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Volumn 177, Issue 2, 2010, Pages 512-524

Cytoskeletal regulation of epithelial barrier function during inflammation

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; JUNCTIONAL ADHESION MOLECULE A; MYOSIN II; RHO KINASE; UVOMORULIN;

EID: 77957278004     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.2353/ajpath.2010.100168     Document Type: Review
Times cited : (291)

References (136)
  • 2
    • 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: Adherens and tight junctions: structure, function and connections to the actin cytoskeleton. Biochim Biophys Acta 2008, 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
  • 3
    • 35548932457 scopus 로고    scopus 로고
    • Structure and mechanism of cadherins and catenins in cell-cell contacts
    • Pokutta S, Weis WI: Structure and mechanism of cadherins and catenins in cell-cell contacts. Annu Rev Cell Dev Biol 2007, 23:237-261
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 237-261
    • Pokutta, S.1    Weis, W.I.2
  • 4
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher A: Microfilament structure and function in the cortical cytoskeleton. Annu Rev Cell Biol 1991, 7:337-374
    • (1991) Annu Rev Cell Biol , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 5
    • 0022172245 scopus 로고
    • Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border
    • Mooseker MS: Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border. Annu Rev Cell Biol 1985, 1:209-241
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 209-241
    • Mooseker, M.S.1
  • 6
    • 0020966680 scopus 로고
    • Mechanism of brush border contractility studied by the quick-freeze, deep-etch method
    • Hirokawa N, Keller TC, 3rd, Chasan R, Mooseker MS: Mechanism of brush border contractility studied by the quick-freeze, deep-etch method. J Cell Biol 1983, 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
  • 7
    • 0023176321 scopus 로고
    • Intestinal absorptive cell tight junctions are linked to cytoskeleton
    • Madara JL: Intestinal absorptive cell tight junctions are linked to cytoskeleton. Am J Physiol 1987, 253:C171-C175
    • (1987) Am J Physiol , vol.253
    • Madara, J.L.1
  • 9
    • 0022451875 scopus 로고
    • Effects of cytochalasin D on occluding junctions of intestinal absorptive cells: Further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity
    • Madara JL, Barenberg D, Carlson S: Effects of cytochalasin D on occluding junctions of intestinal absorptive cells: further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity. J Cell Biol 1986, 102:2125-2136
    • (1986) J Cell Biol , vol.102 , pp. 2125-2136
    • Madara, J.L.1    Barenberg, D.2    Carlson, S.3
  • 10
    • 52049116495 scopus 로고    scopus 로고
    • Actin motors that drive formation and disassembly of epithelial apical junctions
    • Ivanov AI: Actin motors that drive formation and disassembly of epithelial apical junctions. Front Biosci 2008, 13:6662-6681
    • (2008) Front Biosci , vol.13 , pp. 6662-6681
    • Ivanov, A.I.1
  • 11
    • 39849084350 scopus 로고    scopus 로고
    • Structural and functional associations of apical junctions with cytoskeleton
    • Miyoshi J, Takai Y: Structural and functional associations of apical junctions with cytoskeleton. Biochim Biophys Acta 2008, 1778:670-691
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 670-691
    • Miyoshi, J.1    Takai, Y.2
  • 12
    • 33750532088 scopus 로고    scopus 로고
    • Recent understanding of IBD pathogenesis: Implications for future therapies
    • DOI 10.1097/01.mib.0000235827.21778.d5, PII 0005472520061100000007
    • Kucharzik T, Maaser C, Lugering A, Kagnoff M, Mayer L, Targan S, Domschke W: Recent understanding of IBD pathogenesis: implications for future therapies. Inflamm Bowel Dis 2006, 12:1068-1083 (Pubitemid 44665477)
    • (2006) Inflammatory Bowel Diseases , vol.12 , Issue.11 , pp. 1068-1082
    • Kucharzik, T.1    Maaser, C.2    Lugering, A.3    Kagnoff, M.4    Mayer, L.5    Targan, S.6    Domschke, W.7
  • 13
    • 70350509805 scopus 로고    scopus 로고
    • Intestinal mucosal barrier function in health and disease
    • Turner JR: Intestinal mucosal barrier function in health and disease. Nat Rev Immunol 2009, 9:799-809
    • (2009) Nat Rev Immunol , vol.9 , pp. 799-809
    • Turner, J.R.1
  • 15
    • 0027217379 scopus 로고
    • Intestinal permeability and the prediction of relapse in Crohn's disease
    • DOI 10.1016/0140-6736(93)90882-H
    • Wyatt J, Vogelsang H, Hubl W, Waldhoer T, Lochs H: Intestinal permeability and the prediction of relapse in Crohn's disease. Lancet 1993, 341:1437-1439 (Pubitemid 23161445)
    • (1993) Lancet , vol.341 , Issue.8858 , pp. 1437-1439
    • Wyatt, J.1    Vogelsang, H.2    Hubl, W.3    Waldhoer, T.4    Lochs, H.5
  • 18
    • 58249085436 scopus 로고    scopus 로고
    • Reducing small intestinal permeability attenuates colitis in the IL10 gene-deficient mouse
    • Arrieta MC, Madsen K, Doyle J, Meddings J: Reducing small intestinal permeability attenuates colitis in the IL10 gene-deficient mouse. Gut 2009, 58:41-48
    • (2009) Gut , vol.58 , pp. 41-48
    • Arrieta, M.C.1    Madsen, K.2    Doyle, J.3    Meddings, J.4
  • 20
    • 67649216750 scopus 로고    scopus 로고
    • Intestinal barrier function: Molecular regulation and disease pathogenesis
    • Groschwitz KR, Hogan SP: Intestinal barrier function: molecular regulation and disease pathogenesis. J Allergy Clin Immunol 2009, 124:3-20
    • (2009) J Allergy Clin Immunol , vol.124 , pp. 3-20
    • Groschwitz, K.R.1    Hogan, S.P.2
  • 21
    • 15244341423 scopus 로고    scopus 로고
    • Epithelial barrier dysfunction: A unifying theme to explain the pathogenesis of multiple organ dysfunction at the cellular level
    • Fink MP, Delude RL: Epithelial barrier dysfunction: a unifying theme to explain the pathogenesis of multiple organ dysfunction at the cellular level. Crit Care Clin 2005, 21:177-196
    • (2005) Crit Care Clin , vol.21 , pp. 177-196
    • Fink, M.P.1    Delude, R.L.2
  • 22
    • 0027169430 scopus 로고
    • The gastrointestinal tract. The "undrained abscess" of multiple organ failure
    • Marshall JC, Christou NV, Meakins JL: The gastrointestinal tract. The "undrained abscess" of multiple organ failure. Ann Surg 1993, 218:111-119
    • (1993) Ann Surg , vol.218 , pp. 111-119
    • Marshall, J.C.1    Christou, N.V.2    Meakins, J.L.3
  • 23
    • 36849031788 scopus 로고    scopus 로고
    • Epithelium dysfunction in asthma
    • Holgate ST: Epithelium dysfunction in asthma. J Allergy Clin Immunol 2007, 120:1233-1244
    • (2007) J Allergy Clin Immunol , vol.120 , pp. 1233-1244
    • Holgate, S.T.1
  • 24
    • 0346888342 scopus 로고    scopus 로고
    • The airway epithelium: Structural and functional properties in health and disease
    • Knight DA, Holgate ST: The airway epithelium: structural and functional properties in health and disease. Respirology 2003, 8:432-446
    • (2003) Respirology , vol.8 , pp. 432-446
    • Knight, D.A.1    Holgate, S.T.2
  • 25
    • 1042291171 scopus 로고    scopus 로고
    • Actin re-distribution in response to hydrogen peroxide in airway epithelial cells
    • Boardman KC, Aryal AM, Miller WM, Waters CM: Actin re-distribution in response to hydrogen peroxide in airway epithelial cells. J Cell Physiol 2004, 199:57-66
    • (2004) J Cell Physiol , vol.199 , pp. 57-66
    • Boardman, K.C.1    Aryal, A.M.2    Miller, W.M.3    Waters, C.M.4
  • 26
    • 0034530216 scopus 로고    scopus 로고
    • Neutrophil recruitment and increased permeability during acute lung injury induced by lipopolysaccharide
    • Chignard M, Balloy V: Neutrophil recruitment and increased permeability during acute lung injury induced by lipopolysaccharide. Am J Physiol Lung Cell Mol Physiol 2000, 279:L1083-L1090
    • (2000) Am J Physiol Lung Cell Mol Physiol , vol.279
    • Chignard, M.1    Balloy, V.2
  • 28
    • 67349132318 scopus 로고    scopus 로고
    • Regulators of endothelial and epithelial barrier integrity and function in acute lung injury
    • Lucas R, Verin AD, Black SM, Catravas JD: Regulators of endothelial and epithelial barrier integrity and function in acute lung injury. Biochem Pharmacol 2009, 77:1763-1772
    • (2009) Biochem Pharmacol , vol.77 , pp. 1763-1772
    • Lucas, R.1    Verin, A.D.2    Black, S.M.3    Catravas, J.D.4
  • 29
    • 67649205370 scopus 로고    scopus 로고
    • Breakdown in epithelial barrier function in patients with asthma: Identification of novel therapeutic approaches
    • Swindle EJ, Collins JE, Davies DE: Breakdown in epithelial barrier function in patients with asthma: identification of novel therapeutic approaches. J Allergy Clin Immunol 2009, 124:23-34
    • (2009) J Allergy Clin Immunol , vol.124 , pp. 23-34
    • Swindle, E.J.1    Collins, J.E.2    Davies, D.E.3
  • 31
    • 63249123919 scopus 로고    scopus 로고
    • Cytokine regulation of tight junctions
    • Capaldo CT, Nusrat A: Cytokine regulation of tight junctions. Biochim Biophys Acta 2009, 1788:864-871
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 864-871
    • Capaldo, C.T.1    Nusrat, A.2
  • 32
    • 66449091744 scopus 로고    scopus 로고
    • GEF-H1 mediates tumor necrosis factor-α-induced Rho activation and myosin phosphorylation: Role in the regulation of tubular paracellular permeability
    • Kakiashvili E, Speight P, Waheed F, Seth R, Lodyga M, Tanimura S, Kohno M, Rotstein OD, Kapus A, Szaszi K: GEF-H1 mediates tumor necrosis factor-α-induced Rho activation and myosin phosphorylation: role in the regulation of tubular paracellular permeability. J Biol Chem 2009, 284:11454-11466
    • (2009) J Biol Chem , vol.284 , pp. 11454-11466
    • Kakiashvili, E.1    Speight, P.2    Waheed, F.3    Seth, R.4    Lodyga, M.5    Tanimura, S.6    Kohno, M.7    Rotstein, O.D.8    Kapus, A.9    Szaszi, K.10
  • 33
    • 0042283930 scopus 로고    scopus 로고
    • Interleukin-1β and barrier function of retinal pigment epithelial cells (ARPE-19): Aberrant expression of junctional complex molecules
    • DOI 10.1167/iovs.02-0867
    • Abe T, Sugano E, Saigo Y, Tamai M: Interleukin-1β and barrier function of retinal pigment epithelial cells (ARPE-19): aberrant expression of junctional complex molecules. Invest Ophthalmol Vis Sci 2003, 44:4097-4104 (Pubitemid 37047987)
    • (2003) Investigative Ophthalmology and Visual Science , vol.44 , Issue.9 , pp. 4097-4104
    • Abe, T.1    Sugano, E.2    Saigo, Y.3    Tamai, M.4
  • 34
    • 34547096543 scopus 로고    scopus 로고
    • Lipopolysaccharide disrupts tight junctions in cholangiocyte monolayers by a c-Src-. TLR4-, and LBP-dependent mechanism
    • Sheth P, Delos Santos N, Seth A, LaRusso NF, Rao RK: Lipopolysaccharide disrupts tight junctions in cholangiocyte monolayers by a c-Src-. TLR4-, and LBP-dependent mechanism, Am J Physiol Gastrointest Liver Physiol 2007, 293:G308-G318
    • (2007) Am J Physiol Gastrointest Liver Physiol , vol.293
    • Sheth, P.1    Delos Santos, N.2    Seth, A.3    LaRusso, N.F.4    Rao, R.K.5
  • 35
    • 63849274215 scopus 로고    scopus 로고
    • Virus interaction with the apical junctional complex
    • Gonzalez-Mariscal L, Garay E, Lechuga S: Virus interaction with the apical junctional complex. Front Biosci 2009, 14:731-768
    • (2009) Front Biosci , vol.14 , pp. 731-768
    • Gonzalez-Mariscal, L.1    Garay, E.2    Lechuga, S.3
  • 36
    • 52049095466 scopus 로고    scopus 로고
    • Mechanisms of intestinal tight junctional disruption during infection
    • O'Hara JR, Buret AG: Mechanisms of intestinal tight junctional disruption during infection. Front Biosci 2008, 13:7008-7021
    • (2008) Front Biosci , vol.13 , pp. 7008-7021
    • O'Hara, J.R.1    Buret, A.G.2
  • 37
    • 52049083402 scopus 로고    scopus 로고
    • Oxidative stress-induced disruption of epithelial and endothelial tight junctions
    • Rao R: Oxidative stress-induced disruption of epithelial and endothelial tight junctions. Front Biosci 2008, 13:7210-7226
    • (2008) Front Biosci , vol.13 , pp. 7210-7226
    • Rao, R.1
  • 40
    • 0036901407 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-β-catenin complexes from the cytoskeleton by oxidative stress
    • Rao RK, Basuroy S, Rao VU, Karnaky Jr KJ, Gupta A: Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-β-catenin complexes from the cytoskeleton by oxidative stress, Biochem J 2002, 368:471-481
    • (2002) Biochem J , vol.368 , pp. 471-481
    • Rao, R.K.1    Basuroy, S.2    Rao, V.U.3    Karnaky Jr., K.J.4    Gupta, A.5
  • 43
    • 26244450671 scopus 로고    scopus 로고
    • Myosin light chain kinase is involved in lipopolysaccharide-induced disruption of colonic epithelial barrier and bacterial translocation in rats
    • Moriez R, Salvador-Cartier C, Theodorou V, Fioramonti J, Eutamene H, Bueno L: Myosin light chain kinase is involved in lipopolysaccharide-induced disruption of colonic epithelial barrier and bacterial translocation in rats. Am J Pathol 2005, 167:1071-1079 (Pubitemid 41416259)
    • (2005) American Journal of Pathology , vol.167 , Issue.4 , pp. 1071-1079
    • Moriez, R.1    Salvador-Cartier, C.2    Theodorou, V.3    Fioramonti, J.4    Eutamene, H.5    Bueno, L.6
  • 44
    • 1442328839 scopus 로고    scopus 로고
    • Disruption of Paracellular Sealing is an Early Event in Acute Caerulein-Pancreatitis
    • DOI 10.1097/00006676-200403000-00010
    • Schmitt M, Klonowski-Stumpe H, Eckert M, Luthen R, Haussinger D: Disruption of paracellular sealing is an early event in acute caerulein-pancreatitis. Pancreas 2004, 28:181-190 (Pubitemid 38269779)
    • (2004) Pancreas , vol.28 , Issue.2 , pp. 181-190
    • Schmitt, M.1    Klonowski-Stumpe, H.2    Eckert, M.3    Luthen, R.4    Haussinger, D.5
  • 47
    • 0035185891 scopus 로고    scopus 로고
    • Neutrophil transmigration in inflammatory bowel disease is associated with differential expression of epithelial intercellular junction proteins
    • Kucharzik T, Walsh SV, Chen J, Parkos CA, Nusrat A: Neutrophil transmigration in inflammatory bowel disease is associated with differential expression of epithelial intercellular junction proteins. Am J Pathol 2001, 159:2001-2009 (Pubitemid 33104255)
    • (2001) American Journal of Pathology , vol.159 , Issue.6 , pp. 2001-2009
    • Kucharzik, T.1    Walsh, S.V.2    Chen, J.3    Parkos, C.A.4    Nusrat, A.5
  • 48
    • 0032958705 scopus 로고    scopus 로고
    • Altered tight junction structure contributes to the impaired epithelial barrier function in ulcerative colitis
    • DOI 10.1016/S0016-5085(99)70126-5
    • Schmitz H, Barmeyer C, Fromm M, Runkel N, Foss HD, Bentzel CJ, Riecken EO, Schulzke JD: Altered tight junction structure contributes to the impaired epithelial barrier function in ulcerative colitis. Gastroenterology 1999, 116:301-309 (Pubitemid 29055352)
    • (1999) Gastroenterology , vol.116 , Issue.2 , pp. 301-309
    • Schmitz, H.1    Barmeyer, C.2    Fromm, M.3    Runkel, N.4    Foss, H.-D.5    Bentzel, C.J.6    Riecken, E.-O.7    Schulzke, J.-D.8
  • 50
    • 0028972499 scopus 로고
    • Inflammatory bowel disease and adenomas in mice expressing a dominant negative N-cadherin
    • Hermiston ML, Gordon JI: Inflammatory bowel disease and adenomas in mice expressing a dominant negative N-cadherin. Science 1995, 270:1203-1207
    • (1995) Science , vol.270 , pp. 1203-1207
    • Hermiston, M.L.1    Gordon, J.I.2
  • 54
    • 0023631266 scopus 로고
    • Alteration of intestinal tight junction structure and permeability by cytoskeletal contraction
    • Madara JL, Moore R, Carlson S: Alteration of intestinal tight junction structure and permeability by cytoskeletal contraction. Am J Physiol 1987, 253:C854-C861
    • (1987) Am J Physiol , vol.253
    • Madara, J.L.1    Moore, R.2    Carlson, S.3
  • 55
    • 26244442836 scopus 로고    scopus 로고
    • Mechanism of IFN-γ-induced endocytosis of tight junction proteins: Myosin II-dependent vacuolarization of the apical plasma membrane
    • Utech M, Ivanov AI, Samarin SN, Bruewer M, Turner JR, Mrsny RJ, Parkos CA, Nusrat A: Mechanism of IFN-γ-induced endocytosis of tight junction proteins: myosin II-dependent vacuolarization of the apical plasma membrane. Mol Biol Cell 2005, 16:5040-5052
    • (2005) Mol Biol Cell , vol.16 , pp. 5040-5052
    • Utech, M.1    Ivanov, A.I.2    Samarin, S.N.3    Bruewer, M.4    Turner, J.R.5    Mrsny, R.J.6    Parkos, C.A.7    Nusrat, A.8
  • 56
    • 0032977248 scopus 로고    scopus 로고
    • Interferon-γ decreases barrier function in T84 cells by reducing ZO-1 levels and disrupting apical actin
    • Youakim A, Ahdieh M: Interferon-γ decreases barrier function in T84 cells by reducing ZO-1 levels and disrupting apical actin. Am J Physiol 1999, 276:G1279-G1288
    • (1999) Am J Physiol , vol.276
    • Youakim, A.1    Ahdieh, M.2
  • 57
    • 0142093131 scopus 로고    scopus 로고
    • Cytoskeletal rearrangements in gastric epithelial cells in response to Helicobacter pylori infection
    • DOI 10.1099/jmm.0.05229-0
    • Su B, Ceponis PJ, Sherman PM: Cytoskeletal rearrangements in gastric epithelial cells in response to Helicobacter pylori infection. J Med Microbiol 2003, 52:861-867 (Pubitemid 37297314)
    • (2003) Journal of Medical Microbiology , vol.52 , Issue.10 , pp. 861-867
    • Su, B.1    Ceponis, P.J.M.2    Sherman, P.M.3
  • 61
    • 35448998551 scopus 로고    scopus 로고
    • Astrovirus increases epithelial barrier permeability independently of viral replication
    • DOI 10.1128/JVI.00942-07
    • Moser LA, Carter M, Schultz-Cherry S: Astrovirus increases epithelial barrier permeability independently of viral replication. J Virol 2007, 81:11937-11945 (Pubitemid 47623825)
    • (2007) Journal of Virology , vol.81 , Issue.21 , pp. 11937-11945
    • Moser, L.A.1    Carter, M.2    Schultz-Cherry, S.3
  • 63
    • 19644372625 scopus 로고    scopus 로고
    • Dislocation of tight junction proteins without F-actin disruption in inactive Crohn's disease
    • Oshitani N, Watanabe K, Nakamura S, Fujiwara Y, Higuchi K, Arakawa T: Dislocation of tight junction proteins without F-actin disruption in inactive Crohn's disease. Int J Mol Med 2005, 15:407-410
    • (2005) Int J Mol Med , vol.15 , pp. 407-410
    • Oshitani, N.1    Watanabe, K.2    Nakamura, S.3    Fujiwara, Y.4    Higuchi, K.5    Arakawa, T.6
  • 64
    • 0013069021 scopus 로고    scopus 로고
    • Increases in free radicals and cytoskeletal protein oxidation and nitration in the colon of patients with inflammatory bowel disease
    • DOI 10.1136/gut.52.5.720
    • Keshavarzian A, Banan A, Farhadi A, Komanduri S, Mutlu E, Zhang Y, Fields JZ: Increases in free radicals and cytoskeletal protein oxidation and nitration in the colon of patients with inflammatory bowel disease. Gut 2003, 52:720-728 (Pubitemid 36528876)
    • (2003) Gut , vol.52 , Issue.5 , pp. 720-728
    • Keshavarzian, A.1    Banan, A.2    Farhadi, A.3    Komanduri, S.4    Mutlu, E.5    Zhang, Y.6    Fields, J.Z.7
  • 65
    • 34547672619 scopus 로고    scopus 로고
    • Intestinal epithelial cell signalling and chronic inflammation: From the proteome to specific molecular mechanisms
    • DOI 10.1016/j.mrfmmm.2007.05.010, PII S0027510707002436, Nutrigenomics
    • Werner T, Haller D: Intestinal epithelial cell signalling and chronic inflammation: from the proteome to specific molecular mechanisms. Mutat Res 2007, 622:42-57 (Pubitemid 47211180)
    • (2007) Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis , vol.622 , Issue.1-2 , pp. 42-57
    • Werner, T.1    Haller, D.2
  • 67
  • 68
    • 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
    • Ivanov AI, McCall IC, Parkos CA, Nusrat A: Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex. Mol Biol Cell 2004, 15:2639-2651
    • (2004) Mol Biol Cell , vol.15 , pp. 2639-2651
    • Ivanov, A.I.1    McCall, I.C.2    Parkos, C.A.3    Nusrat, A.4
  • 69
    • 2642580994 scopus 로고    scopus 로고
    • Pulmonary endothelial cell barrier enhancement by sphingosine 1-phosphate: Roles for cortactin and myosin light chain kinase
    • Dudek SM, Jacobson JR, Chiang ET, Birukov KG, Wang P, Zhan X, Garcia JG: Pulmonary endothelial cell barrier enhancement by sphingosine 1-phosphate: roles for cortactin and myosin light chain kinase. J Biol Chem 2004, 279:24692-24700
    • (2004) J Biol Chem , vol.279 , pp. 24692-24700
    • Dudek, S.M.1    Jacobson, J.R.2    Chiang, E.T.3    Birukov, K.G.4    Wang, P.5    Zhan, X.6    Garcia, J.G.7
  • 70
    • 44449149681 scopus 로고    scopus 로고
    • Cell responses regulated by early reorganization of actin cytoskeleton
    • Papakonstanti EA, Stournaras C: Cell responses regulated by early reorganization of actin cytoskeleton. FEBS Lett 2008, 582:2120-2127
    • (2008) FEBS Lett , vol.582 , pp. 2120-2127
    • Papakonstanti, E.A.1    Stournaras, C.2
  • 71
    • 66749172932 scopus 로고    scopus 로고
    • Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility
    • Ivanov AI, Samarin SN, Bachar M, Parkos CA, Nusrat A: Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility. BMC Cell Biol 2009, 10:36
    • (2009) BMC Cell Biol , vol.10 , pp. 36
    • Ivanov, A.I.1    Samarin, S.N.2    Bachar, M.3    Parkos, C.A.4    Nusrat, A.5
  • 74
    • 33845993635 scopus 로고    scopus 로고
    • Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration
    • Sandquist JC, Swenson KI, Demali KA, Burridge K, Means AR: Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration. J Biol Chem 2006, 281:35873-35883
    • (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
  • 75
    • 4744364577 scopus 로고    scopus 로고
    • Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice
    • DOI 10.1074/jbc.C400352200
    • Conti MA, Even-Ram S, Liu C, Yamada KM, Adelstein RS: Defects in cell adhesion and the visceral endoderm following ablation of non-muscle myosin heavy chain II-A in mice. J Biol Chem 2004, 279:41263-41266 (Pubitemid 39313562)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41263-41266
    • Conti, M.A.1    Even-Ram, S.2    Liu, C.3    Yamada, K.M.4    Adelstein, R.S.5
  • 76
    • 21744445075 scopus 로고    scopus 로고
    • Regulation of myosin II during cytokinesis in higher eukaryotes
    • Matsumura F: Regulation of myosin II during cytokinesis in higher eukaryotes. Trends Cell Biol 2005, 15:371-377
    • (2005) Trends Cell Biol , vol.15 , pp. 371-377
    • Matsumura, F.1
  • 77
    • 33845335504 scopus 로고    scopus 로고
    • Traction forces of fibroblasts are regulated by the Rho-dependent kinase but not by the myosin light chain kinase
    • Beningo KA, Hamao K, Dembo M, Wang YL, Hosoya H: Traction forces of fibroblasts are regulated by the Rho-dependent kinase but not by the myosin light chain kinase. Arch Biochem Biophys 2006, 456:224-231
    • (2006) Arch Biochem Biophys , vol.456 , pp. 224-231
    • Beningo, K.A.1    Hamao, K.2    Dembo, M.3    Wang, Y.L.4    Hosoya, H.5
  • 78
    • 0041384357 scopus 로고    scopus 로고
    • LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment
    • DOI 10.1242/jcs.00606
    • Smith A, Bracke M, Leitinger B, Porter JC, Hogg N: LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment. J Cell Sci 2003, 116:3123-3133 (Pubitemid 37038961)
    • (2003) Journal of Cell Science , vol.116 , Issue.15 , pp. 3123-3133
    • Smith, A.1    Bracke, M.2    Leitinger, B.3    Porter, J.C.4    Hogg, N.5
  • 79
    • 34548491399 scopus 로고    scopus 로고
    • Rho/Rho-associated kinase-II signaling mediates disassembly of epithelial apical junctions
    • DOI 10.1091/mbc.E07-04-0315
    • Samarin SN, Ivanov AI, Flatau G, Parkos CA, Nusrat A: Rho/Rho-associated kinase-II signaling mediates disassembly of epithelial apical junctions. Mol Biol Cell 2007, 18:3429-3439 (Pubitemid 47378682)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.9 , pp. 3429-3439
    • Samarin, S.N.1    Ivanov, A.I.2    Flatau, G.3    Parkos, C.A.4    Nusrat, A.5
  • 80
    • 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: 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 2004, 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
  • 81
    • 0036305635 scopus 로고    scopus 로고
    • ROCK and Dia have opposing effects on adherens junctions downstream of Rho
    • DOI 10.1038/ncb796
    • Sahai E, Marshall CJ: ROCK and Dia have opposing effects on adherens junctions downstream of Rho. Nat Cell Biol 2002, 4:408-415 (Pubitemid 34746158)
    • (2002) Nature Cell Biology , vol.4 , Issue.6 , pp. 408-415
    • Sahai, E.1    Marshall, C.J.2
  • 82
    • 47049102226 scopus 로고    scopus 로고
    • Tight junctional disruption and apoptosis in an in vitro model of Citrobacter rodentium infection
    • Flynn AN, Buret AG: Tight junctional disruption and apoptosis in an in vitro model of Citrobacter rodentium infection. Microb Pathog 2008, 45:98-104
    • (2008) Microb Pathog , vol.45 , pp. 98-104
    • Flynn, A.N.1    Buret, A.G.2
  • 83
    • 34548478100 scopus 로고    scopus 로고
    • Roles of Rho/ROCK and MLCK in TNF-α-induced changes in endothelial morphology and permeability
    • McKenzie JA, Ridley AJ: Roles of Rho/ROCK and MLCK in TNF-α-induced changes in endothelial morphology and permeability. J Cell Physiol 2007, 213:221-228
    • (2007) J Cell Physiol , vol.213 , pp. 221-228
    • McKenzie, J.A.1    Ridley, A.J.2
  • 87
    • 9644274187 scopus 로고    scopus 로고
    • Integrity of cell-cell contacts is a critical regulator of TGF-β1-induced epithelial-to-myofibroblast transition: Role for β-catenin
    • Masszi A, Fan L, Rosivall L, McCulloch CA, Rotstein OD, Mucsi I, Kapus A: Integrity of cell-cell contacts is a critical regulator of TGF-β1-induced epithelial-to-myofibroblast transition: role for β-catenin. Am J Pathol 2004, 165:1955-1967 (Pubitemid 39578374)
    • (2004) American Journal of Pathology , vol.165 , Issue.6 , pp. 1955-1967
    • Masszi, A.1    Fan, L.2    Rosivall, L.3    McCulloch, C.A.4    Rotstein, O.D.5    Mucsi, I.6    Kapus, A.7
  • 88
    • 63849237020 scopus 로고    scopus 로고
    • Regulation of epithelial apical junctional complex by Rho family GTPases
    • Samarin S, Nusrat A: Regulation of epithelial apical junctional complex by Rho family GTPases. Front Biosci 2009, 14:1129-1142
    • (2009) Front Biosci , vol.14 , pp. 1129-1142
    • Samarin, S.1    Nusrat, A.2
  • 89
  • 90
    • 4444224948 scopus 로고    scopus 로고
    • Upregulation of Rho-kinase (ROCK-2) expression and enhanced contraction to endothelin-1 in the mesenteric artery from lipopolysaccharide-treated rats
    • DOI 10.1016/j.ejphar.2004.07.092, PII S001429990400826X
    • Buyukafsar K, Arikan O, Ark M, Kubat H, Ozveren E: Upregulation of Rho-kinase (ROCK-2) expression and enhanced contraction to endothelin- 1 in the mesenteric artery from lipopolysaccharide-treated rats. Eur J Pharmacol 2004, 498:211-217 (Pubitemid 39208081)
    • (2004) European Journal of Pharmacology , vol.498 , Issue.1-3 , pp. 211-217
    • Buyukafsar, K.1    Arikan, O.2    Ark, M.3    Kubat, H.4    Ozveren, E.5
  • 91
    • 4644236321 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli activates the RhoA signaling pathway via the stimulation of GEF-H1
    • DOI 10.1038/sj.emboj.7600359
    • Matsuzawa T, Kuwae A, Yoshida S, Sasakawa C, Abe A: Enteropathogenic Escherichia coli activates the RhoA signaling pathway via the stimulation of GEF-H1. EMBO J 2004, 23:3570-3582 (Pubitemid 39265546)
    • (2004) EMBO Journal , vol.23 , Issue.17 , pp. 3570-3582
    • Matsuzawa, T.1    Kuwae, A.2    Yoshida, S.3    Sasakawa, C.4    Abe, A.5
  • 93
  • 95
    • 45949086355 scopus 로고    scopus 로고
    • Mechanism of IL-1β-induced increase in intestinal epithelial tight junction permeability
    • Al-Sadi R, Ye D, Dokladny K, Ma TY: Mechanism of IL-1β-induced increase in intestinal epithelial tight junction permeability. J Immunol 2008, 180:5653-5661
    • (2008) J Immunol , vol.180 , pp. 5653-5661
    • Al-Sadi, R.1    Ye, D.2    Dokladny, K.3    Ma, T.Y.4
  • 96
    • 34250190636 scopus 로고    scopus 로고
    • LIGHT signals directly to intestinal epithelia to cause barrier dysfunction via cytoskeletal and endocytic mechanisms
    • Schwarz BT, Wang F, Shen L, Clayburgh DR, Su L, Wang Y, Fu YX, Turner JR: LIGHT signals directly to intestinal epithelia to cause barrier dysfunction via cytoskeletal and endocytic mechanisms. Gastroenterology 2007, 132:2383-2394
    • (2007) Gastroenterology , vol.132 , pp. 2383-2394
    • Schwarz, B.T.1    Wang, F.2    Shen, L.3    Clayburgh, D.R.4    Su, L.5    Wang, Y.6    Fu, Y.X.7    Turner, J.R.8
  • 98
    • 28444489667 scopus 로고    scopus 로고
    • Helicobacter pylori activates myosin light-chain kinase to disrupt claudin-4 and claudin-5 and increase epithelial permeability
    • Fedwick JP, Lapointe TK, Meddings JB, Sherman PM, Buret AG: Helicobacter pylori activates myosin light-chain kinase to disrupt claudin-4 and claudin-5 and increase epithelial permeability. Infect Immun 2005, 73:7844-7852
    • (2005) Infect Immun , vol.73 , pp. 7844-7852
    • Fedwick, J.P.1    Lapointe, T.K.2    Meddings, J.B.3    Sherman, P.M.4    Buret, A.G.5
  • 99
    • 0032036518 scopus 로고    scopus 로고
    • Signal Transduction Pathways Involved in Enterohemorrhagic Escherichia coli-Induced Alterations in T84 Epithelial Permeability
    • Philpott DJ, McKay DM, Mak W, Perdue MH, Sherman PM: Signal transduction pathways involved in enterohemorrhagic Escherichia coli-induced alterations in T84 epithelial permeability. Infect Immun 1998, 66:1680-1687 (Pubitemid 128471535)
    • (1998) Infection and Immunity , vol.66 , Issue.4 , pp. 1680-1687
    • Philpott, D.J.1    Mckay, D.M.2    Mak, W.3    Perdue, M.H.4    Sherman, P.M.5
  • 100
    • 0036789132 scopus 로고    scopus 로고
    • Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion
    • Scott KG, Meddings JB, Kirk DR, Lees-Miller SP, Buret AG: Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion. Gastroenterology 2002, 123:1179-1190
    • (2002) Gastroenterology , vol.123 , pp. 1179-1190
    • Scott, K.G.1    Meddings, J.B.2    Kirk, D.R.3    Lees-Miller, S.P.4    Buret, A.G.5
  • 101
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • DOI 10.1042/BJ20021535
    • Bain J, McLauchlan H, Elliott M, Cohen P: The specificities of protein kinase inhibitors: an update. Biochem J 2003, 371:199-204 (Pubitemid 36458094)
    • (2003) Biochemical Journal , vol.371 , Issue.1 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 102
    • 0036305854 scopus 로고    scopus 로고
    • A membrane-permeant peptide that inhibits MLC kinase restores barrier function in in vitro models of intestinal disease
    • DOI 10.1053/gast.2002.34235
    • Zolotarevsky Y, Hecht G, Koutsouris A, Gonzalez DE, Quan C, Tom J, Mrsny RJ, Turner JR: A membrane-permeant peptide that inhibits MLC kinase restores barrier function in in vitro models of intestinal disease. Gastroenterology 2002, 123:163-172 (Pubitemid 34747537)
    • (2002) Gastroenterology , vol.123 , Issue.1 , pp. 163-172
    • Zolotarevsky, Y.1    Hecht, G.2    Koutsouris, A.3    Gonzalez, D.E.4    Quan, C.5    Tom, J.6    Mrsny, R.J.7    Turner, J.R.8
  • 104
    • 58649090901 scopus 로고    scopus 로고
    • Targeted epithelial tight junction dysfunction causes immune activation and contributes to development of experimental colitis
    • Su L, Shen L, Clayburgh DR, Nalle SC, Sullivan EA, Meddings JB, Abraham C, Turner JR: Targeted epithelial tight junction dysfunction causes immune activation and contributes to development of experimental colitis. Gastroenterology 2009, 136:551-563
    • (2009) Gastroenterology , vol.136 , pp. 551-563
    • Su, L.1    Shen, L.2    Clayburgh, D.R.3    Nalle, S.C.4    Sullivan, E.A.5    Meddings, J.B.6    Abraham, C.7    Turner, J.R.8
  • 106
    • 0033754902 scopus 로고    scopus 로고
    • The polymerization motor
    • Theriot JA: The polymerization motor. Traffic 2000, 1:19-28
    • (2000) Traffic , vol.1 , pp. 19-28
    • Theriot, J.A.1
  • 107
    • 19644382735 scopus 로고    scopus 로고
    • Differential roles for actin polymerization and a myosin II motor in assembly of the epithelial apical junctional complex
    • DOI 10.1091/mbc.E05-01-0043
    • Ivanov AI, Hunt D, Utech M, Nusrat A, Parkos CA: Differential roles for actin polymerization and a myosin II motor in assembly of the epithelial apical junctional complex. Mol Biol Cell 2005, 16:2636-2650 (Pubitemid 40741212)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.6 , pp. 2636-2650
    • Ivanov, A.I.1    Hunt, D.2    Utech, M.3    Nusrat, A.4    Parkos, C.A.5
  • 108
    • 24344457031 scopus 로고    scopus 로고
    • Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis
    • Shen L, Turner JR: Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis. Mol Biol Cell 2005, 16:3919-3936
    • (2005) Mol Biol Cell , vol.16 , pp. 3919-3936
    • Shen, L.1    Turner, J.R.2
  • 109
    • 36549035377 scopus 로고    scopus 로고
    • A cytoskeletal demolition worker: Myosin II acts as an actin depolymerization agent
    • Haviv L, Gillo D, Backouche F, Bernheim-Groswasser A: A cytoskeletal demolition worker: myosin II acts as an actin depolymerization agent. J Mol Biol 2008, 375:325-330
    • (2008) J Mol Biol , vol.375 , pp. 325-330
    • Haviv, L.1    Gillo, D.2    Backouche, F.3    Bernheim-Groswasser, A.4
  • 110
    • 53449100875 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in smooth muscle: A new paradigm for the regulation of smooth muscle contraction
    • Gunst SJ, Zhang W: Actin cytoskeletal dynamics in smooth muscle: a new paradigm for the regulation of smooth muscle contraction. Am J Physiol Cell Physiol 2008, 295:C576-C587
    • (2008) Am J Physiol Cell Physiol , vol.295
    • Gunst, S.J.1    Zhang, W.2
  • 113
    • 77649222989 scopus 로고    scopus 로고
    • Rac1 inactivation by lethal toxin from Clostridium sordellii modifies Focal Adhesions upstream of actin depolymerization
    • Geny B, Grassart A, Manich M, Chicanne G, Payrastre B, Sauvonnet N, Popoff MR: Rac1 inactivation by lethal toxin from Clostridium sordellii modifies Focal Adhesions upstream of actin depolymerization. Cell Microbiol 2010, 12:217-232
    • (2010) Cell Microbiol , vol.12 , pp. 217-232
    • Geny, B.1    Grassart, A.2    Manich, M.3    Chicanne, G.4    Payrastre, B.5    Sauvonnet, N.6    Popoff, M.R.7
  • 114
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono S: Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int Rev Cytol 2007, 258:1-82
    • (2007) Int Rev Cytol , vol.258 , pp. 1-82
    • Ono, S.1
  • 115
    • 0348011602 scopus 로고    scopus 로고
    • Regulation of the neuronal actin cytoskeleton by ADF/cofilin
    • Sarmiere PD, Bamburg JR: Regulation of the neuronal actin cytoskeleton by ADF/cofilin. J Neurobiol 2004, 58:103-117
    • (2004) J Neurobiol , vol.58 , pp. 103-117
    • Sarmiere, P.D.1    Bamburg, J.R.2
  • 116
    • 34249315804 scopus 로고    scopus 로고
    • Lim kinases, regulators of actin dynamics
    • Bernard O: Lim kinases, regulators of actin dynamics. Int J Biochem Cell Biol 2007, 39:1071-1076
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1071-1076
    • Bernard, O.1
  • 118
    • 56249085965 scopus 로고    scopus 로고
    • Cofilin mediates tight-junction opening by redistributing actin and tight-junction proteins
    • Nagumo Y, Han J, Bellila A, Isoda H, Tanaka T: Cofilin mediates tight-junction opening by redistributing actin and tight-junction proteins. Biochem Biophys Res Commun 2008, 377:921-925
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 921-925
    • Nagumo, Y.1    Han, J.2    Bellila, A.3    Isoda, H.4    Tanaka, T.5
  • 121
    • 33646130148 scopus 로고    scopus 로고
    • Upregulation of profilin, cofilin-2 and LIMK2 in cultured pulmonary artery smooth muscle cells and in pulmonary arteries of monocrotaline-treated rats
    • Dai YP, Bongalon S, Tian H, Parks SD, Mutafova-Yambolieva VN, Yamboliev IA: Upregulation of profilin, cofilin-2 and LIMK2 in cultured pulmonary artery smooth muscle cells and in pulmonary arteries of monocrotaline-treated rats. Vascul Pharmacol 2006, 44:275-282
    • (2006) Vascul Pharmacol , vol.44 , pp. 275-282
    • Dai, Y.P.1    Bongalon, S.2    Tian, H.3    Parks, S.D.4    Mutafova-Yambolieva, V.N.5    Yamboliev, I.A.6
  • 123
    • 50549097734 scopus 로고    scopus 로고
    • Defects in actin dynamics lead to an autoinflammatory condition through the upregulation of CXCL5
    • Verdoni AM, Smith RS, Ikeda A, Ikeda S: Defects in actin dynamics lead to an autoinflammatory condition through the upregulation of CXCL5. PLoS One 2008, 3:e2701
    • (2008) PLoS One , vol.3
    • Verdoni, A.M.1    Smith, R.S.2    Ikeda, A.3    Ikeda, S.4
  • 124
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin Promotes Actin Polymerization and Defines the Direction of Cell Motility
    • DOI 10.1126/science.1094561
    • Ghosh M, Song X, Mouneimne G, Sidani M, Lawrence DS, Condeelis JS: Cofilin promotes actin polymerization and defines the direction of cell motility. Science 2004, 304:743-746 (Pubitemid 38560882)
    • (2004) Science , vol.304 , Issue.5671 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 126
    • 0033981223 scopus 로고    scopus 로고
    • Parallel actin bundles and their multiple actin-bundling proteins
    • Bartles JR: Parallel actin bundles and their multiple actin-bundling proteins. Curr Opin Cell Biol 2000, 12:72-78
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 72-78
    • Bartles, J.R.1
  • 127
    • 0141764815 scopus 로고    scopus 로고
    • Actin filament turnover regulated by cross-linking accounts for the size, shape, location, and number of actin bundles in Drosophila bristles
    • DOI 10.1091/mbc.E03-03-0158
    • Tilney LG, Connelly PS, Ruggiero L, Vranich KA, Guild GM: Actin filament turnover regulated by cross-linking accounts for the size, shape, location, and number of actin bundles in Drosophila bristles. Mol Biol Cell 2003, 14:3953-3966 (Pubitemid 37186300)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.10 , pp. 3953-3966
    • Tilney, L.G.1    Connelly, P.S.2    Ruggiero, L.3    Vranich, K.A.4    Guild, G.M.5
  • 128
    • 38349138921 scopus 로고    scopus 로고
    • EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt
    • Abe K, Takeichi M: EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt. Proc Natl Acad Sci USA 2008, 105:13-19
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13-19
    • Abe, K.1    Takeichi, M.2
  • 129
    • 0026760071 scopus 로고
    • A sarcomeric α-actinin truncated at the carboxyl end induces the breakdown of stress fibers in PtK2 cells and the formation of nemaline-like bodies and breakdown of myofibrils in myotubes
    • Schultheiss T, Choi J, Lin ZX, DiLullo C, Cohen-Gould L, Fischman D, Holtzer H: A sarcomeric α-actinin truncated at the carboxyl end induces the breakdown of stress fibers in PtK2 cells and the formation of nemaline-like bodies and breakdown of myofibrils in myotubes. Proc Natl Acad Sci USA 1992, 89:9282-9286
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9282-9286
    • Schultheiss, T.1    Choi, J.2    Lin, Z.X.3    DiLullo, C.4    Cohen-Gould, L.5    Fischman, D.6    Holtzer, H.7
  • 130
    • 43249083763 scopus 로고    scopus 로고
    • Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions
    • DOI 10.1128/MCB.00144-08
    • Nakatsuji H, Nishimura N, Yamamura R, Kanayama HO, Sasaki T: Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions. Mol Cell Biol 2008, 28:3324-3335 (Pubitemid 351657096)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.10 , pp. 3324-3335
    • Nakatsuji, H.1    Nishimura, N.2    Yamamura, R.3    Kanayama, H.-O.4    Sasaki, T.5
  • 135
    • 0035800777 scopus 로고    scopus 로고
    • The Cytoskeletal/Non-musele Isoform of alpha-Actinin Is Phosphorylated on Its Actin-binding Domain by the Focal Adhesion Kinase
    • DOI 10.1074/jbc.M101678200
    • Izaguirre G, Aguirre L, Hu YP, Lee HY, Schlaepfer DD, Aneskievich BJ, Haimovich B: The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase. J Biol Chem 2001, 276:28676-28685 (Pubitemid 37451942)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.31 , pp. 28676-28685
    • Izaguirre, G.1    Aguirre, L.2    Hu, Y.-P.3    Lee, H.Y.4    Schlaepfer, D.D.5    Aneskievich, B.J.6    Haimovich, B.7
  • 136
    • 36849010967 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase/mitogen-activated protein kinase regulates actin organization and cell motility by phosphorylating the actin cross-linking protein EPLIN
    • DOI 10.1128/MCB.00661-07
    • Han MY, Kosako H, Watanabe T, Hattori S: Extracellular signal-regulated kinase/mitogen-activated protein kinase regulates actin organization and cell motility by phosphorylating the actin cross-linking protein EPLIN. Mol Cell Biol 2007, 27:8190-8204 (Pubitemid 350234233)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.23 , pp. 8190-8204
    • Han, M.-Y.1    Kosako, H.2    Watanabe, T.3    Hattori, S.4


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