynamics of nonmuscle myosins IIs in cardiac and in skeletal muscle cells." FASEB Journal 24, S1 (2010). http://dx.doi.org/10.1096/fasebj.24.1_supplement.180.7.

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16

Li, Xiaofei, Callie McLain, Michael S. Samuel, Michael F. Olson та Glenn L. Radice. "Actomyosin-mediated cellular tension promotes Yap nuclear translocation and myocardial proliferation through α5 integrin signaling". Development, 9 січня 2023. http://dx.doi.org/10.1242/dev.201013.

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The cardiomyocyte phenotypic switch from a proliferative to terminally differentiated state results in the loss of regenerative potential of the mammalian heart shortly after birth. Nonmuscle myosin IIB (NM IIB)-mediated actomyosin contractility regulates cardiomyocyte cytokinesis in the embryonic heart, and NM IIB levels decline after birth suggesting a role for cellular tension in the regulation of cardiomyocyte cell cycle activity in the postnatal heart. To investigate the role of actomyosin contractility in cardiomyocyte cell cycle arrest, we conditionally-activated ROCK2 kinase domain (RO

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17

Liu, Yingqi, Rui Li, Xin-xin Chen, et al. "Nonmuscle Myosin Heavy Chain IIA Recognizes Sialic Acids on Sialylated RNA Viruses To Suppress Proinflammatory Responses via the DAP12-Syk Pathway." mBio 10, no. 3 (2019). http://dx.doi.org/10.1128/mbio.00574-19.

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ABSTRACT Viral infections induce proinflammatory signaling cascades and inflammatory cytokine production, which is precisely regulated for host benefits. In the current study, we unravel a previously unappreciated role of nonmuscle myosin heavy chain IIA (NMHC-IIA) as a negative regulator in inflammatory responses. We identified that cell surface NMHC-IIA recognized sialic acids on sialylated RNA viruses during early infections and interacted with an immune adaptor DNAX activation protein of 12 kDa (DAP12) to recruit downstream spleen tyrosine kinase (Syk), leading to suppressed virus-triggere

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18

Taskinen, Maria Emilia, Elisa Närvä, James R. W. Conway, et al. "MASTL promotes cell contractility and motility through kinase-independent signaling." Journal of Cell Biology 219, no. 6 (2020). http://dx.doi.org/10.1083/jcb.201906204.

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Microtubule-associated serine/threonine-protein kinase-like (MASTL) is a mitosis-accelerating kinase with emerging roles in cancer progression. However, possible cell cycle–independent mechanisms behind its oncogenicity remain ambiguous. Here, we identify MASTL as an activator of cell contractility and MRTF-A/SRF (myocardin-related transcription factor A/serum response factor) signaling. Depletion of MASTL increased cell spreading while reducing contractile actin stress fibers in normal and breast cancer cells and strongly impairing breast cancer cell motility and invasion. Transcriptome and p

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