메뉴 건너뛰기




Volumn 6, Issue 5, 2011, Pages

Two distinct integrin-mediated mechanisms contribute to apical lumen formation in Epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA6BETA4 INTEGRIN; INTEGRIN RECEPTOR; PROTEIN CDC42; RAC1 PROTEIN; VERY LATE ACTIVATION ANTIGEN 2; SMALL INTERFERING RNA; VERY LATE ACTIVATION ANTIGEN 3;

EID: 79955872975     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019453     Document Type: Article
Times cited : (51)

References (54)
  • 1
    • 0037428084 scopus 로고    scopus 로고
    • Tube morphogenesis: Making and shaping biological tubes
    • Lubarsky B, Krasnow MA, (2003) Tube morphogenesis: Making and shaping biological tubes. Cell 112: 19-28.
    • (2003) Cell , vol.112 , pp. 19-28
    • Lubarsky, B.1    Krasnow, M.A.2
  • 2
    • 54549091120 scopus 로고    scopus 로고
    • From cells to organs: Building polarized tissue
    • Bryant DM, Mostov KE, (2008) From cells to organs: Building polarized tissue. Nat Rev Mol Cell Biol 9: 887-901.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 887-901
    • Bryant, D.M.1    Mostov, K.E.2
  • 3
    • 0037020196 scopus 로고    scopus 로고
    • The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini
    • Debnath J, Mills KR, Collins NL, Reginato MJ, Muthuswamy SK, et al. (2002) The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini. Cell 111: 29-40.
    • (2002) Cell , vol.111 , pp. 29-40
    • Debnath, J.1    Mills, K.R.2    Collins, N.L.3    Reginato, M.J.4    Muthuswamy, S.K.5
  • 4
    • 1542513774 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is required for induction of autophagy during lumen formation in vitro
    • Mills KR, Reginato M, Debnath J, Queenan B, Brugge JS, (2004) Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is required for induction of autophagy during lumen formation in vitro. Proc Natl Acad Sci U S A 101: 3438-3443.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3438-3443
    • Mills, K.R.1    Reginato, M.2    Debnath, J.3    Queenan, B.4    Brugge, J.S.5
  • 5
    • 41449087759 scopus 로고    scopus 로고
    • Cell-polarity dynamics controls the mechanism of lumen formation in epithelial morphogenesis
    • Martin-Belmonte F, Yu W, Rodriguez-Fraticelli AE, Ewald A, Werb Z, et al. (2008) Cell-polarity dynamics controls the mechanism of lumen formation in epithelial morphogenesis. Curr Biol 18: 507-513.
    • (2008) Curr Biol , vol.18 , pp. 507-513
    • Martin-Belmonte, F.1    Yu, W.2    Rodriguez-Fraticelli, A.E.3    Ewald, A.4    Werb, Z.5
  • 6
    • 0033063569 scopus 로고    scopus 로고
    • BMP signaling plays a role in visceral endoderm differentiation and cavitation in the early mouse embryo
    • Coucouvanis E, Martin GR, (1999) BMP signaling plays a role in visceral endoderm differentiation and cavitation in the early mouse embryo. Development 126: 535-546.
    • (1999) Development , vol.126 , pp. 535-546
    • Coucouvanis, E.1    Martin, G.R.2
  • 7
    • 41549086164 scopus 로고    scopus 로고
    • Regulation of cell polarity during epithelial morphogenesis
    • Martin-Belmonte F, Mostov K, (2008) Regulation of cell polarity during epithelial morphogenesis. Curr Opin Cell Biol 20: 227-234.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 227-234
    • Martin-Belmonte, F.1    Mostov, K.2
  • 8
    • 0034854201 scopus 로고    scopus 로고
    • Rac1 orientates epithelial apical polarity through effects on basolateral laminin assembly
    • O'Brien LE, Jou TS, Pollack AL, Zhang Q, Hansen SH, et al. (2001) Rac1 orientates epithelial apical polarity through effects on basolateral laminin assembly. Nat Cell Biol 3: 831-88.
    • (2001) Nat Cell Biol , vol.3 , pp. 831-888
    • O'Brien, L.E.1    Jou, T.S.2    Pollack, A.L.3    Zhang, Q.4    Hansen, S.H.5
  • 9
    • 12844272106 scopus 로고    scopus 로고
    • {Beta}1-integrin orients epithelial polarity via Rac1 and laminin
    • Yu W, Datta A, Leroy P, O'Brien L E, Mak G, et al. (2005) {Beta}1-integrin orients epithelial polarity via Rac1 and laminin. Mol Biol Cell 16: 433-445.
    • (2005) Mol Biol Cell , vol.16 , pp. 433-445
    • Yu, W.1    Datta, A.2    Leroy, P.3    O'Brien, L.E.4    Mak, G.5
  • 10
    • 0037941157 scopus 로고    scopus 로고
    • Integrins in epithelial cell polarity: Using antibodies to analyze adhesive function and morphogenesis
    • Matlin KS, Haus B, Zuk A, (2003) Integrins in epithelial cell polarity: Using antibodies to analyze adhesive function and morphogenesis. Methods 30: 235-246.
    • (2003) Methods , vol.30 , pp. 235-246
    • Matlin, K.S.1    Haus, B.2    Zuk, A.3
  • 11
    • 0032493934 scopus 로고    scopus 로고
    • Novel roles for alpha3beta1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes
    • Hodivala-Dilke KM, DiPersio CM, Kreidberg JA, Hynes RO, (1998) Novel roles for alpha3beta1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes. J Cell Biol 142: 1357-1369.
    • (1998) J Cell Biol , vol.142 , pp. 1357-1369
    • Hodivala-Dilke, K.M.1    DiPersio, C.M.2    Kreidberg, J.A.3    Hynes, R.O.4
  • 12
    • 35648976145 scopus 로고    scopus 로고
    • Intrinsic signaling functions of the beta4 integrin intracellular domain
    • Merdek KD, Yang X, Taglienti CA, Shaw LM, Mercurio AM, (2007) Intrinsic signaling functions of the beta4 integrin intracellular domain. J Biol Chem 282: 30322-30330.
    • (2007) J Biol Chem , vol.282 , pp. 30322-30330
    • Merdek, K.D.1    Yang, X.2    Taglienti, C.A.3    Shaw, L.M.4    Mercurio, A.M.5
  • 13
    • 0031848143 scopus 로고    scopus 로고
    • Ligand-independent role of the beta 4 integrin subunit in the formation of hemidesmosomes
    • Nievers MG, Schaapveld RQ, Oomen LC, Fontao L, Geerts D, et al. (1998) Ligand-independent role of the beta 4 integrin subunit in the formation of hemidesmosomes. J Cell Sci 111: 1659-1672.
    • (1998) J Cell Sci , vol.111 , pp. 1659-1672
    • Nievers, M.G.1    Schaapveld, R.Q.2    Oomen, L.C.3    Fontao, L.4    Geerts, D.5
  • 15
    • 13844289424 scopus 로고    scopus 로고
    • Gp135/podocalyxin and NHERF-2 participate in the formation of a preapical domain during polarization of MDCK cells
    • Meder D, Shevchenko A, Simons K, Fullekrug J, (2005) Gp135/podocalyxin and NHERF-2 participate in the formation of a preapical domain during polarization of MDCK cells. J Cell Biol 168: 303-313.
    • (2005) J Cell Biol , vol.168 , pp. 303-313
    • Meder, D.1    Shevchenko, A.2    Simons, K.3    Fullekrug, J.4
  • 16
    • 0028978235 scopus 로고
    • The alpha 2 beta 1 integrin regulates collagen-mediated MDCK epithelial membrane remodeling and tubule formation
    • Schwimmer R, Ojakian GK, (1995) The alpha 2 beta 1 integrin regulates collagen-mediated MDCK epithelial membrane remodeling and tubule formation. J Cell Sci 108: 2487-2498.
    • (1995) J Cell Sci , vol.108 , pp. 2487-2498
    • Schwimmer, R.1    Ojakian, G.K.2
  • 17
    • 0032514214 scopus 로고    scopus 로고
    • Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity
    • Jou TS, Nelson WJ, (1998) Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity. J Cell Biol 142: 85-100.
    • (1998) J Cell Biol , vol.142 , pp. 85-100
    • Jou, T.S.1    Nelson, W.J.2
  • 18
    • 0242585394 scopus 로고    scopus 로고
    • The rho family of small GTPases is involved in epithelial cystogenesis and tubulogenesis
    • Rogers KK, Jou TS, Guo W, Lipschutz JH, (2003) The rho family of small GTPases is involved in epithelial cystogenesis and tubulogenesis. Kidney Int 63: 1632-1644.
    • (2003) Kidney Int , vol.63 , pp. 1632-1644
    • Rogers, K.K.1    Jou, T.S.2    Guo, W.3    Lipschutz, J.H.4
  • 19
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander EE, ten Klooster JP, van Delft S, van der Kammen RA, Collard JG, (1999) Rac downregulates rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J Cell Biol 147: 1009-1022.
    • (1999) J Cell Biol , vol.147 , pp. 1009-1022
    • Sander, E.E.1    ten Klooster, J.P.2    van Delft, S.3    van der Kammen, R.A.4    Collard, J.G.5
  • 20
    • 51049124493 scopus 로고    scopus 로고
    • Involvement of RhoA, ROCK I and myosin II in inverted orientation of epithelial polarity
    • Yu W, Shewan AM, Brakeman P, Eastburn DJ, Datta A, et al. (2008) Involvement of RhoA, ROCK I and myosin II in inverted orientation of epithelial polarity. EMBO Rep 9: 923-929.
    • (2008) EMBO Rep , vol.9 , pp. 923-929
    • Yu, W.1    Shewan, A.M.2    Brakeman, P.3    Eastburn, D.J.4    Datta, A.5
  • 21
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42--the centre of polarity
    • Etienne-Manneville S, (2004) Cdc42--the centre of polarity. J Cell Sci 117: 1291-1300.
    • (2004) J Cell Sci , vol.117 , pp. 1291-1300
    • Etienne-Manneville, S.1
  • 22
    • 0037328574 scopus 로고    scopus 로고
    • Hepatocyte growth factor switches orientation of polarity and mode of movement during morphogenesis of multicellular epithelial structures
    • Yu W, O'Brien LE, Wang F, Bourne H, Mostov KE, et al. (2003) Hepatocyte growth factor switches orientation of polarity and mode of movement during morphogenesis of multicellular epithelial structures. Mol Biol Cell 14: 748-763.
    • (2003) Mol Biol Cell , vol.14 , pp. 748-763
    • Yu, W.1    O'Brien, L.E.2    Wang, F.3    Bourne, H.4    Mostov, K.E.5
  • 23
    • 0028101021 scopus 로고
    • Orientation of spindle axis and distribution of plasma membrane proteins during cell division in polarized MDCKII cells
    • Reinsch S, Karsenti E, (1994) Orientation of spindle axis and distribution of plasma membrane proteins during cell division in polarized MDCKII cells. J Cell Biol 126: 1509-1526.
    • (1994) J Cell Biol , vol.126 , pp. 1509-1526
    • Reinsch, S.1    Karsenti, E.2
  • 24
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42
    • Martin-Belmonte F, Gassama A, Datta A, Yu W, Rescher U, et al. (2007) PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128: 383-397.
    • (2007) Cell , vol.128 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5
  • 25
    • 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
  • 26
    • 0034110936 scopus 로고    scopus 로고
    • Formation of hemidesmosome-like structures in the absence of ligand binding by the (alpha)6(beta)4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the (beta)4 integrin subunit
    • Nievers MG, Kuikman I, Geerts D, Leigh IM, Sonnenberg A, (2000) Formation of hemidesmosome-like structures in the absence of ligand binding by the (alpha)6(beta)4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the (beta)4 integrin subunit. J Cell Sci 113: 963-973.
    • (2000) J Cell Sci , vol.113 , pp. 963-973
    • Nievers, M.G.1    Kuikman, I.2    Geerts, D.3    Leigh, I.M.4    Sonnenberg, A.5
  • 27
    • 33748199154 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells
    • Gassama-Diagne A, Yu W, ter Beest M, Martin-Belmonte F, Kierbel A, et al. (2006) Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells. Nat Cell Biol 8: 963-970.
    • (2006) Nat Cell Biol , vol.8 , pp. 963-970
    • Gassama-Diagne, A.1    Yu, W.2    ter Beest, M.3    Martin-Belmonte, F.4    Kierbel, A.5
  • 28
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski R, Hall A, Mellman I, (1999) Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat Cell Biol 1: 8-13.
    • (1999) Nat Cell Biol , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 29
    • 0034903162 scopus 로고    scopus 로고
    • Selective control of basolateral membrane protein polarity by cdc42
    • Cohen D, Musch A, Rodriguez-Boulan E, (2001) Selective control of basolateral membrane protein polarity by cdc42. Traffic 2: 556-564.
    • (2001) Traffic , vol.2 , pp. 556-564
    • Cohen, D.1    Musch, A.2    Rodriguez-Boulan, E.3
  • 30
    • 0035341316 scopus 로고    scopus 로고
    • cdc42 regulates the exit of apical and basolateral proteins from the trans-golgi network
    • Musch A, Cohen D, Kreitzer G, Rodriguez-Boulan E, (2001) cdc42 regulates the exit of apical and basolateral proteins from the trans-golgi network. EMBO J 20: 2171-2179.
    • (2001) EMBO J , vol.20 , pp. 2171-2179
    • Musch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 31
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe AB, Hall A, (2005) Rho GTPases: Biochemistry and biology. Annu Rev Cell Dev Biol 21: 247-269.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 32
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the rho family of GTPases
    • Clark EA, King WG, Brugge JS, Symons M, Hynes RO, (1998) Integrin-mediated signals regulated by members of the rho family of GTPases. J Cell Biol 142: 573-586.
    • (1998) J Cell Biol , vol.142 , pp. 573-586
    • Clark, E.A.1    King, W.G.2    Brugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 33
    • 0035152391 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the rho family of GTPases
    • Cox EA, Sastry SK, Huttenlocher A, (2001) Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the rho family of GTPases. Mol Biol Cell 12: 265-277.
    • (2001) Mol Biol Cell , vol.12 , pp. 265-277
    • Cox, E.A.1    Sastry, S.K.2    Huttenlocher, A.3
  • 34
    • 0037415640 scopus 로고    scopus 로고
    • Rac and Cdc42 play distinct roles in regulating PI(3,4,5)P3 and polarity during neutrophil chemotaxis
    • Srinivasan S, Wang F, Glavas S, Ott A, Hofmann F, et al. (2003) Rac and Cdc42 play distinct roles in regulating PI(3,4,5)P3 and polarity during neutrophil chemotaxis. J Cell Biol 160: 375-385.
    • (2003) J Cell Biol , vol.160 , pp. 375-385
    • Srinivasan, S.1    Wang, F.2    Glavas, S.3    Ott, A.4    Hofmann, F.5
  • 35
    • 33747423320 scopus 로고    scopus 로고
    • Rac1 links integrin-mediated adhesion to the control of lactational differentiation in mammary epithelia
    • Akhtar N, Streuli CH, (2006) Rac1 links integrin-mediated adhesion to the control of lactational differentiation in mammary epithelia. J Cell Biol 173: 781-793.
    • (2006) J Cell Biol , vol.173 , pp. 781-793
    • Akhtar, N.1    Streuli, C.H.2
  • 36
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta
    • Etienne-Manneville S, Hall A, (2001) Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell 106: 489-498.
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 37
    • 15444367651 scopus 로고    scopus 로고
    • Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1
    • Zhou H, Kramer RH, (2005) Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1. J Biol Chem 280: 10624-10635.
    • (2005) J Biol Chem , vol.280 , pp. 10624-10635
    • Zhou, H.1    Kramer, R.H.2
  • 38
    • 0035941357 scopus 로고    scopus 로고
    • Ligation of integrin alpha 3beta 1 by laminin 5 at the wound edge activates rho-dependent adhesion of leading keratinocytes on collagen
    • Nguyen BP, Ren XD, Schwartz MA, Carter WG, (2001) Ligation of integrin alpha 3beta 1 by laminin 5 at the wound edge activates rho-dependent adhesion of leading keratinocytes on collagen. J Biol Chem 276: 43860-43870.
    • (2001) J Biol Chem , vol.276 , pp. 43860-43870
    • Nguyen, B.P.1    Ren, X.D.2    Schwartz, M.A.3    Carter, W.G.4
  • 39
    • 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
  • 40
    • 77952356153 scopus 로고    scopus 로고
    • The Cdc42 GEF intersectin 2 controls mitotic spindle orientation to form the lumen during epithelial morphogenesis
    • Rodriguez-Fraticelli AE, Vergarajauregui S, Eastburn DJ, Datta A, Alonso MA, et al. (2010) The Cdc42 GEF intersectin 2 controls mitotic spindle orientation to form the lumen during epithelial morphogenesis. J Cell Biol 189: 725-738.
    • (2010) J Cell Biol , vol.189 , pp. 725-738
    • Rodriguez-Fraticelli, A.E.1    Vergarajauregui, S.2    Eastburn, D.J.3    Datta, A.4    Alonso, M.A.5
  • 41
    • 0032841712 scopus 로고    scopus 로고
    • (Alpha)3(beta)1 integrin regulates epithelial cytoskeletal organization
    • Wang Z, Symons JM, Goldstein SL, McDonald A, Miner JH, et al. (1999) (Alpha)3(beta)1 integrin regulates epithelial cytoskeletal organization. J Cell Sci 112: 2925-2935.
    • (1999) J Cell Sci , vol.112 , pp. 2925-2935
    • Wang, Z.1    Symons, J.M.2    Goldstein, S.L.3    McDonald, A.4    Miner, J.H.5
  • 42
    • 0142059943 scopus 로고    scopus 로고
    • Distinct ligand binding sites in integrin alpha3beta1 regulate matrix adhesion and cell-cell contact
    • Zhang F, Tom CC, Kugler MC, Ching TT, Kreidberg JA, et al. (2003) Distinct ligand binding sites in integrin alpha3beta1 regulate matrix adhesion and cell-cell contact. J Cell Biol 163: 177-188.
    • (2003) J Cell Biol , vol.163 , pp. 177-188
    • Zhang, F.1    Tom, C.C.2    Kugler, M.C.3    Ching, T.T.4    Kreidberg, J.A.5
  • 43
    • 60849098434 scopus 로고    scopus 로고
    • Integrin alpha3beta1-dependent beta-catenin phosphorylation links epithelial smad signaling to cell contacts
    • Kim Y, Kugler MC, Wei Y, Kim KK, Li X, et al. (2009) Integrin alpha3beta1-dependent beta-catenin phosphorylation links epithelial smad signaling to cell contacts. J Cell Biol 184: 309-322.
    • (2009) J Cell Biol , vol.184 , pp. 309-322
    • Kim, Y.1    Kugler, M.C.2    Wei, Y.3    Kim, K.K.4    Li, X.5
  • 44
    • 61449213806 scopus 로고    scopus 로고
    • Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails
    • Legate KR, Fassler R, (2009) Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails. J Cell Sci 122: 187-198.
    • (2009) J Cell Sci , vol.122 , pp. 187-198
    • Legate, K.R.1    Fassler, R.2
  • 45
    • 0024202621 scopus 로고
    • The polarized distribution of an apical cell surface glycoprotein is maintained by interactions with the cytoskeleton of madin-darby canine kidney cells
    • Ojakian GK, Schwimmer R, (1988) The polarized distribution of an apical cell surface glycoprotein is maintained by interactions with the cytoskeleton of madin-darby canine kidney cells. J Cell Biol 107: 2377-2387.
    • (1988) J Cell Biol , vol.107 , pp. 2377-2387
    • Ojakian, G.K.1    Schwimmer, R.2
  • 46
    • 0025340884 scopus 로고
    • The alpha 1/beta 1 and alpha 6/beta 1 integrin heterodimers mediate cell attachment to distinct sites on laminin
    • Hall DE, Reichardt LF, Crowley E, Holley B, Moezzi H, et al. (1990) The alpha 1/beta 1 and alpha 6/beta 1 integrin heterodimers mediate cell attachment to distinct sites on laminin. J Cell Biol 110: 2175-2184.
    • (1990) J Cell Biol , vol.110 , pp. 2175-2184
    • Hall, D.E.1    Reichardt, L.F.2    Crowley, E.3    Holley, B.4    Moezzi, H.5
  • 47
    • 0025753821 scopus 로고
    • Human lung tumor-associated antigen identified as an extracellular matrix adhesion molecule
    • Chen FA, Repasky EA, Bankert RB, (1991) Human lung tumor-associated antigen identified as an extracellular matrix adhesion molecule. J Exp Med 173: 1111-1119.
    • (1991) J Exp Med , vol.173 , pp. 1111-1119
    • Chen, F.A.1    Repasky, E.A.2    Bankert, R.B.3
  • 48
    • 0032921536 scopus 로고    scopus 로고
    • Identification of laminin-10/11 as a strong cell adhesive complex for a normal and a malignant human epithelial cell line
    • Ferletta M, Ekblom P, (1999) Identification of laminin-10/11 as a strong cell adhesive complex for a normal and a malignant human epithelial cell line. J Cell Sci 112: 1-10.
    • (1999) J Cell Sci , vol.112 , pp. 1-10
    • Ferletta, M.1    Ekblom, P.2
  • 49
    • 33644990678 scopus 로고    scopus 로고
    • Requirements for vav guanine nucleotide exchange factors and rho GTPases in FcgammaR- and complement-mediated phagocytosis
    • Hall AB, Gakidis MA, Glogauer M, Wilsbacher JL, Gao S, et al. (2006) Requirements for vav guanine nucleotide exchange factors and rho GTPases in FcgammaR- and complement-mediated phagocytosis. Immunity 24: 305-316.
    • (2006) Immunity , vol.24 , pp. 305-316
    • Hall, A.B.1    Gakidis, M.A.2    Glogauer, M.3    Wilsbacher, J.L.4    Gao, S.5
  • 50
    • 35748941239 scopus 로고    scopus 로고
    • Contributions of galectin-3 and -9 to epithelial cell adhesion analysed by single cell force spectroscopy
    • Friedrichs J, Torkko JM, Helenius J, Teravainen TP, Fullekrug J, et al. (2007) Contributions of galectin-3 and-9 to epithelial cell adhesion analysed by single cell force spectroscopy. J Biol Chem 282: 29375-29383.
    • (2007) J Biol Chem , vol.282 , pp. 29375-29383
    • Friedrichs, J.1    Torkko, J.M.2    Helenius, J.3    Teravainen, T.P.4    Fullekrug, J.5
  • 51
    • 44449156338 scopus 로고    scopus 로고
    • Depletion of apical transport proteins perturbs epithelial cyst formation and ciliogenesis
    • Torkko JM, Manninen A, Schuck S, Simons K, (2008) Depletion of apical transport proteins perturbs epithelial cyst formation and ciliogenesis. J Cell Sci 121: 1193-1203.
    • (2008) J Cell Sci , vol.121 , pp. 1193-1203
    • Torkko, J.M.1    Manninen, A.2    Schuck, S.3    Simons, K.4
  • 52
    • 0041935939 scopus 로고    scopus 로고
    • U. S. National Institutes of Health,Bethesda, MD, USA
    • Rasband WS, (1997-2010) ImageJ U. S. National Institutes of Health,Bethesda, MD, USA.
    • (1997) ImageJ
    • Rasband, W.S.1
  • 53
    • 1842737717 scopus 로고    scopus 로고
    • Generation of single and double knockdowns in polarized epithelial cells by retrovirus-mediated RNA interference
    • Schuck S, Manninen A, Honsho M, Fullekrug J, Simons K, (2004) Generation of single and double knockdowns in polarized epithelial cells by retrovirus-mediated RNA interference. Proc Natl Acad Sci U S A 101: 4912-4917.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4912-4917
    • Schuck, S.1    Manninen, A.2    Honsho, M.3    Fullekrug, J.4    Simons, K.5
  • 54
    • 27644505702 scopus 로고    scopus 로고
    • Caveolin-1 is not essential for biosynthetic apical membrane transport
    • Manninen A, Verkade P, Le Lay S, Torkko J, Kasper M, et al. (2005) Caveolin-1 is not essential for biosynthetic apical membrane transport. Mol Cell Biol 25: 10087-10096.
    • (2005) Mol Cell Biol , vol.25 , pp. 10087-10096
    • Manninen, A.1    Verkade, P.2    Le Lay, S.3    Torkko, J.4    Kasper, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.