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Volumn 5, Issue , 2015, Pages

Phosphorylation of nonmuscle myosin II-A regulatory light chain resists Sendai virus fusion with host cells

Author keywords

[No Author keywords available]

Indexed keywords

BLEBBISTATIN; FUSED HETEROCYCLIC RINGS; MYOSIN IIA; MYOSIN IIB; MYOSIN LIGHT CHAIN; RHO KINASE; SMALL INTERFERING RNA;

EID: 84930216354     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep10395     Document Type: Article
Times cited : (18)

References (52)
  • 1
    • 77954683314 scopus 로고    scopus 로고
    • Entry and fusion of emerging paramyxoviruses
    • Dutch, R. E. Entry and fusion of emerging paramyxoviruses. PLoS Pathog. 6, e1000881 (2010).
    • (2010) PLoS Pathog. , vol.6 , pp. e1000881
    • Dutch, R.E.1
  • 2
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: Lessons from paramyxovirus F
    • Lamb, R. A. & Jardetzky, T. S. Structural basis of viral invasion: lessons from paramyxovirus F. Curr. Opin. Struct. Biol. 17, 427-436 (2007).
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 3
    • 33744734984 scopus 로고    scopus 로고
    • The structural basis of paramyxovirus invasion
    • Russell, C. J. & Luque, L. E. The structural basis of paramyxovirus invasion. Trends Microbiol. 14, 243-246 (2006).
    • (2006) Trends Microbiol. , vol.14 , pp. 243-246
    • Russell, C.J.1    Luque, L.E.2
  • 4
    • 58549102514 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion
    • Bissonnette, M. L., Donald, J. E., DeGrado, W. F., Jardetzky, T. S. & Lamb, R. A. Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion. J. Mol. Biol. 386, 14-36 (2009).
    • (2009) J. Mol. Biol. , vol.386 , pp. 14-36
    • Bissonnette, M.L.1    Donald, J.E.2    Degrado, W.F.3    Jardetzky, T.S.4    Lamb, R.A.5
  • 5
    • 0036891868 scopus 로고    scopus 로고
    • Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion
    • Takimoto, T., Taylor, G. L., Connaris, H. C., Crennell, S. J. & Portner, A. Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion. J. Virol. 76, 13028-13033 (2002).
    • (2002) J. Virol. , vol.76 , pp. 13028-13033
    • Takimoto, T.1    Taylor, G.L.2    Connaris, H.C.3    Crennell, S.J.4    Portner, A.5
  • 6
    • 0026637939 scopus 로고
    • Biological activity of paramyxovirus fusion proteins: Factors infuencing formation of syncytia
    • Horvath, C. M., Paterson, R. G., Shaughnessy, M. A., Wood, R. & Lamb, R. A. Biological activity of paramyxovirus fusion proteins: factors infuencing formation of syncytia. J. Virol. 66, 4564-4569 (1992).
    • (1992) J. Virol. , vol.66 , pp. 4564-4569
    • Horvath, C.M.1    Paterson, R.G.2    Shaughnessy, M.A.3    Wood, R.4    Lamb, R.A.5
  • 7
    • 58149116454 scopus 로고    scopus 로고
    • Dependence of myoblast fusion on a cortical actin wall and nonmuscle myosin IIA
    • Duan, R. & Gallagher, P. J. Dependence of myoblast fusion on a cortical actin wall and nonmuscle myosin IIA. Dev. Biol. 325, 374-385 (2009).
    • (2009) Dev. Biol. , vol.325 , pp. 374-385
    • Duan, R.1    Gallagher, P.J.2
  • 8
    • 44849143151 scopus 로고    scopus 로고
    • Myosin II contributes to fusion pore expansion during exocytosis
    • Neco, P. et al. Myosin II contributes to fusion pore expansion during exocytosis. J. Biol. Chem. 283, 10949-10957 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 10949-10957
    • Neco, P.1
  • 9
    • 34247335100 scopus 로고    scopus 로고
    • Myosin IIA is involved in the endocytosis of CXCR4 induced by SDF-1alpha
    • Rey, M. et al. Myosin IIA is involved in the endocytosis of CXCR4 induced by SDF-1alpha. J. Cell Sci. 120, 1126-1133 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 1126-1133
    • Rey, M.1
  • 10
    • 40849139246 scopus 로고    scopus 로고
    • Inhibition of "self " engulfment through deactivation of myosin-II at the phagocytic synapse between human cells
    • Tsai, R. K. & Discher, D. E. Inhibition of "self " engulfment through deactivation of myosin-II at the phagocytic synapse between human cells. J. Cell Biol. 180, 989-1003 (2008).
    • (2008) J. Cell Biol. , vol.180 , pp. 989-1003
    • Tsai, R.K.1    Discher, D.E.2
  • 11
    • 4444384584 scopus 로고    scopus 로고
    • Modulation of acto-myosin contractility in skeletal muscle myoblasts uncouples growth arrest from diferentiation
    • Dhawan, J. & Helfman, D. M. Modulation of acto-myosin contractility in skeletal muscle myoblasts uncouples growth arrest from diferentiation. J. Cell Sci. 117, 3735-3748 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 3735-3748
    • Dhawan, J.1    Helfman, D.M.2
  • 12
    • 33749389189 scopus 로고    scopus 로고
    • Non-muscle myosins 2A and 2B drive changes in cell morphology that occur as myoblasts align and fuse
    • Swailes, N. T., Colegrave, M., Knight, P. J. & Peckham, M. Non-muscle myosins 2A and 2B drive changes in cell morphology that occur as myoblasts align and fuse. J. Cell Sci. 119, 3561-3570 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 3561-3570
    • Swailes, N.T.1    Colegrave, M.2    Knight, P.J.3    Peckham, M.4
  • 15
    • 84904383731 scopus 로고    scopus 로고
    • Regulation of nonmuscle myosin II during 3-methylcholanthrene induced dediferentiation of C2C12 myotubes
    • Dey, S. K., Saha, S., Das, P., Das, M. R. & Jana, S. S. Regulation of nonmuscle myosin II during 3-methylcholanthrene induced dediferentiation of C2C12 myotubes. Exp. Cell Res. 326, 68-77 (2014).
    • (2014) Exp. Cell Res. , vol.326 , pp. 68-77
    • Dey, S.K.1    Saha, S.2    Das, P.3    Das, M.R.4    Jana, S.S.5
  • 16
    • 84875140647 scopus 로고    scopus 로고
    • The efect of including the C2 insert of nonmuscle myosin II-C on neuritogenesis
    • Saha, S. et al. The efect of including the C2 insert of nonmuscle myosin II-C on neuritogenesis. J. Biol. Chem. 288, 7815-7828 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 7815-7828
    • Saha, S.1
  • 18
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor
    • Straight, A. F. et al. Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor. Science 299, 1743-1747 (2003).
    • (2003) Science , vol.299 , pp. 1743-1747
    • Straight, A.F.1
  • 19
    • 77950826944 scopus 로고    scopus 로고
    • Reciprocal regulation of AKT and MAP kinase dictates virus-host cell fusion
    • Sharma, N. R. et al. Reciprocal regulation of AKT and MAP kinase dictates virus-host cell fusion. J. Virol. 84, 4366-4382 (2010).
    • (2010) J. Virol. , vol.84 , pp. 4366-4382
    • Sharma, N.R.1
  • 20
    • 33646410929 scopus 로고    scopus 로고
    • Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration
    • Betapudi, V., Licate, L. S. & Egelhof, T. T. Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration. Cancer Res. 66, 4725-4733 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 4725-4733
    • Betapudi, V.1    Licate, L.S.2    Egelhof, T.T.3
  • 21
    • 84861683378 scopus 로고    scopus 로고
    • Gene duplication and conversion events shaped three homologous, diferentially expressed myosin regulatory light chain (MLC2) genes
    • Gerrits, L. et al. Gene duplication and conversion events shaped three homologous, diferentially expressed myosin regulatory light chain (MLC2) genes. Eur. J. Cell Biol. 91, 629-639 (2012).
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 629-639
    • Gerrits, L.1
  • 22
    • 2342435249 scopus 로고    scopus 로고
    • The N-terminus of the long MLCK induces a disruption in normal spindle morphology and metaphase arrest
    • Dulyaninova, N. G., Patskovsky, Y. V. & Bresnick, A. R. The N-terminus of the long MLCK induces a disruption in normal spindle morphology and metaphase arrest. J. Cell. Sci. 117, 1481-1493 (2004).
    • (2004) J. Cell. Sci. , vol.117 , pp. 1481-1493
    • Dulyaninova, N.G.1    Patskovsky, Y.V.2    Bresnick, A.R.3
  • 23
    • 79955619444 scopus 로고    scopus 로고
    • Chelerythrine perturbs lamellar actomyosin flaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase
    • Tan, I., Lai, J., Yong, J., Li, S. F. & Leung, T. Chelerythrine perturbs lamellar actomyosin flaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase. FEBS Lett. 585, 1260-1268 (2011).
    • (2011) FEBS Lett. , vol.585 , pp. 1260-1268
    • Tan, I.1    Lai, J.2    Yong, J.3    Li, S.F.4    Leung, T.5
  • 24
    • 84884737749 scopus 로고    scopus 로고
    • Protein kinase C activation decreases peripheral actin network density and increases central nonmuscle myosin II contractility in neuronal growth cones
    • Yang, Q. et al. Protein kinase C activation decreases peripheral actin network density and increases central nonmuscle myosin II contractility in neuronal growth cones. Mol. Biol. Cell 24, 3097-3114 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3097-3114
    • Yang, Q.1
  • 25
    • 3543072944 scopus 로고    scopus 로고
    • Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function
    • Berdeaux, R. L., Diaz, B., Kim, L. & Martin, G. S. Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function. J. Cell Biol. 166, 317-323 (2004).
    • (2004) J. Cell Biol. , vol.166 , pp. 317-323
    • Berdeaux, R.L.1    Diaz, B.2    Kim, L.3    Martin, G.S.4
  • 26
    • 0030957356 scopus 로고    scopus 로고
    • Viral manipulations of the actin cytoskeleton
    • Cudmore, S., Reckmann, I. & Way, M. Viral manipulations of the actin cytoskeleton. Trends Microbiol. 5, 142-148 (1997).
    • (1997) Trends Microbiol. , vol.5 , pp. 142-148
    • Cudmore, S.1    Reckmann, I.2    Way, M.3
  • 27
    • 1842862375 scopus 로고    scopus 로고
    • The role of the cytoskeleton during viral infection
    • Dohner, K. & Sodeik, B. The role of the cytoskeleton during viral infection. Curr Top Microbiol. Immunol. 285, 67-108 (2005).
    • (2005) Curr Top Microbiol. Immunol. , vol.285 , pp. 67-108
    • Dohner, K.1    Sodeik, B.2
  • 28
    • 79956141898 scopus 로고    scopus 로고
    • Subversion of the actin cytoskeleton during viral infection
    • Taylor, M. P., Koyuncu, O. O. & Enquist, L. W. Subversion of the actin cytoskeleton during viral infection. Nat. Rev. Microbiol. 9, 427-439 (2011).
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 427-439
    • Taylor, M.P.1    Koyuncu, O.O.2    Enquist, L.W.3
  • 29
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik, L. V. & Kozlov, M. M. Membrane hemifusion: crossing a chasm in two leaps. Cell 123, 375-382 (2005).
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 30
    • 84855274274 scopus 로고    scopus 로고
    • The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell components
    • Laliberte, J. P., Weisberg, A. S. & Moss, B. The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell components. PLoS Pathog. 7, e1002446 (2011).
    • (2011) PLoS Pathog. , vol.7 , pp. e1002446
    • Laliberte, J.P.1    Weisberg, A.S.2    Moss, B.3
  • 31
    • 77953704441 scopus 로고    scopus 로고
    • The actin cytoskeleton inhibits pore expansion during PIV5 fusion protein-promoted cell-cell fusion
    • Wurth, M. A. et al. The actin cytoskeleton inhibits pore expansion during PIV5 fusion protein-promoted cell-cell fusion. Virology 404, 117-126 (2010).
    • (2010) Virology , vol.404 , pp. 117-126
    • Wurth, M.A.1
  • 32
    • 77956334580 scopus 로고    scopus 로고
    • A spindle-independent cleavage furrow positioning pathway
    • Cabernard, C., Prehoda, K. E. & Doe, C. Q. A spindle-independent cleavage furrow positioning pathway. Nature 467, 91-94 (2010).
    • (2010) Nature , vol.467 , pp. 91-94
    • Cabernard, C.1    Prehoda, K.E.2    Doe, C.Q.3
  • 33
    • 78049391891 scopus 로고    scopus 로고
    • Polarized myosin produces unequal-size daughters during asymmetric cell division
    • Ou, G., Stuurman, N., D'Ambrosio, M. & Vale, R. D. Polarized myosin produces unequal-size daughters during asymmetric cell division. Science 330, 677-680 (2010).
    • (2010) Science , vol.330 , pp. 677-680
    • Ou, G.1    Stuurman, N.2    D'Ambrosio, M.3    Vale, R.D.4
  • 34
    • 84908053868 scopus 로고    scopus 로고
    • Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers
    • Shutova, M. S., Spessott, W. A., Giraudo, C. G. & Svitkina, T. Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers. Curr. Biol. 24, 1958-1968 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 1958-1968
    • Shutova, M.S.1    Spessott, W.A.2    Giraudo, C.G.3    Svitkina, T.4
  • 36
    • 76649092961 scopus 로고    scopus 로고
    • Cytoskeletal coherence requires myosin-IIA contractility
    • Cai, Y. et al. Cytoskeletal coherence requires myosin-IIA contractility. J. Cell Sci. 123, 413-423 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 413-423
    • Cai, Y.1
  • 37
    • 33845993635 scopus 로고    scopus 로고
    • Rho kinase diferentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration
    • Sandquist, J. C., Swenson, K. I., Demali, K. A., Burridge, K. & Means, A. R. Rho kinase diferentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration. J. Biol. Chem. 281, 35873-35883 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 35873-35883
    • Sandquist, J.C.1    Swenson, K.I.2    Demali, K.A.3    Burridge, K.4    Means, A.R.5
  • 38
    • 84859175662 scopus 로고    scopus 로고
    • Membrane fssion is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains
    • Boucrot, E. et al. Membrane fssion is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains. Cell 149, 124-136 (2012).
    • (2012) Cell , vol.149 , pp. 124-136
    • Boucrot, E.1
  • 39
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • Campelo, F., McMahon, H. T. & Kozlov, M. M. The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophys. J. 95, 2325-2339 (2008).
    • (2008) Biophys. J. , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 40
    • 0027211806 scopus 로고
    • Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Sendai virus envelopes with cells
    • Bagai, S., Puri, A., Blumenthal, R. & Sarkar, D. P. Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Sendai virus envelopes with cells. J. Virol. 67, 3312-3318 (1993).
    • (1993) J. Virol. , vol.67 , pp. 3312-3318
    • Bagai, S.1    Puri, A.2    Blumenthal, R.3    Sarkar, D.P.4
  • 41
    • 0016173457 scopus 로고
    • Fusion of intact human erythrocytes and erythrocyte ghosts
    • Peretz, H., Toister, Z., Laster, Y. & Loyter, A. Fusion of intact human erythrocytes and erythrocyte ghosts. J. Cell Biol. 63, 1-11 (1974).
    • (1974) J. Cell Biol. , vol.63 , pp. 1-11
    • Peretz, H.1    Toister, Z.2    Laster, Y.3    Loyter, A.4
  • 42
    • 0001658090 scopus 로고
    • Counts of infuenza virus particles
    • Donald, H. B. & Isaacs, A. Counts of infuenza virus particles. J. Gen. Microbiol. 10, 457-464 (1954).
    • (1954) J. Gen. Microbiol. , vol.10 , pp. 457-464
    • Donald, H.B.1    Isaacs, A.2
  • 43
    • 0023759873 scopus 로고
    • The protein kinase inhibitor staurosporine, like phorbol esters, induces the association of protein kinase C with membranes
    • Wolf, M. & Baggiolini, M. The protein kinase inhibitor staurosporine, like phorbol esters, induces the association of protein kinase C with membranes. Biochemical and Biophysical Research Communications 154, 1273-1279 (1988).
    • (1988) Biochemical and Biophysical Research Communications , vol.154 , pp. 1273-1279
    • Wolf, M.1    Baggiolini, M.2
  • 44
    • 0034652115 scopus 로고    scopus 로고
    • Survival function of ERK1/2 as IL-3-activated, staurosporine-resistant Bcl2 kinases
    • Deng, X., Ruvolo, P., Carr, B. & May, W. S., Jr. Survival function of ERK1/2 as IL-3-activated, staurosporine-resistant Bcl2 kinases. Proc. Natl. Acad. Sci. USA 97, 1578-1583 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1578-1583
    • Deng, X.1    Ruvolo, P.2    Carr, B.3    May, Jr.W.S.4
  • 45
    • 84885120931 scopus 로고    scopus 로고
    • Combination treatments with the PKC inhibitor, enzastaurin, enhance the cytotoxicity of the anti-mesothelin immunotoxin, SS1P
    • Mattoo, A. R., Pastan, I. & Fitzgerald, D. Combination treatments with the PKC inhibitor, enzastaurin, enhance the cytotoxicity of the anti-mesothelin immunotoxin, SS1P. PLoS One 8, e75576 (2013).
    • (2013) PLoS One , vol.8 , pp. e75576
    • Mattoo, A.R.1    Pastan, I.2    Fitzgerald, D.3
  • 46
    • 0033514379 scopus 로고    scopus 로고
    • Dimensional and mechanical dynamics of active and stable edges in motile fbroblasts investigated by using atomic force microscopy
    • Rotsch, C., Jacobson, K. & Radmacher, M. Dimensional and mechanical dynamics of active and stable edges in motile fbroblasts investigated by using atomic force microscopy. Proc. Natl. Acad. Sci. USA 96, 921-926 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 921-926
    • Rotsch, C.1    Jacobson, K.2    Radmacher, M.3
  • 47
    • 80051919561 scopus 로고    scopus 로고
    • LPA(1)-induced migration requires nonmuscle myosin II light chain phosphorylation in breast cancer cells
    • Kim, J. H. & Adelstein, R. S. LPA(1)-induced migration requires nonmuscle myosin II light chain phosphorylation in breast cancer cells. J. Cell Physiol. 226, 2881-2893 (2011).
    • (2011) J. Cell Physiol. , vol.226 , pp. 2881-2893
    • Kim, J.H.1    Adelstein, R.S.2
  • 48
    • 84871997465 scopus 로고    scopus 로고
    • Crawling from sof to stif matrix polarizes the cytoskeleton and phosphoregulates myosin-II heavy chain
    • Raab, M. et al. Crawling from sof to stif matrix polarizes the cytoskeleton and phosphoregulates myosin-II heavy chain. J. Cell Biol. 199, 669-683 (2012).
    • (2012) J. Cell Biol. , vol.199 , pp. 669-683
    • Raab, M.1
  • 49
    • 59649130347 scopus 로고    scopus 로고
    • Non-muscle myosin IIA diferentially regulates intestinal epithelial cell restitution and matrix invasion
    • Babbin, B. A. et al. Non-muscle myosin IIA diferentially regulates intestinal epithelial cell restitution and matrix invasion. Am. J. Pathol. 174, 436-448 (2009).
    • (2009) Am. J. Pathol. , vol.174 , pp. 436-448
    • Babbin, B.A.1
  • 50
    • 78649654888 scopus 로고    scopus 로고
    • Ablation of nonmuscle myosin II-B and II-C reveals a role for nonmuscle myosin II in cardiac myocyte karyokinesis
    • Ma, X. et al. Ablation of nonmuscle myosin II-B and II-C reveals a role for nonmuscle myosin II in cardiac myocyte karyokinesis. Mol. Biol. Cell 21, 3952-3962 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3952-3962
    • Ma, X.1
  • 52
    • 0021673527 scopus 로고
    • Fluorescence method for measuring the kinetics of fusion between biological membranes
    • Hoekstra, D., de Boer, T., Klappe, K. & Wilschut, J. Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry 23, 5675-5681 (1984).
    • (1984) Biochemistry , vol.23 , pp. 5675-5681
    • Hoekstra, D.1    De Boer, T.2    Klappe, K.3    Wilschut, J.4


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