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Volumn 14, Issue 8, 2004, Pages 427-434

The ins and outs of E-cadherin trafficking

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FIBROBLAST GROWTH FACTOR; GUANOSINE TRIPHOSPHATASE; PROTEIN; SOMATOMEDIN; UVOMORULIN; VASCULOTROPIN;

EID: 4143146438     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2004.07.007     Document Type: Review
Times cited : (318)

References (81)
  • 1
    • 0036270751 scopus 로고    scopus 로고
    • Regulated transport of the glucose transporter GLUT4
    • N.J. Bryant Regulated transport of the glucose transporter GLUT4 Nat. Rev. Mol. Cell Biol. 3 2002 267 277
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 267-277
    • Bryant, N.J.1
  • 2
    • 0037404210 scopus 로고    scopus 로고
    • The ins and outs of aquaporin-2 trafficking
    • D. Brown The ins and outs of aquaporin-2 trafficking Am. J. Physiol. Renal Physiol. 284 2003 F893 F901
    • (2003) Am. J. Physiol. Renal Physiol. , vol.284
    • Brown, D.1
  • 3
    • 0036341207 scopus 로고    scopus 로고
    • Signal transduction and endocytosis: Close encounters of many kinds
    • A. Sorkin, and M. Von Zastrow Signal transduction and endocytosis: close encounters of many kinds Nat. Rev. Mol. Cell Biol. 3 2002 600 614
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 600-614
    • Sorkin1    Von Zastrow, M.A.2
  • 4
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • R. Jahn Membrane fusion Cell 112 2003 519 533
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1
  • 5
    • 0037099313 scopus 로고    scopus 로고
    • PKCε controls the traffic of β1 integrins in motile cells
    • J. Ivaska PKCε controls the traffic of β1 integrins in motile cells EMBO J. 21 2002 3608 3619
    • (2002) EMBO J. , vol.21 , pp. 3608-3619
    • Ivaska, J.1
  • 6
    • 0035076508 scopus 로고    scopus 로고
    • The cadherin superfamily
    • B.D. Angst The cadherin superfamily J. Cell Sci. 114 2001 625 626
    • (2001) J. Cell Sci. , vol.114 , pp. 625-626
    • Angst, B.D.1
  • 7
    • 0026940189 scopus 로고
    • Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions
    • S. Tsukita Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions Curr. Opin. Cell Biol. 4 1992 834 839
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 834-839
    • Tsukita, S.1
  • 9
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • A.S. Yap Molecular and functional analysis of cadherin-based adherens junctions Annu. Rev. Cell Dev. Biol. 13 1997 119 146
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 119-146
    • Yap, A.S.1
  • 10
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • J.S. Bonifacino, and B.S. Glick The mechanisms of vesicle budding and fusion Cell 116 2004 153 166
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino1    Glick, B.S.J.S.2
  • 11
    • 0033593803 scopus 로고    scopus 로고
    • Coupling assembly of the E-cadherin-β-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells
    • Y.T. Chen Coupling assembly of the E-cadherin-β-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells J. Cell Biol. 144 1999 687 699
    • (1999) J. Cell Biol. , vol.144 , pp. 687-699
    • Chen, Y.T.1
  • 12
    • 0242290269 scopus 로고    scopus 로고
    • ctn to E-cadherin at the basolateral plasma membrane in polarized epithelia
    • ctn to E-cadherin at the basolateral plasma membrane in polarized epithelia J. Biol. Chem. 278 2003 43480 43488
    • (2003) J. Biol. Chem. , vol.278 , pp. 43480-43488
    • Miranda, K.C.1
  • 13
    • 0028305138 scopus 로고
    • Dynamics of cadherin-catenin complex formation: Novel protein interactions and pathways of complex assembly
    • L. Hinck Dynamics of cadherin-catenin complex formation: novel protein interactions and pathways of complex assembly J. Cell Biol. 125 1994 1327 1340
    • (1994) J. Cell Biol. , vol.125 , pp. 1327-1340
    • Hinck, L.1
  • 14
    • 0242456020 scopus 로고    scopus 로고
    • P120 catenin associates with kinesin and facilitates the transport of cadherin-catenin complexes to intercellular junctions
    • X. Chen p120 catenin associates with kinesin and facilitates the transport of cadherin-catenin complexes to intercellular junctions J. Cell Biol. 163 2003 547 557
    • (2003) J. Cell Biol. , vol.163 , pp. 547-557
    • Chen, X.1
  • 15
    • 0038607961 scopus 로고    scopus 로고
    • N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane
    • J.K. Wahl 3rd N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane J. Biol. Chem. 278 2003 17269 17276
    • (2003) J. Biol. Chem. , vol.278 , pp. 17269-17276
    • Wahl III, J.K.1
  • 16
    • 0031767359 scopus 로고    scopus 로고
    • Proprotein cleavage of E-cadherin by furin in baculovirus over-expression system: Potential role of other convertases in mammalian cells
    • H. Posthaus Proprotein cleavage of E-cadherin by furin in baculovirus over-expression system: potential role of other convertases in mammalian cells FEBS Lett. 438 1998 306 310
    • (1998) FEBS Lett. , vol.438 , pp. 306-310
    • Posthaus, H.1
  • 17
    • 0035933872 scopus 로고    scopus 로고
    • A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • K.C. Miranda A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells J. Biol. Chem. 276 2001 22565 22572
    • (2001) J. Biol. Chem. , vol.276 , pp. 22565-22572
    • Miranda, K.C.1
  • 19
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 γ-sigma1 and AP-3 δ-σ3 hemicomplexes
    • K. Janvier Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 γ-sigma1 and AP-3 δ-σ3 hemicomplexes J. Cell Biol. 163 2003 1281 1290
    • (2003) J. Cell Biol. , vol.163 , pp. 1281-1290
    • Janvier, K.1
  • 20
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • C.L. Jackson, and J.E. Casanova Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors Trends Cell Biol. 10 2000 60 67
    • (2000) Trends Cell Biol. , vol.10 , pp. 60-67
    • Jackson1    Casanova, J.E.C.L.2
  • 21
    • 1842865213 scopus 로고    scopus 로고
    • ARF-directed guanine-nucleotide-exchange (GEP) proteins
    • G. Pacheco-Rodriguez ARF-directed guanine-nucleotide-exchange (GEP) proteins Methods Mol. Biol. 189 2002 181 189
    • (2002) Methods Mol. Biol. , vol.189 , pp. 181-189
    • Pacheco-Rodriguez, G.1
  • 22
    • 0036295057 scopus 로고    scopus 로고
    • Dominant-negative mutant of BIG2, an ARF-guanine nucleotide exchange factor, specifically affects membrane trafficking from the trans-Golgi network through inhibiting membrane association of AP-1 and GGA coat proteins
    • C. Shinotsuka Dominant-negative mutant of BIG2, an ARF-guanine nucleotide exchange factor, specifically affects membrane trafficking from the trans-Golgi network through inhibiting membrane association of AP-1 and GGA coat proteins Biochem. Biophys. Res. Commun. 294 2002 254 260
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 254-260
    • Shinotsuka, C.1
  • 23
    • 9144274368 scopus 로고    scopus 로고
    • Mutations in ARFGEF2 implicate vesicle trafficking in neural progenitor proliferation and migration in the human cerebral cortex
    • V.L. Sheen Mutations in ARFGEF2 implicate vesicle trafficking in neural progenitor proliferation and migration in the human cerebral cortex Nat. Genet. 36 2004 69 76
    • (2004) Nat. Genet. , vol.36 , pp. 69-76
    • Sheen, V.L.1
  • 24
    • 0141816599 scopus 로고    scopus 로고
    • Presenilin 1 is involved in maturation and trafficking of N-cadherin to the plasma membrane
    • K. Uemura Presenilin 1 is involved in maturation and trafficking of N-cadherin to the plasma membrane J. Neurosci. Res. 74 2003 184 191
    • (2003) J. Neurosci. Res. , vol.74 , pp. 184-191
    • Uemura, K.1
  • 25
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1-γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • P. Marambaud A presenilin-1-γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions EMBO J. 21 2002 1948 1956
    • (2002) EMBO J. , vol.21 , pp. 1948-1956
    • Marambaud, P.1
  • 26
    • 1642423571 scopus 로고    scopus 로고
    • The FAM deubiquitylating enzyme localises to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and (β)-catenin
    • R.Z. Murray The FAM deubiquitylating enzyme localises to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and (β)-catenin Mol. Biol. Cell 15 2004 1591 1599
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1591-1599
    • Murray, R.Z.1
  • 27
    • 1642342675 scopus 로고    scopus 로고
    • Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells
    • P. Laprise Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells J. Biol. Chem. 279 2004 10157 10166
    • (2004) J. Biol. Chem. , vol.279 , pp. 10157-10166
    • Laprise, P.1
  • 28
    • 0037320597 scopus 로고    scopus 로고
    • Three-dimensional analysis of post-Golgi carrier exocytosis in epithelial cells
    • G. Kreitzer Three-dimensional analysis of post-Golgi carrier exocytosis in epithelial cells Nat. Cell Biol. 5 2003 126 136
    • (2003) Nat. Cell Biol. , vol.5 , pp. 126-136
    • Kreitzer, G.1
  • 29
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • K.K. Grindstaff Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells Cell 93 1998 731 740
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1
  • 30
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • W. Guo The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis EMBO J. 18 1999 1071 1080
    • (1999) EMBO J. , vol.18 , pp. 1071-1080
    • Guo, W.1
  • 31
    • 1242284588 scopus 로고    scopus 로고
    • Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells
    • C. Yeaman Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells J. Cell Sci. 117 2004 559 570
    • (2004) J. Cell Sci. , vol.117 , pp. 559-570
    • Yeaman, C.1
  • 32
    • 0029847075 scopus 로고    scopus 로고
    • Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells
    • S.H. Low Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells Mol. Biol. Cell 7 1996 2007 2018
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2007-2018
    • Low, S.H.1
  • 33
    • 0001331879 scopus 로고    scopus 로고
    • Recycling of E-cadherin: A potential mechanism for regulating cadherin dynamics
    • T.L. Le Recycling of E-cadherin: a potential mechanism for regulating cadherin dynamics J. Cell Biol. 146 1999 219 232
    • (1999) J. Cell Biol. , vol.146 , pp. 219-232
    • Le T., L.1
  • 34
    • 0347360336 scopus 로고    scopus 로고
    • Endocytosis of epithelial apical junctional proteins by a clathrin-mediated pathway into a unique storage compartment
    • A.I. Ivanov Endocytosis of epithelial apical junctional proteins by a clathrin-mediated pathway into a unique storage compartment Mol. Biol. Cell 15 2004 176 188
    • (2004) Mol. Biol. Cell , vol.15 , pp. 176-188
    • Ivanov, A.I.1
  • 35
    • 0038418651 scopus 로고    scopus 로고
    • Characterization of E-cadherin endocytosis in isolated MCF-7 and chinese hamster ovary cells: The initial fate of unbound E-cadherin
    • A.D. Paterson Characterization of E-cadherin endocytosis in isolated MCF-7 and chinese hamster ovary cells: the initial fate of unbound E-cadherin J. Biol. Chem. 278 2003 21050 21057
    • (2003) J. Biol. Chem. , vol.278 , pp. 21050-21057
    • Paterson, A.D.1
  • 36
    • 0035158750 scopus 로고    scopus 로고
    • RAC1 regulates adherens junctions through endocytosis of E-cadherin
    • N. Akhtar, and N.A. Hotchin RAC1 regulates adherens junctions through endocytosis of E-cadherin Mol. Biol. Cell 12 2001 847 862
    • (2001) Mol. Biol. Cell , vol.12 , pp. 847-862
    • Akhtar1    Hotchin, N.A.N.2
  • 37
    • 0345736990 scopus 로고    scopus 로고
    • Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of β-catenin, and enhanced tumor cell invasion
    • Z. Lu Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of β-catenin, and enhanced tumor cell invasion Cancer Cell 4 2003 499 515
    • (2003) Cancer Cell , vol.4 , pp. 499-515
    • Lu, Z.1
  • 38
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • R.G. Parton, and A.A. Richards Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms Traffic 4 2003 724 738
    • (2003) Traffic , vol.4 , pp. 724-738
    • Parton1    Richards, A.A.R.G.2
  • 40
    • 0033581834 scopus 로고    scopus 로고
    • Coendocytosis of cadherin and c-Met coupled to disruption of cell-cell adhesion in MDCK cells - Regulation by Rho, Rac and Rab small G proteins
    • T. Kamei Coendocytosis of cadherin and c-Met coupled to disruption of cell-cell adhesion in MDCK cells - regulation by Rho, Rac and Rab small G proteins Oncogene 18 1999 6776 6784
    • (1999) Oncogene , vol.18 , pp. 6776-6784
    • Kamei, T.1
  • 41
    • 0036904274 scopus 로고    scopus 로고
    • Sorting out the cellular functions of sorting nexins
    • C.A. Worby, and J.E. Dixon Sorting out the cellular functions of sorting nexins Nat. Rev. Mol. Cell Biol. 3 2002 919 931
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 919-931
    • Worby1    Dixon, J.E.C.A.2
  • 42
    • 0031573934 scopus 로고    scopus 로고
    • Characterization of the role of cadherin in regulating cell adhesion during sea urchin development
    • J.R. Miller, and D.R. McClay Characterization of the role of cadherin in regulating cell adhesion during sea urchin development Dev. Biol. 192 1997 323 339
    • (1997) Dev. Biol. , vol.192 , pp. 323-339
    • Miller1    McClay, D.R.J.R.2
  • 43
    • 0031259778 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and cadherin-catenin function
    • J.M. Daniel, and A.B. Reynolds Tyrosine phosphorylation and cadherin-catenin function Bioessays 19 1997 883 891
    • (1997) Bioessays , vol.19 , pp. 883-891
    • Daniel1    Reynolds, A.B.J.M.2
  • 44
    • 0036121308 scopus 로고    scopus 로고
    • Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex
    • Y. Fujita Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex Nat. Cell Biol. 4 2002 222 231
    • (2002) Nat. Cell Biol. , vol.4 , pp. 222-231
    • Fujita, Y.1
  • 45
    • 1042267263 scopus 로고    scopus 로고
    • Cell adhesion and signalling by cadherins and Ig-CAMs in cancer
    • U. Cavallaro, and G. Christofori Cell adhesion and signalling by cadherins and Ig-CAMs in cancer Nat. Rev. Cancer 4 2004 118 132
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 118-132
    • Cavallaro1    Christofori, G.U.2
  • 46
    • 0036781973 scopus 로고    scopus 로고
    • A signaling pathway leading to metastasis is controlled by N-cadherin and the FGF receptor
    • K. Suyama A signaling pathway leading to metastasis is controlled by N-cadherin and the FGF receptor Cancer Cell 2 2002 301 314
    • (2002) Cancer Cell , vol.2 , pp. 301-314
    • Suyama, K.1
  • 47
    • 0242456021 scopus 로고    scopus 로고
    • Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells
    • K. Xiao Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells J. Cell Biol. 163 2003 535 545
    • (2003) J. Cell Biol. , vol.163 , pp. 535-545
    • Xiao, K.1
  • 48
    • 0242708621 scopus 로고    scopus 로고
    • A core function for p120-catenin in cadherin turnover
    • M.A. Davis A core function for p120-catenin in cadherin turnover J. Cell Biol. 163 2003 525 534
    • (2003) J. Cell Biol. , vol.163 , pp. 525-534
    • Davis, M.A.1
  • 49
    • 0033784843 scopus 로고    scopus 로고
    • The transcription factor snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression
    • A. Cano The transcription factor snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression Nat. Cell Biol. 2 2000 76 83
    • (2000) Nat. Cell Biol. , vol.2 , pp. 76-83
    • Cano, A.1
  • 50
    • 0033789680 scopus 로고    scopus 로고
    • The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells
    • E. Batlle The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells Nat. Cell Biol. 2 2000 84 89
    • (2000) Nat. Cell Biol. , vol.2 , pp. 84-89
    • Batlle, E.1
  • 51
    • 0034964418 scopus 로고    scopus 로고
    • The two-handed e box binding zinc finger protein SIP1 downregulates E-cadherin and induces invasion
    • J. Comijn The two-handed E box binding zinc finger protein SIP1 downregulates E-cadherin and induces invasion Mol. Cell 7 2001 1267 1278
    • (2001) Mol. Cell , vol.7 , pp. 1267-1278
    • Comijn, J.1
  • 52
    • 0035920152 scopus 로고    scopus 로고
    • A new role for E12/E47 in the repression of E-cadherin expression and epithelial-mesenchymal transitions
    • M.A. Perez-Moreno A new role for E12/E47 in the repression of E-cadherin expression and epithelial-mesenchymal transitions J. Biol. Chem. 276 2001 27424 27431
    • (2001) J. Biol. Chem. , vol.276 , pp. 27424-27431
    • Perez-Moreno, M.A.1
  • 53
    • 0035408007 scopus 로고    scopus 로고
    • FGF signaling regulates mesoderm cell fate specification and morphogenetic movement at the primitive streak
    • B. Ciruna, and J. Rossant FGF signaling regulates mesoderm cell fate specification and morphogenetic movement at the primitive streak Dev. Cell 1 2001 37 49
    • (2001) Dev. Cell , vol.1 , pp. 37-49
    • Ciruna1    Rossant, J.B.2
  • 54
    • 0036513626 scopus 로고    scopus 로고
    • The snail superfamily of zinc-finger transcription factors
    • M.A. Nieto The snail superfamily of zinc-finger transcription factors Nat. Rev. Mol. Cell Biol. 3 2002 155 166
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 155-166
    • Nieto, M.A.1
  • 55
    • 0345599013 scopus 로고    scopus 로고
    • Autoregulation of E-cadherin expression by cadherin-cadherin interactions: The roles of β-catenin signaling, Slug, and MAPK
    • M. Conacci-Sorrell Autoregulation of E-cadherin expression by cadherin-cadherin interactions: the roles of β-catenin signaling, Slug, and MAPK J. Cell Biol. 163 2003 847 857
    • (2003) J. Cell Biol. , vol.163 , pp. 847-857
    • Conacci-Sorrell, M.1
  • 56
    • 0036356505 scopus 로고    scopus 로고
    • Dynamin-dependent endocytosis is necessary for convergent-extension movements in Xenopus animal cap explants
    • O. Jarrett Dynamin-dependent endocytosis is necessary for convergent-extension movements in Xenopus animal cap explants Int. J. Dev. Biol. 46 2002 467 473
    • (2002) Int. J. Dev. Biol. , vol.46 , pp. 467-473
    • Jarrett, O.1
  • 57
    • 0037213412 scopus 로고    scopus 로고
    • Invasion of mammalian cells by Listeria monocytogenes: Functional mimicry to subvert cellular functions
    • P. Cossart Invasion of mammalian cells by Listeria monocytogenes: functional mimicry to subvert cellular functions Trends Cell Biol. 13 2003 23 31
    • (2003) Trends Cell Biol. , vol.13 , pp. 23-31
    • Cossart, P.1
  • 58
    • 1642278077 scopus 로고    scopus 로고
    • Breaking into the epithelial apical-junctional complex - News from pathogen hackers
    • R. Vogelmann Breaking into the epithelial apical-junctional complex - news from pathogen hackers Curr. Opin. Cell Biol. 16 2004 86 93
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 86-93
    • Vogelmann, R.1
  • 59
    • 18744399547 scopus 로고    scopus 로고
    • A novel role for p120 catenin in E-cadherin function
    • R.C. Ireton A novel role for p120 catenin in E-cadherin function J. Cell Biol. 159 2002 465 476
    • (2002) J. Cell Biol. , vol.159 , pp. 465-476
    • Ireton, R.C.1
  • 60
    • 1342304120 scopus 로고    scopus 로고
    • P120 catenin associates with microtubules: Inverse relationship between microtubule binding and Rho GTPase regulation
    • C.M. Franz, and A.J. Ridley p120 catenin associates with microtubules: inverse relationship between microtubule binding and Rho GTPase regulation J. Biol. Chem. 279 2004 6588 6594
    • (2004) J. Biol. Chem. , vol.279 , pp. 6588-6594
    • Franz1    Ridley, A.J.C.M.2
  • 61
    • 1542364448 scopus 로고    scopus 로고
    • A novel interaction between kinesin and p120 modulates p120 localization and function
    • M. Yanagisawa A novel interaction between kinesin and p120 modulates p120 localization and function J. Biol. Chem. 279 2004 9512 9521
    • (2004) J. Biol. Chem. , vol.279 , pp. 9512-9521
    • Yanagisawa, M.1
  • 63
    • 0025882048 scopus 로고
    • PDGF, CSF-1, and EGF induce tyrosine phosphorylation of p120, a pp60src transformation-associated substrate
    • J.R. Downing, and A.B. Reynolds PDGF, CSF-1, and EGF induce tyrosine phosphorylation of p120, a pp60src transformation-associated substrate Oncogene 6 1991 607 613
    • (1991) Oncogene , vol.6 , pp. 607-613
    • Downing1    Reynolds, A.B.J.R.2
  • 65
    • 2342420097 scopus 로고    scopus 로고
    • EGFR signaling to p120-catenin through phosphorylation at Y228
    • D.J. Mariner EGFR signaling to p120-catenin through phosphorylation at Y228 J. Cell Sci. 117 2004 1339 1350
    • (2004) J. Cell Sci. , vol.117 , pp. 1339-1350
    • Mariner, D.J.1
  • 66
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, β-catenin, and cadherin pathways
    • W.J. Nelson, and R. Nusse Convergence of Wnt, β-catenin, and cadherin pathways Science 303 2004 1483 1487
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson1    Nusse, R.W.J.2
  • 67
    • 0033945110 scopus 로고    scopus 로고
    • Membrane traffic in polarized epithelial cells
    • K.E. Mostov Membrane traffic in polarized epithelial cells Curr. Opin. Cell Biol. 12 2000 483 490
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 483-490
    • Mostov, K.E.1
  • 68
    • 0037572145 scopus 로고    scopus 로고
    • Ezrin regulates E-cadherin-dependent adherens junction assembly through Rac1 activation
    • P. Pujuguet Ezrin regulates E-cadherin-dependent adherens junction assembly through Rac1 activation Mol. Biol. Cell 14 2003 2181 2191
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2181-2191
    • Pujuguet, P.1
  • 69
    • 1642602671 scopus 로고    scopus 로고
    • Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network
    • C. Yeaman Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network Nat. Cell Biol. 6 2004 106 112
    • (2004) Nat. Cell Biol. , vol.6 , pp. 106-112
    • Yeaman, C.1
  • 70
    • 0036076405 scopus 로고    scopus 로고
    • Protein kinase C regulates endocytosis and recycling of E-cadherin
    • T.L. Le Protein kinase C regulates endocytosis and recycling of E-cadherin Am. J. Physiol. Cell Physiol. 283 2002 C489 C499
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283
    • Le T., L.1
  • 71
    • 0036902709 scopus 로고    scopus 로고
    • ARF6-GTP recruits Nm23-H1 to facilitate dynamin-mediated endocytosis during adherens junctions disassembly
    • F. Palacios ARF6-GTP recruits Nm23-H1 to facilitate dynamin-mediated endocytosis during adherens junctions disassembly Nat. Cell Biol. 4 2002 929 936
    • (2002) Nat. Cell Biol. , vol.4 , pp. 929-936
    • Palacios, F.1
  • 72
    • 0032493903 scopus 로고    scopus 로고
    • Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin- mediated cell-cell adhesion
    • S. Kuroda Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin- mediated cell-cell adhesion Science 281 1998 832 835
    • (1998) Science , vol.281 , pp. 832-835
    • Kuroda, S.1
  • 73
    • 0035651254 scopus 로고    scopus 로고
    • Rho-family GTPases in cadherin-mediated cell-cell adhesion
    • M. Fukata, and K. Kaibuchi Rho-family GTPases in cadherin-mediated cell-cell adhesion Nat. Rev. Mol. Cell Biol. 2 2001 887 897
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 887-897
    • Fukata1    Kaibuchi, K.M.2
  • 74
    • 0034600035 scopus 로고    scopus 로고
    • Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells
    • A.J. Charron Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells J. Cell Biol. 149 2000 111 124
    • (2000) J. Cell Biol. , vol.149 , pp. 111-124
    • Charron, A.J.1
  • 75
    • 0036048217 scopus 로고    scopus 로고
    • Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling
    • E. Avizienyte Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling Nat. Cell Biol. 4 2002 632 638
    • (2002) Nat. Cell Biol. , vol.4 , pp. 632-638
    • Avizienyte, E.1
  • 76
    • 0032563564 scopus 로고    scopus 로고
    • Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein
    • C.L. Adams Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein J. Cell Biol. 142 1998 1105 1119
    • (1998) J. Cell Biol. , vol.142 , pp. 1105-1119
    • Adams, C.L.1
  • 77
    • 0030698191 scopus 로고    scopus 로고
    • Inhibition of invasion of epithelial cells by Tiam1-Rac signaling
    • P.L. Hordijk Inhibition of invasion of epithelial cells by Tiam1-Rac signaling Science 278 1997 1464 1466
    • (1997) Science , vol.278 , pp. 1464-1466
    • Hordijk, P.L.1
  • 78
    • 0033730417 scopus 로고    scopus 로고
    • Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell-cell adhesion in normal human keratinocytes
    • V.M. Braga Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell-cell adhesion in normal human keratinocytes Mol. Biol. Cell 11 2000 3703 3721
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3703-3721
    • Braga, V.M.1
  • 79
    • 0031819246 scopus 로고    scopus 로고
    • The role of cadherin endocytosis in endothelial barrier regulation: Involvement of protein kinase C and actin-cadherin interactions
    • J.S. Alexander The role of cadherin endocytosis in endothelial barrier regulation: involvement of protein kinase C and actin-cadherin interactions Inflammation 22 1998 419 433
    • (1998) Inflammation , vol.22 , pp. 419-433
    • Alexander, J.S.1
  • 80
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • A.J. Ridley Rho family proteins: coordinating cell responses Trends Cell Biol. 11 2001 471 477
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 81
    • 2642536202 scopus 로고    scopus 로고
    • Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor
    • J.D. Topp Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor J. Biol. Chem. 279 2004 24612 24623
    • (2004) J. Biol. Chem. , vol.279 , pp. 24612-24623
    • Topp, J.D.1


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