메뉴 건너뛰기




Volumn 23, Issue 9, 2012, Pages 1675-1687

Myosin-X functions in polarized epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN; MYOSIN X; UNCLASSIFIED DRUG;

EID: 84860378478     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E11-04-0358     Document Type: Article
Times cited : (31)

References (87)
  • 2
    • 0030464473 scopus 로고    scopus 로고
    • Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion
    • DOI 10.1083/jcb.135.6.1899
    • Adams CL, Nelson WJ, Smith SJ (1996). Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion. J Cell Biol 135, 1899-1911. (Pubitemid 27036450)
    • (1996) Journal of Cell Biology , vol.135 , Issue.6 II , pp. 1899-1911
    • Adams, C.L.1    Nelson, W.J.2    Smith, S.J.3
  • 3
    • 77949407751 scopus 로고    scopus 로고
    • The motor protein myosin-X transports VE-cadherin along filopodia to allow the formation of early endothelial cell-cell contacts
    • Almagro S et al. (2010). The motor protein myosin-X transports VE-cadherin along filopodia to allow the formation of early endothelial cell-cell contacts. Mol Cell Biol 30, 1703-1717.
    • (2010) Mol Cell Biol , vol.30 , pp. 1703-1717
    • Almagro, S.1
  • 6
    • 34247148026 scopus 로고    scopus 로고
    • Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells
    • DOI 10.1083/jcb.200608126
    • Au JS, Puri C, Ihrke G, Kendrick-Jones J, Buss F (2007). Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells. J Cell Biol 177, 103-114. (Pubitemid 46588405)
    • (2007) Journal of Cell Biology , vol.177 , Issue.1 , pp. 103-114
    • Au, J.S.-Y.1    Puri, C.2    Ihrke, G.3    Kendrick-Jones, J.4    Buss, F.5
  • 7
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda MS, Whitney JA, Flores C, Gonzalez S, Cereijido M, Matter K (1996). Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J Cell Biol 134, 1031-1049. (Pubitemid 26278226)
    • (1996) Journal of Cell Biology , vol.134 , Issue.4 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 8
    • 34047250470 scopus 로고    scopus 로고
    • Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10
    • DOI 10.1074/jbc.M607174200
    • Bennett RD, Mauer AS, Strehler EE (2007). Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10. J Biol Chem 282, 3205-3212. (Pubitemid 47084364)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 3205-3212
    • Bennett, R.D.1    Mauer, A.S.2    Strehler, E.E.3
  • 9
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • DOI 10.1038/ncb762
    • Berg JS, Cheney RE (2002). Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat Cell Biol 4, 246-250. (Pubitemid 34218199)
    • (2002) Nature Cell Biology , vol.4 , Issue.3 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 10
    • 0033766768 scopus 로고    scopus 로고
    • Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin
    • Berg JS, Derfler BH, Pennisi CM, Corey DP, Cheney RE (2000). Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin. J Cell Sci 113, 3439-3451.
    • (2000) J Cell Sci , vol.113 , pp. 3439-3451
    • Berg, J.S.1    Derfler, B.H.2    Pennisi, C.M.3    Corey, D.P.4    Cheney, R.E.5
  • 12
    • 0021991243 scopus 로고
    • Cell-adhesion molecule uvomorulin is localized in the intermediate junctions of adult intestinal epithelial cells
    • DOI 10.1083/jcb.100.1.327
    • Boller K, Vestweber D, Kemler R (1985). Cell-adhesion molecule uvomorulin is localized in the intermediate junctions of adult intestinal epithelial cells. J Cell Biol 100, 327-332. (Pubitemid 15151911)
    • (1985) Journal of Cell Biology , vol.100 , Issue.1 , pp. 327-332
    • Boller, K.1    Vestweber, D.2    Kemler, R.3
  • 13
    • 0017137019 scopus 로고
    • Proteins of the kidney microvillus membrane. Identification of subunits after sodium dodecylsulphate/polyacrylamidegel electrophoresis
    • Booth AG, Kenny AJ (1976). Proteins of the kidney microvillus membrane. Identification of subunits after sodium dodecylsulphate/polyacrylamidegel electrophoresis. Biochem J 159, 395-407.
    • (1976) Biochem J , vol.159 , pp. 395-407
    • Booth, A.G.1    Kenny, A.J.2
  • 14
    • 77951054905 scopus 로고    scopus 로고
    • An unconventional myosin required for cell polarization and chemotaxis
    • Breshears LM, Wessels D, Soll DR, Titus MA (2010). An unconventional myosin required for cell polarization and chemotaxis. Proc Natl Acad Sci USA 107, 6918-6923.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 6918-6923
    • Breshears, L.M.1    Wessels, D.2    Soll, D.R.3    Titus, M.A.4
  • 15
    • 3242705077 scopus 로고    scopus 로고
    • RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin
    • DOI 10.1152/ajpcell.00087.2004
    • Bruewer M, Hopkins AM, Hobert ME, Nusrat A, Madara JL (2004). RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin. Am J Physiol Cell Physiol 287, C327-C335. (Pubitemid 38955223)
    • (2004) American Journal of Physiology - Cell Physiology , vol.287 , Issue.2
    • Bruewer, M.1    Hopkins, A.M.2    Hobert, M.E.3    Nusrat, A.4    Madara, J.L.5
  • 16
    • 33846065117 scopus 로고    scopus 로고
    • Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells
    • DOI 10.1091/mbc.E06-05-0471
    • Capaldo CT, Macara IG (2007). Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells. Mol Biol Cell 18, 189-200. (Pubitemid 46066720)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.1 , pp. 189-200
    • Capaldo, C.T.1    Macara, I.G.2
  • 17
    • 0017891781 scopus 로고
    • Polarized monolayers formed by epithelial cells on a permeable and translucent support
    • Cereijido M, Robbins ES, Dolan WJ, Rotunno CA, Sabatini DD (1978). Polarized monolayers formed by epithelial cells on a permeable and translucent support. J Cell Biol 77, 853-880. (Pubitemid 8347746)
    • (1978) Journal of Cell Biology , vol.77 , Issue.3 , pp. 853-880
    • Cereijido, M.1    Robbins, E.S.2    Dolan, W.J.3
  • 18
    • 0017855840 scopus 로고
    • Morphological factors influencing transepithelial permeability: A model for the resistance of the zonula occludens
    • Claude P (1978). Morphological factors influencing transepithelial permeability: a model for the resistance of the zonula occludens. J Membr Biol 39, 219-232.
    • (1978) J Membr Biol , vol.39 , pp. 219-232
    • Claude, P.1
  • 20
    • 69949106214 scopus 로고    scopus 로고
    • Cadherin adhesion receptors orient the mitotic spindle during symmetric cell division in mammalian epithelia
    • den Elzen N, Buttery CV, Maddugoda MP, Ren G, Yap AS (2009). Cadherin adhesion receptors orient the mitotic spindle during symmetric cell division in mammalian epithelia. Mol Biol Cell 20, 3740-3750.
    • (2009) Mol Biol Cell , vol.20 , pp. 3740-3750
    • Den Elzen, N.1    Buttery, C.V.2    Maddugoda, M.P.3    Ren, G.4    Yap, A.S.5
  • 21
    • 84863116784 scopus 로고    scopus 로고
    • Zonula occludens (ZO)-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia
    • Fanning AS, Van Itallie C, Anderson JM (2012). Zonula occludens (ZO)-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia. Mol Biol Cell 23, 577-590.
    • (2012) Mol Biol Cell , vol.23 , pp. 577-590
    • Fanning, A.S.1    Van Itallie, C.2    Anderson, J.M.3
  • 24
    • 0022569860 scopus 로고
    • A functional assay for proteins involved in establishing and epithelial occluding barrier: Identification of a uvomorulin-like polypeptide
    • Gumbiner B, Simons K (1986). A functional assay for proteins involved in establishing an epithelial occluding barrier: identification of a uvomorulinlike polypeptide. J Cell Biol 102, 457-468. (Pubitemid 16140806)
    • (1986) Journal of Cell Biology , vol.102 , Issue.2 , pp. 457-468
    • Gumbiner, B.1    Simons, K.2
  • 25
    • 0023071937 scopus 로고
    • The role of uvomorulin in the formation of epithelial occluding junctions
    • Gumbiner B, Simons K (1987). The role of uvomorulin in the formation of epithelial occluding junctions. Ciba Found Symp 125, 168-186.
    • (1987) Ciba Found Symp , vol.125 , pp. 168-186
    • Gumbiner, B.1    Simons, K.2
  • 27
    • 77953878405 scopus 로고    scopus 로고
    • Adherens junctions: From molecules to morphogenesis
    • Harris TJ, Tepass U (2010). Adherens junctions: from molecules to morphogenesis. Nat Rev Mol Cell Biol 11, 502-514.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 502-514
    • Harris, T.J.1    Tepass, U.2
  • 28
    • 39849100440 scopus 로고    scopus 로고
    • Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton
    • DOI 10.1016/j.bbamem.2007.07.012, PII S0005273607002714
    • Hartsock A, Nelson WJ (2008). Adherens and tight junctions: structure, function and connections to the actin cytoskeleton. Biochim Biophys Acta 1778, 660-669. (Pubitemid 351317795)
    • (2008) Biochimica et Biophysica Acta - Biomembranes , vol.1778 , Issue.3 , pp. 660-669
    • Hartsock, A.1    Nelson, W.J.2
  • 29
    • 0019859146 scopus 로고
    • Quick-freeze, deep etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells
    • Hirokawa N, Heuser JE (1981). Quick-freeze, deep-etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells. J Cell Biol 91, 399-409. (Pubitemid 12215627)
    • (1981) Journal of Cell Biology , vol.91 , Issue.2 I , pp. 399-409
    • Hirokawa, N.1    Heuser, J.E.2
  • 30
    • 0020966680 scopus 로고
    • Mechanism of brush border contractility studied by the quick-freeze, deep-etch method
    • Hirokawa N, Keller TC, III, Chasan R, Mooseker MS (1983). Mechanism of brush border contractility studied by the quick-freeze, deep-etch method. J Cell Biol 96, 1325-1336. (Pubitemid 13029637)
    • (1983) Journal of Cell Biology , vol.96 , Issue.5 , pp. 1325-1336
    • Hirokawa, N.1    Keller III, T.C.S.2    Chasan, R.3    Mooseker, M.S.4
  • 31
    • 0020352825 scopus 로고
    • Interactions between actin filaments and between actin filaments and membranes in quick-frozen and deeply etched hair cells of the chick ear
    • DOI 10.1083/jcb.95.1.249
    • Hirokawa N, Tilney LG (1982). Interactions between actin filaments and between actin filaments and membranes in quick-frozen and deeply etched hair cells of the chick ear. J Cell Biol 95, 249-261. (Pubitemid 13197095)
    • (1982) Journal of Cell Biology , vol.95 , Issue.1 , pp. 249-261
    • Hirokawa, N.1    Tilney, L.G.2
  • 32
    • 52049116495 scopus 로고    scopus 로고
    • Actin motors that drive formation and disassembly of epithelial apical junctions
    • Ivanov AI (2008). Actin motors that drive formation and disassembly of epithelial apical junctions. Front Biosci 13, 6662-6681.
    • (2008) Front Biosci , vol.13 , pp. 6662-6681
    • Ivanov, A.I.1
  • 33
    • 39849103291 scopus 로고    scopus 로고
    • A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions
    • Ivanov AI, Bachar M, Babbin BA, Adelstein RS, Nusrat A, Parkos CA (2007). A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions. PLoS One 2, e658.
    • (2007) PLoS One , vol.2
    • Ivanov, A.I.1    Bachar, M.2    Babbin, B.A.3    Adelstein, R.S.4    Nusrat, A.5    Parkos, C.A.6
  • 35
    • 2542424590 scopus 로고    scopus 로고
    • Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex
    • DOI 10.1091/mbc.E04-02-0163
    • Ivanov AI, McCall IC, Parkos CA, Nusrat A (2004). Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex. Mol Biol Cell 15, 2639-2651. (Pubitemid 38691854)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.6 , pp. 2639-2651
    • Ivanov, A.I.1    McCall, I.C.2    Parkos, C.A.3    Nusrat, A.4
  • 36
    • 58149191544 scopus 로고    scopus 로고
    • Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis
    • Jaffe AB, Kaji N, Durgan J, Hall A (2008). Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis. J Cell Biol 183, 625-633.
    • (2008) J Cell Biol , vol.183 , pp. 625-633
    • Jaffe, A.B.1    Kaji, N.2    Durgan, J.3    Hall, A.4
  • 37
    • 0001600881 scopus 로고
    • Morphology of the loop of Henle, distal tubule, and collecting duct
    • Handbook of Physiology, ed. E. E. Windhager, New York: Oxford University Press
    • Kaissling B, Kriz W (1992). Morphology of the loop of Henle, distal tubule, and collecting duct. In: Renal Physiology, Vol. 1, Handbook of Physiology, ed. E. E. Windhager, New York: Oxford University Press, 109-168.
    • (1992) Renal Physiology , vol.1 , pp. 109-168
    • Kaissling, B.1    Kriz, W.2
  • 38
    • 84856777960 scopus 로고    scopus 로고
    • Myosin-X: A MyTH-FERM myosin at the tips of filopodia
    • Kerber ML, Cheney RE (2011). Myosin-X: a MyTH-FERM myosin at the tips of filopodia. J Cell Sci 124, 3733-3741.
    • (2011) J Cell Sci , vol.124 , pp. 3733-3741
    • Kerber, M.L.1    Cheney, R.E.2
  • 40
    • 17644397906 scopus 로고    scopus 로고
    • Mechanism of action of myosin X, a membrane-associated molecular motor
    • DOI 10.1074/jbc.M500616200
    • Kovacs M, Wang F, Sellers JR (2005). Mechanism of action of myosin X, a membrane-associated molecular motor. J Biol Chem 280, 15071-15083. (Pubitemid 40562861)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15071-15083
    • Kovacs, M.1    Wang, F.2    Sellers, J.R.3
  • 41
    • 0036675536 scopus 로고    scopus 로고
    • Tube morphogenesis
    • DOI 10.1016/S0962-8924(02)02332-2, PII S0962892402023322
    • Krasnow MA, Nelson WJ (2002). Tube morphogenesis. Trends Cell Biol 12, 351. (Pubitemid 35015137)
    • (2002) Trends in Cell Biology , vol.12 , Issue.8 , pp. 351
    • Krasnow, M.A.1    Nelson, W.J.2
  • 44
    • 81755184378 scopus 로고    scopus 로고
    • Structural basis of the myosin X PH1(N)-PH2-PH1(C) tandem as a specific and acute cellular PI(3,4,5)P(3) sensor
    • Lu Q, Yu J, Yan J, Wei Z, Zhang M (2011). Structural basis of the myosin X PH1(N)-PH2-PH1(C) tandem as a specific and acute cellular PI(3,4,5)P(3) sensor. Mol Biol Cell 22, 4268-4278.
    • (2011) Mol Biol Cell , vol.22 , pp. 4268-4278
    • Lu, Q.1    Yu, J.2    Yan, J.3    Wei, Z.4    Zhang, M.5
  • 45
    • 0031943571 scopus 로고    scopus 로고
    • Regulation of the movement of solutes across tight junctions
    • Madara JL (1998). Regulation of the movement of solutes across tight junctions. Annu Rev Physiol 60, 143-159.
    • (1998) Annu Rev Physiol , vol.60 , pp. 143-159
    • Madara, J.L.1
  • 46
    • 34547591456 scopus 로고    scopus 로고
    • Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell-cell contacts in mammalian epithelial cells
    • DOI 10.1083/jcb.200612042
    • Maddugoda MP, Crampton MS, Shewan AM, Yap AS (2007). Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell-cell contacts in mammalian epithelial cells. J Cell Biol 178, 529-540. (Pubitemid 47196159)
    • (2007) Journal of Cell Biology , vol.178 , Issue.3 , pp. 529-540
    • Maddugoda, M.P.1    Crampton, M.S.2    Shewan, A.M.3    Yap, A.S.4
  • 47
    • 79952814622 scopus 로고    scopus 로고
    • Hepatocyte growth factor acutely perturbs actin filament anchorage at the epithelial zonula adherens
    • Mangold S, Wu SK, Norwood SJ, Collins BM, Hamilton NA, Thorn P, Yap AS (2011). Hepatocyte growth factor acutely perturbs actin filament anchorage at the epithelial zonula adherens. Curr Biol 21, 503-507.
    • (2011) Curr Biol , vol.21 , pp. 503-507
    • Mangold, S.1    Wu, S.K.2    Norwood, S.J.3    Collins, B.M.4    Hamilton, N.A.5    Thorn, P.6    Yap, A.S.7
  • 48
    • 78651493412 scopus 로고    scopus 로고
    • Planar polarization of the atypical myosin Dachs orients cell divisions in Drosophila
    • Mao Y, Tournier AL, Bates PA, Gale JE, Tapon N, Thompson BJ (2011). Planar polarization of the atypical myosin Dachs orients cell divisions in Drosophila. Genes Dev 25, 131-136.
    • (2011) Genes Dev , vol.25 , pp. 131-136
    • Mao, Y.1    Tournier, A.L.2    Bates, P.A.3    Gale, J.E.4    Tapon, N.5    Thompson, B.J.6
  • 49
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-Mediated Apical Segregation of Phosphoinositides Controls Epithelial Morphogenesis through Cdc42
    • DOI 10.1016/j.cell.2006.11.051, PII S0092867407000050
    • Martin-Belmonte F, Gassama A, Datta A, Yu W, Rescher U, Gerke V, Mostov K (2007). PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128, 383-397. (Pubitemid 46123512)
    • (2007) Cell , vol.128 , Issue.2 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5    Gerke, V.6    Mostov, K.7
  • 50
    • 2442595175 scopus 로고    scopus 로고
    • The Spatial and Temporal Dynamics of Pleckstrin Homology Domain Binding at the Plasma Membrane Measured by Imaging Single Molecules in Live Mouse Myoblasts
    • DOI 10.1074/jbc.M312140200
    • Mashanov GI, Tacon D, Peckham M, Molloy JE (2004). The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts. J Biol Chem 279, 15274-15280. (Pubitemid 38618924)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 15274-15280
    • Mashanov, G.I.1    Tacon, D.2    Peckham, M.3    Molloy, J.E.4
  • 53
    • 33745269374 scopus 로고    scopus 로고
    • Zonula occludens-1 function in the assembly of tight junctions in Madin-Darby canine kidney epithelial cells
    • DOI 10.1091/mbc.E05-07-0650
    • McNeil E, Capaldo CT, Macara IG (2006). Zonula occludens-1 function in the assembly of tight junctions in Madin-Darby canine kidney epithelial cells. Mol Biol Cell 17, 1922-1932. (Pubitemid 44011607)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1922-1932
    • McNeil, E.1    Capaldo, C.T.2    Macara, I.G.3
  • 54
    • 52949112224 scopus 로고    scopus 로고
    • MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity
    • Muller T et al. (2008). MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity. Nat Genet 40, 1163-1165.
    • (2008) Nat Genet , vol.40 , pp. 1163-1165
    • Muller, T.1
  • 57
    • 0037459077 scopus 로고    scopus 로고
    • Sticky business: Orchestrating cellular signals at adherens junctions
    • DOI 10.1016/S0092-8674(03)00108-9
    • Perez-Moreno M, Jamora C, Fuchs E (2003). Sticky business: orchestrating cellular signals at adherens junctions. Cell 112, 535-548. (Pubitemid 36263085)
    • (2003) Cell , vol.112 , Issue.4 , pp. 535-548
    • Perez-Moreno, M.1    Jamora, C.2    Fuchs, E.3
  • 58
    • 38049037417 scopus 로고    scopus 로고
    • Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors
    • Pi X, Ren R, Kelley R, Zhang C, Moser M, Bohil AB, Divito M, Cheney RE, Patterson C (2007). Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors. J Cell Biol 179, 1569-1582.
    • (2007) J Cell Biol , vol.179 , pp. 1569-1582
    • Pi, X.1    Ren, R.2    Kelley, R.3    Zhang, C.4    Moser, M.5    Bohil, A.B.6    Divito, M.7    Cheney, R.E.8    Patterson, C.9
  • 59
    • 77957874785 scopus 로고    scopus 로고
    • PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia formation
    • Plantard L, Arjonen A, Lock JG, Nurani G, Ivaska J, Stromblad S (2010). PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia formation. J Cell Sci 123, 3525-3534.
    • (2010) J Cell Sci , vol.123 , pp. 3525-3534
    • Plantard, L.1    Arjonen, A.2    Lock, J.G.3    Nurani, G.4    Ivaska, J.5    Stromblad, S.6
  • 60
    • 77952396762 scopus 로고    scopus 로고
    • Tuba, a Cdc42 GEF, is required for polarized spindle orientation during epithelial cyst formation
    • Qin Y, Meisen WH, Hao Y, Macara IG (2010). Tuba, a Cdc42 GEF, is required for polarized spindle orientation during epithelial cyst formation. J Cell Biol 189, 661-669.
    • (2010) J Cell Biol , vol.189 , pp. 661-669
    • Qin, Y.1    Meisen, W.H.2    Hao, Y.3    Macara, I.G.4
  • 64
    • 0028218489 scopus 로고
    • Integrin expression and localization in normal MDCK cells and transformed MDCK cells lacking apical polarity
    • Schoenenberger CA, Zuk A, Zinkl GM, Kendall D, Matlin KS (1994). Integrin expression and localization in normal MDCK cells and transformed MDCK cells lacking apical polarity. J Cell Sci 107, 527-541. (Pubitemid 24072884)
    • (1994) Journal of Cell Science , vol.107 , Issue.2 , pp. 527-541
    • Schoenenberger, C.-A.1    Zuk, A.2    Zinkl, G.M.3    Kendall, D.4    Matlin, K.S.5
  • 65
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
    • Schoumacher M, Goldman RD, Louvard D, Vignjevic DM (2010). Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J Cell Biol 189, 541-556.
    • (2010) J Cell Biol , vol.189 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 68
    • 26244455734 scopus 로고    scopus 로고
    • Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts
    • DOI 10.1091/mbc.E05-04-0330
    • Shewan AM, Maddugoda M, Kraemer A, Stehbens SJ, Verma S, Kovacs EM, Yap AS (2005). Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts. Mol Biol Cell 16, 4531-4542. (Pubitemid 41416439)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4531-4542
    • Shewan, A.M.1    Maddugoda, M.2    Kraemer, A.3    Stehbens, S.J.4    Verma, S.5    Kovacs, E.M.6    Yap, A.S.7
  • 69
    • 14744275517 scopus 로고    scopus 로고
    • PATJ regulates tight junction formation and polarity in mammalian epithelial cells
    • DOI 10.1083/jcb.200408064
    • Shin K, Straight S, Margolis B (2005). PATJ regulates tight junction formation and polarity in mammalian epithelial cells. J Cell Biol 168, 705-711. (Pubitemid 40328155)
    • (2005) Journal of Cell Biology , vol.168 , Issue.5 , pp. 705-711
    • Shin, K.1    Straight, S.2    Margolis, B.3
  • 71
    • 25844435342 scopus 로고    scopus 로고
    • Myosin-X: A molecular motor at the cell's fingertips
    • DOI 10.1016/j.tcb.2005.08.006, PII S0962892405002047
    • Sousa AD, Cheney RE (2005). Myosin-X: a molecular motor at the cell's fingertips. Trends Cell Biol 15, 533-539. (Pubitemid 41396435)
    • (2005) Trends in Cell Biology , vol.15 , Issue.10 , pp. 533-539
    • Sousa, A.D.1    Cheney, R.E.2
  • 72
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (Zonula Occludens) in a variety of epithelia
    • DOI 10.1083/jcb.103.3.755
    • Stevenson BR, Siliciano JD, Mooseker MS, Goodenough DA (1986). Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J Cell Biol 103, 755-766. (Pubitemid 17177325)
    • (1986) Journal of Cell Biology , vol.103 , Issue.3 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3
  • 74
    • 35548932103 scopus 로고    scopus 로고
    • The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation
    • DOI 10.1083/jcb.200703178
    • Tokuo H, Mabuchi K, Ikebe M (2007). The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation. J Cell Biol 179, 229-238. (Pubitemid 350004887)
    • (2007) Journal of Cell Biology , vol.179 , Issue.2 , pp. 229-238
    • Tokuo, H.1    Mabuchi, K.2    Ikebe, M.3
  • 75
    • 33947596005 scopus 로고    scopus 로고
    • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner
    • DOI 10.1038/sj.emboj.7601599, PII 7601599
    • Toyoshima F, Nishida E (2007). Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner. EMBO J 26, 1487-1498. (Pubitemid 46480928)
    • (2007) EMBO Journal , vol.26 , Issue.6 , pp. 1487-1498
    • Toyoshima, F.1    Nishida, E.2
  • 78
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie CM, Anderson JM (2006). Claudins and epithelial paracellular transport. Annu Rev Physiol 68, 403-429.
    • (2006) Annu Rev Physiol , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 79
    • 70349317350 scopus 로고    scopus 로고
    • ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton
    • Van Itallie CM, Fanning AS, Bridges A, Anderson JM (2009). ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton. Mol Biol Cell 20, 3930-3940.
    • (2009) Mol Biol Cell , vol.20 , pp. 3930-3940
    • Van Itallie, C.M.1    Fanning, A.S.2    Bridges, A.3    Anderson, J.M.4
  • 80
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell- cell adhesion
    • Vasioukhin V, Bauer C, Yin M, Fuchs E (2000). Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell 100, 209-219. (Pubitemid 30064909)
    • (2000) Cell , vol.100 , Issue.2 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 81
    • 77953509417 scopus 로고    scopus 로고
    • Myosin-X induces filopodia by multiple elongation mechanism
    • Watanabe TM, Tokuo H, Gonda K, Higuchi H, Ikebe M (2010). Myosin-X induces filopodia by multiple elongation mechanism. J Biol Chem 285, 19605-19614.
    • (2010) J Biol Chem , vol.285 , pp. 19605-19614
    • Watanabe, T.M.1    Tokuo, H.2    Gonda, K.3    Higuchi, H.4    Ikebe, M.5
  • 82
    • 4644326930 scopus 로고    scopus 로고
    • A microtubule-binding myosin required for nuclear anchoring and spindle assembly
    • DOI 10.1038/nature02834
    • Weber KL, Sokac AM, Berg JS, Cheney RE, Bement WM (2004). A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 431, 325-329. (Pubitemid 39265669)
    • (2004) Nature , vol.431 , Issue.7006 , pp. 325-329
    • Weber, K.L.1    Sokac, A.M.2    Berg, J.S.3    Cheney, R.E.4    Bement, W.M.5
  • 83
    • 79952761581 scopus 로고    scopus 로고
    • Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain
    • Wei Z, Yan J, Lu Q, Pan L, Zhang M (2011). Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain. Proc Natl Acad Sci USA 108, 3572-3577.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3572-3577
    • Wei, Z.1    Yan, J.2    Lu, Q.3    Pan, L.4    Zhang, M.5
  • 84
    • 47549089279 scopus 로고    scopus 로고
    • Myosin-10 and actin filaments are essential for mitotic spindle function
    • DOI 10.1083/jcb.200804062
    • Woolner S, O'Brien LL, Wiese C, Bement WM (2008). Myosin-10 and actin filaments are essential for mitotic spindle function. J Cell Biol 182, 77-88. (Pubitemid 352008623)
    • (2008) Journal of Cell Biology , vol.182 , Issue.1 , pp. 77-88
    • Woolner, S.1    O'Brien, L.L.2    Wiese, C.3    Bement, W.M.4
  • 85
    • 0038670331 scopus 로고    scopus 로고
    • Possible involvement of myosin-X in intercellular adhesion: Importance of serial pleckstrin homology regions for intracellular localization
    • DOI 10.1034/j.1600-0854.2004.00688.x
    • Yonezawa S, Yoshizaki N, Sano M, Hanai A, Masaki S, Takizawa T, Kageyama T, Moriyama A (2003). Possible involvement of myosin-X in intercellular adhesion: importance of serial pleckstrin homology regions for intracellular localization. Dev Growth Differ 45, 175-185. (Pubitemid 36566888)
    • (2003) Development Growth and Differentiation , vol.45 , Issue.2 , pp. 175-185
    • Yonezawa, S.1    Yoshizaki, N.2    Sano, M.3    Hanai, A.4    Masaki, S.5    Takizawa, T.6    Kageyama, T.7    Moriyama, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.