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Volumn 10, Issue 12, 2009, Pages 843-853

Integrins: Masters and slaves of endocytic transport

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOGENESIS INHIBITOR; CAVEOLIN; CILENGITIDE; CLATHRIN; INTEGRIN; LIPID; NOCODAZOLE; PROTEIN KINASE C ALPHA; RAC PROTEIN; RECEPTOR; RHO FACTOR; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; S 36578; TRASTUZUMAB; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG; VITRONECTIN RECEPTOR;

EID: 70549101138     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2799     Document Type: Review
Times cited : (423)

References (87)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. Integrins: bidirectional, allosteric signaling machines. Cell 11 0, 673-687 (2002).
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 0035575458 scopus 로고    scopus 로고
    • Integrin signaling revisited
    • Schwartz, M. A. Integrin signaling revisited. Trends Cell Biol. 11, 466-470 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 466-470
    • Schwartz, M.A.1
  • 3
    • 22544475578 scopus 로고    scopus 로고
    • Regulation of growth factor signaling and cell cycle progression by cell adhesion and adhesion-dependent changes in cellular tension
    • Walker, J. L., Fournier, A. K. & Assoian, R. K. Regulation of growth factor signaling and cell cycle progression by cell adhesion and adhesion-dependent changes in cellular tension. Cytokine Growth Factor Rev. 16, 395-405 (2005).
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 395-405
    • Walker, J.L.1    Fournier, A.K.2    Assoian, R.K.3
  • 4
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and-2 directly bind the C-terminal region of β integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger, D. S., Bouaouina, M. & Calderwood, D. A. Kindlin-1 and-2 directly bind the C-terminal region of β integrin cytoplasmic tails and exert integrin-specific activation effects. J. Biol. Chem. 284, 11485-11497 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 5
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for β2 integrin-mediated leukocyte adhesion to endothelial cells
    • Moser, M. et al. Kindlin-3 is required for β2 integrin-mediated leukocyte adhesion to endothelial cells. Nature Med. 15, 300-305 (2009).
    • (2009) Nature Med. , vol.15 , pp. 300-305
    • Moser, M.1
  • 6
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser, M., Legate, K. R., Zent, R. & Fassler, R. The tail of integrins, talin, and kindlins. Science 324, 895-899 (2009).
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 7
    • 33845987101 scopus 로고    scopus 로고
    • Structural basis of integrin activation by talin
    • Wegener, K. L. et al. Structural basis of integrin activation by talin. Cell 128, 171-182 (2007).
    • (2007) Cell , vol.128 , pp. 171-182
    • Wegener, K.L.1
  • 8
    • 44649198353 scopus 로고    scopus 로고
    • Endocytic transport of integrins during cell migration and invasion
    • Caswell, P. & Norman, J. Endocytic transport of integrins during cell migration and invasion. Trends Cell Biol. 18, 257-263 (2008).
    • (2008) Trends Cell Biol. , vol.18 , pp. 257-263
    • Caswell, P.1    Norman, J.2
  • 9
    • 33645515261 scopus 로고    scopus 로고
    • Integrin trafficking and the control of cell migration
    • Caswell, P. T. & Norman, J. C. Integrin trafficking and the control of cell migration. Traffic 7, 14-21 (2006).
    • (2006) Traffic , vol.7 , pp. 14-21
    • Caswell, P.T.1    Norman, J.C.2
  • 10
    • 33748466150 scopus 로고    scopus 로고
    • Endocytic recycling pathways: Emerging regulators of cell migration
    • Jones, M. C., Caswell, P. T. & Norman, J. C. Endocytic recycling pathways: emerging regulators of cell migration. Curr. Opin. Cell Biol. 18, 549-557 (2006).
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 549-557
    • Jones, M.C.1    Caswell, P.T.2    Norman, J.C.3
  • 11
    • 33750339742 scopus 로고    scopus 로고
    • Integrin traffic
    • Pellinen, T. & Ivaska, J. Integrin traffic. J. Cell Sci. 1 1 9, 3723-3731 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 3723-3731
    • Pellinen, T.1    Ivaska, J.2
  • 12
    • 0030014148 scopus 로고    scopus 로고
    • Moving membrane up to the front of migrating cells
    • Bretscher, M. S. Moving membrane up to the front of migrating cells. Cell 85, 465-467 (1996).
    • (1996) Cell , vol.85 , pp. 465-467
    • Bretscher, M.S.1
  • 13
    • 51449087302 scopus 로고    scopus 로고
    • Integrin trafficking regulated by Rab21 is necessary for cytokinesis
    • Pellinen, T. et al. Integrin trafficking regulated by Rab21 is necessary for cytokinesis. Dev. Cell 15, 371-385 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 371-385
    • Pellinen, T.1
  • 14
    • 34848816931 scopus 로고    scopus 로고
    • Rab25 associates with α5β1 integrin to promote invasive migration in 3D microenvironments
    • Caswell, P. T. et al. Rab25 associates with α5β1 integrin to promote invasive migration in 3D microenvironments. Dev. Cell 13, 496-510 (2007).
    • (2007) Dev. Cell , vol.13 , pp. 496-510
    • Caswell, P.T.1
  • 15
    • 34248226275 scopus 로고    scopus 로고
    • αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration
    • White, D. P., Caswell, P. T. & Norman, J. C. αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration. J. Cell Biol. 177, 515-525 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 515-525
    • White, D.P.1    Caswell, P.T.2    Norman, J.C.3
  • 16
    • 53749092962 scopus 로고    scopus 로고
    • Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments
    • Caswell, P. T. et al. Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments. J. Cell Biol. 183, 143-155 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 143-155
    • Caswell, P.T.1
  • 17
    • 64149106522 scopus 로고    scopus 로고
    • Stimulation of tumor growth and angiogenesis by low concentrations of RGD-mimetic integrin inhibitors
    • Reynolds, A. R. et al. Stimulation of tumor growth and angiogenesis by low concentrations of RGD-mimetic integrin inhibitors. Nature Med. 15, 392-400 (2009).
    • (2009) Nature Med. , vol.15 , pp. 392-400
    • Reynolds, A.R.1
  • 18
    • 49649095969 scopus 로고    scopus 로고
    • Caveolin-1-dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover
    • Shi, F. & Sottile, J. Caveolin-1-dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover. J. Cell Sci. 121, 2360-2371 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2360-2371
    • Shi, F.1    Sottile, J.2
  • 19
    • 0742323005 scopus 로고    scopus 로고
    • Caveolae are a novel pathway for membrane-type 1 matrix metalloproteinase traffic in human endothelial cells
    • Galvez, B. G. et al. Caveolae are a novel pathway for membrane-type 1 matrix metalloproteinase traffic in human endothelial cells. Mol. Biol. Cell 15, 678-687 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 678-687
    • Galvez, B.G.1    Al, E.2
  • 20
    • 34250820373 scopus 로고    scopus 로고
    • Numb controls integrin endocytosis for directional cell migration with aPKC and PAR-3
    • Nishimura, T. & Kaibuchi, K. Numb controls integrin endocytosis for directional cell migration with aPKC and PAR-3. Dev. Cell 13, 15-28 (2007).
    • (2007) Dev. Cell , vol.13 , pp. 15-28
    • Nishimura, T.1    Kaibuchi, K.2
  • 22
    • 3543047295 scopus 로고    scopus 로고
    • Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells
    • Ortiz, D. F. et al. Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells. J. Biol. Chem. 279, 32761-32770 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 32761-32770
    • Ortiz, D.F.1    Al, E.2
  • 23
    • 34347230941 scopus 로고    scopus 로고
    • HS1-associated protein X-1 regulates carcinoma cell migration and invasion via clathrin-mediated endocytosis of integrin αvβ6
    • Ramsay, A. G. et al. HS1-associated protein X-1 regulates carcinoma cell migration and invasion via clathrin-mediated endocytosis of integrin αvβ6. Cancer Res. 67, 5275-5284 (2007).
    • (2007) Cancer Res. , vol.67 , pp. 5275-5284
    • Ramsay, A.G.1
  • 24
    • 0037418244 scopus 로고    scopus 로고
    • Integrin β cytoplasmic domain interactions with phosphotyrosine- binding domains: A structural prototype for diversity in integrin signaling
    • Calderwood, D. A. et al. Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: a structural prototype for diversity in integrin signaling. Proc. Natl Acad. Sci. USA 100, 2272-2277 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2272-2277
    • Calderwood, D.A.1    Al, E.2
  • 25
    • 64049099993 scopus 로고    scopus 로고
    • Focal adhesion disassembly requires clathrin-dependent endocytosis of integrins
    • Chao, W. T. & Kunz, J. Focal adhesion disassembly requires clathrin-dependent endocytosis of integrins. FEBS Lett. 583, 1337-1343 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 1337-1343
    • Chao, W.T.1    Kunz, J.2
  • 26
    • 67650435126 scopus 로고    scopus 로고
    • Quantitative proteomics identifies a Dab2/integrin module regulating cell migration
    • Teckchandani, A. et al. Quantitative proteomics identifies a Dab2/integrin module regulating cell migration. J. Cell Biol. 186, 99-111 (2009).
    • (2009) J. Cell Biol. , vol.186 , pp. 99-111
    • Teckchandani, A.1
  • 27
    • 20444370219 scopus 로고    scopus 로고
    • Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase
    • Ezratty, E. J., Partridge, M. A. & Gundersen, G. G. Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase. Nature Cell Biol. 7, 581-590 (2005).
    • (2005) Nature Cell Biol. , vol.7 , pp. 581-590
    • Ezratty, E.J.1    Partridge, M.A.2    Gundersen, G.G.3
  • 28
    • 58849090461 scopus 로고    scopus 로고
    • Neuropilin-1/GIPC1 signaling regulates α5β1 integrin traffic and function in endothelial cells
    • Valdembri, D. et al. Neuropilin-1/GIPC1 signaling regulates α5β1 integrin traffic and function in endothelial cells. PLoS Biol. 7, e25 (2009).
    • (2009) PLoS Biol. , vol.7
    • Valdembri, D.1
  • 29
    • 0034688995 scopus 로고    scopus 로고
    • Determination of cell adhesion sites of neuropilin-1
    • Shimizu, M., Murakami, Y., Suto, F. & Fujisawa, H. Determination of cell adhesion sites of neuropilin-1. J. Cell Biol. 148, 1283-1293 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 1283-1293
    • Shimizu, M.1    Murakami, Y.2    Suto, F.3    Fujisawa, H.4
  • 31
    • 0032549799 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
    • Soker, S., Takashima, S., Miao, H. Q., Neufeld, G. & Klagsbrun, M. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell 92, 735-745 (1998).
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 32
    • 33748077106 scopus 로고    scopus 로고
    • Binding of internalized receptors to the PDZ domain of GIPC/synectin recruits myosin VI to endocytic vesicles
    • Naccache, S. N., Hasson, T. & Horowitz, A. Binding of internalized receptors to the PDZ domain of GIPC/synectin recruits myosin VI to endocytic vesicles. Proc. Natl Acad. Sci. USA 103, 12735-12740 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12735-12740
    • Naccache, S.N.1    Hasson, T.2    Horowitz, A.3
  • 33
    • 53249096017 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and semaphorin induce neuropilin-1 endocytosis via separate pathways
    • Salikhova, A. et al. Vascular endothelial growth factor and semaphorin induce neuropilin-1 endocytosis via separate pathways. Circ. Res. 103, e71-e79 (2008).
    • (2008) Circ. Res. , vol.103
    • Salikhova, A.1    Al, E.2
  • 34
    • 48549088895 scopus 로고    scopus 로고
    • Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • Sigismund, S. et al. Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Dev. Cell 15, 209-219 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 209-219
    • Sigismund, S.1
  • 35
    • 0033565261 scopus 로고    scopus 로고
    • PKCα regulates β1 integrin-dependent cell motility through association and control of integrin traffic
    • Ng, T. et al. PKCα regulates β1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J. 18, 3909-3923 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3909-3923
    • Ng, T.1
  • 36
    • 0742305342 scopus 로고    scopus 로고
    • Clustering induces a lateral redistribution of α2β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization
    • Upla, P. et al. Clustering induces a lateral redistribution of α2β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization. Mol. Biol. Cell 15, 625-636 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 625-636
    • Upla, P.1    Al, E.2
  • 37
    • 28644449881 scopus 로고    scopus 로고
    • 2 integrin, LFA-1, during leukocyte chemotaxis
    • Fabbri, M. et al. Dynamic partitioning into lipid rafts controls the endo-exocytic cycle of the αL/β2 integrin, LFA-1, during leukocyte chemotaxis. Mol. Biol. Cell 16, 5793-5803 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5793-5803
    • Fabbri, M.1
  • 38
    • 0033568213 scopus 로고    scopus 로고
    • A tyrosine-based sorting signal in the β2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand-supported migration
    • Fabbri, M. et al. A tyrosine-based sorting signal in the β2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand-supported migration. EMBO J. 18, 4915-4925 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4915-4925
    • Fabbri, M.1
  • 39
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • Valdez-Taubas, J. & Pelham, H. R. Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling. Curr. Biol. 13, 1636-1640 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.2
  • 40
    • 22944455544 scopus 로고    scopus 로고
    • Regulators of endocytosis maintain localized receptor tyrosine kinase signaling in guided migration
    • Jekely, G., Sung, H. H., Luque, C. M. & Rorth, P. Regulators of endocytosis maintain localized receptor tyrosine kinase signaling in guided migration. Dev. Cell 9, 197-207 (2005).
    • (2005) Dev. Cell , vol.9 , pp. 197-207
    • Jekely, G.1    Sung, H.H.2    Luque, C.M.3    Rorth, P.4
  • 41
    • 46149125934 scopus 로고    scopus 로고
    • Endocytic trafficking of Rac is required for the spatial restriction of signaling in cell migration
    • Palamidessi, A. et al. Endocytic trafficking of Rac is required for the spatial restriction of signaling in cell migration. Cell 134, 135-147 (2008).
    • (2008) Cell , vol.134 , pp. 135-147
    • Palamidessi, A.1
  • 42
    • 0034656322 scopus 로고    scopus 로고
    • Oriented endocytic recycling of α5β1 in motile neutrophils
    • Pierini, L. M., Lawson, M. A., Eddy, R. J., Hendey, B. & Maxfield, F. R. Oriented endocytic recycling of α5β1 in motile neutrophils. Blood 95, 2471-2480 (2000).
    • (2000) Blood , vol.95 , pp. 2471-2480
    • Pierini, L.M.1    Lawson, M.A.2    Eddy, R.J.3    Hendey, B.4    Maxfield, F.R.5
  • 43
    • 0037350449 scopus 로고    scopus 로고
    • Real-time analysis of clathrin-mediated endocytosis during cell migration
    • Rappoport, J. Z. & Simon, S. M. Real-time analysis of clathrin-mediated endocytosis during cell migration. J. Cell Sci. 11 6, 847-855 (2003).
    • (2003) J. Cell Sci. , vol.11 , Issue.6 , pp. 847-855
    • Rappoport, J.Z.1    Simon, S.M.2
  • 44
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis, C. M., Webb, D. J., Donais, K. & Horwitz, A. F. Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells. J. Cell Biol. 153, 1427-1440 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1427-1440
    • Laukaitis, C.M.1    Webb, D.J.2    Donais, K.3    Horwitz, A.F.4
  • 45
    • 0028339264 scopus 로고
    • In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella
    • Hopkins, C. R., Gibson, A., Shipman, M., Strickland, D. K. & Trowbridge, I. S. In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella. J. Cell Biol. 125, 1265-1274 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 1265-1274
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Strickland, D.K.4    Trowbridge, I.S.5
  • 46
    • 1142269809 scopus 로고    scopus 로고
    • Protein kinase D-mediated anterograde membrane trafficking is required for fibroblast motility
    • Prigozhina, N. L. & Waterman-Storer, C. M. Protein kinase D-mediated anterograde membrane trafficking is required for fibroblast motility. Curr. Biol. 14, 88-98 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 88-98
    • Prigozhina, N.L.1    Waterman-Storer, C.M.2
  • 47
    • 0344034726 scopus 로고    scopus 로고
    • Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge
    • Schmoranzer, J., Kreitzer, G. & Simon, S. M. Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge. J. Cell Sci. 1 1 6, 4513-4519 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 4513-4519
    • Schmoranzer, J.1    Kreitzer, G.2    Simon, S.M.3
  • 48
    • 33747447033 scopus 로고    scopus 로고
    • Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of β1-integrins
    • Pellinen, T. et al. Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of β1-integrins. J. Cell Biol. 173, 767-780 (2006).
    • (2006) J. Cell Biol. , vol.173 , pp. 767-780
    • Pellinen, T.1
  • 49
    • 0344305784 scopus 로고    scopus 로고
    • Cell migration: Integrating signals from front to back
    • Ridley, A. J. et al. Cell migration: integrating signals from front to back. Science 302, 1704-1709 (2003).
    • (2003) Science , vol.302 , pp. 1704-1709
    • Ridley, A.J.1
  • 50
    • 24144458264 scopus 로고    scopus 로고
    • A Rac switch regulates random versus directionally persistent cell migration
    • Pankov, R. et al. A Rac switch regulates random versus directionally persistent cell migration. J. Cell Biol. 170, 793-802 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 793-802
    • Pankov, R.1
  • 51
    • 33750337537 scopus 로고    scopus 로고
    • Endosomes generate localized Rho-ROCK-MLC2-based contractile signals via Endo180 to promote adhesion disassembly
    • Sturge, J., Wienke, D. & Isacke, C. M. Endosomes generate localized Rho-ROCK-MLC2-based contractile signals via Endo180 to promote adhesion disassembly. J. Cell Biol. 175, 337-347 (2006).
    • (2006) J. Cell Biol. , vol.175 , pp. 337-347
    • Sturge, J.1    Wienke, D.2    Isacke, C.M.3
  • 52
    • 18844424325 scopus 로고    scopus 로고
    • Integrins control motile strategy through a Rho-cofilin pathway
    • Danen, E. H. et al. Integrins control motile strategy through a Rho-cofilin pathway. J. Cell Biol. 169, 515-526 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 515-526
    • Danen, E.H.1
  • 53
    • 22244473991 scopus 로고    scopus 로고
    • A microtubule-dependent zone of active RhoA during cleavage plane specification
    • Bement, W. M., Benink, H. A. & von Dassow, G. A microtubule-dependent zone of active RhoA during cleavage plane specification. J. Cell Biol. 170, 91-101 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 91-101
    • Bement, W.M.1    Benink, H.A.2    Von Dassow, G.3
  • 54
    • 19944433788 scopus 로고    scopus 로고
    • The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis
    • Wilson, G. M. et al. The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis. Mol. Biol. Cell 16, 849-860 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 849-860
    • Wilson, G.M.1    Al, E.2
  • 55
    • 48249110666 scopus 로고    scopus 로고
    • Nuf a Rab11 effector, maintains cytokinetic furrow integrity by promoting local actin polymerization
    • Cao, J., Albertson, R., Riggs, B., Field, C. M. & Sullivan, W. Nuf, a Rab11 effector, maintains cytokinetic furrow integrity by promoting local actin polymerization. J. Cell Biol. 182, 301-313 (2008).
    • (2008) J. Cell Biol. , vol.182 , pp. 301-313
    • Cao, J.1    Albertson, R.2    Riggs, B.3    Field, C.M.4    Sullivan, W.5
  • 56
    • 33644858630 scopus 로고    scopus 로고
    • Rho GTPases in animal cell mitosis
    • Narumiya, S. & Yasuda, S. Rho GTPases in animal cell mitosis. Curr. Opin. Cell Biol. 18, 199-205 (2006).
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 199-205
    • Narumiya, S.1    Yasuda, S.2
  • 57
    • 0842331441 scopus 로고    scopus 로고
    • Integrins regulate Rac targeting by internalization of membrane domains
    • del Pozo, M. A. et al. Integrins regulate Rac targeting by internalization of membrane domains. Science 303, 839-842 (2004).
    • (2004) Science , vol.303 , pp. 839-842
    • Del Pozo, M.A.1
  • 58
    • 26944437142 scopus 로고    scopus 로고
    • Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization
    • del Pozo, M. A. et al. Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization. Nature Cell Biol. 7, 901-908 (2005).
    • (2005) Nature Cell Biol. , vol.7 , pp. 901-908
    • Del Pozo, M.A.1
  • 60
    • 0842333243 scopus 로고    scopus 로고
    • αvβ3 and αvβ5 integrin antagonists inhibit angiogenesis in vitro
    • Nisato, R. E., Tille, J. C., Jonczyk, A., Goodman, S. L. & Pepper, M. S. αvβ3 and αvβ5 integrin antagonists inhibit angiogenesis in vitro. Angiogenesis 6, 105-119 (2003).
    • (2003) Angiogenesis , vol.6 , pp. 105-119
    • Nisato, R.E.1    Tille, J.C.2    Jonczyk, A.3    Goodman, S.L.4    Pepper, M.S.5
  • 61
    • 33751191637 scopus 로고    scopus 로고
    • Blockade of αvβ3 and αvβ5 integrins by RGD mimetics induces anoikis and not integrin-mediated death in human endothelial cells
    • Maubant, S. et al. Blockade of αvβ3 and αvβ5 integrins by RGD mimetics induces anoikis and not integrin-mediated death in human endothelial cells. Blood 108, 3035-3044 (2006).
    • (2006) Blood , vol.108 , pp. 3035-3044
    • Maubant, S.1
  • 62
    • 34249113455 scopus 로고    scopus 로고
    • Integrin inhibitors reaching the clinic
    • Stupp, R. & Ruegg, C. Integrin inhibitors reaching the clinic. J. Clin. Oncol. 25, 1637-1638 (2007)
    • (2007) J. Clin. Oncol. , vol.25 , pp. 1637-1638
    • Stupp, R.1    Ruegg, C.2
  • 63
    • 33645551144 scopus 로고    scopus 로고
    • Integrins: Molecular targets in cancer therapy
    • Tucker, G. C. Integrins: molecular targets in cancer therapy. Curr. Oncol. Rep. 8, 96-103 (2006).
    • (2006) Curr. Oncol. Rep. , vol.8 , pp. 96-103
    • Tucker, G.C.1
  • 64
    • 0033549864 scopus 로고    scopus 로고
    • N-methylated cyclic RGD peptides as highly active and selective αvβ3 integrin antagonists
    • Dechantsreiter, M. A. et al. N-methylated cyclic RGD peptides as highly active and selective αVβ3 integrin antagonists. J. Med. Chem. 42, 3033-3040 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 3033-3040
    • Dechantsreiter, M.A.1    Al, E.2
  • 65
    • 0036152857 scopus 로고    scopus 로고
    • Enhanced pathological angiogenesis in mice lacking β3 integrin or β3 and β5 integrins
    • Reynolds, L. E. et al. Enhanced pathological angiogenesis in mice lacking β3 integrin or β3 and β5 integrins. Nature Med. 8, 27-34 (2002).
    • (2002) Nature Med. , vol.8 , pp. 27-34
    • Reynolds, L.E.1
  • 66
    • 29144488505 scopus 로고    scopus 로고
    • Distinct roles of Akt1 and Akt2 in regulating cell migration and epithelial-mesenchymal transition
    • Irie, H. Y. et al. Distinct roles of Akt1 and Akt2 in regulating cell migration and epithelial-mesenchymal transition. J. Cell Biol. 171, 1023-1034 (2005).
    • (2005) J. Cell Biol. , vol.171 , pp. 1023-1034
    • Irie, H.Y.1
  • 67
    • 68849092564 scopus 로고    scopus 로고
    • Genomic amplicons target vesicle recycling in breast cancer
    • Mills, G. B., Jurisica, I., Yarden, Y. & Norman, J. C. Genomic amplicons target vesicle recycling in breast cancer. J. Clin. Invest. 11 9, 2123-2127 (2009).
    • (2009) J. Clin. Invest. , vol.11 , Issue.9 , pp. 2123-2127
    • Mills, G.B.1    Jurisica, I.2    Yarden, Y.3    Norman, J.C.4
  • 68
    • 68849084073 scopus 로고    scopus 로고
    • RCP is a human breast cancer-promoting gene with Ras-activating function
    • Zhang, J. et al. RCP is a human breast cancer-promoting gene with Ras-activating function. J. Clin. Invest. 119, 2171-2183 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 2171-2183
    • Zhang, J.1    Al, E.2
  • 69
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C. et al. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1
  • 70
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of a5(31 integrins promotes early fibronectin fibrillogenesis
    • Pankov, R. et al. Integrin dynamics and matrix assembly: tensin-dependent translocation of a5(31 integrins promotes early fibronectin fibrillogenesis. J. Cell Biol. 148, 1075-1090 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 1075-1090
    • Pankov, R.1    Al, E.2
  • 71
    • 65749084249 scopus 로고    scopus 로고
    • VEGFR1 (Flt1) regulates Rab4 recycling to control fibronectin polymerization and endothelial vessel branching
    • Jones, M. C. et al. VEGFR1 (Flt1) regulates Rab4 recycling to control fibronectin polymerization and endothelial vessel branching. Traffic 10, 754-766 (2009).
    • (2009) Traffic , vol.10 , pp. 754-766
    • Jones, M.C.1
  • 72
    • 0038141338 scopus 로고    scopus 로고
    • Fibronectin requirement in branching morphogenesis
    • Sakai, T., Larsen, M. & Yamada, K. M. Fibronectin requirement in branching morphogenesis. Nature 423, 876-881 (2003).
    • (2003) Nature , vol.423 , pp. 876-881
    • Sakai, T.1    Larsen, M.2    Yamada, K.M.3
  • 73
    • 66149100509 scopus 로고    scopus 로고
    • Real-time study of E-cadherin and membrane dynamics in living animals: Implications for disease modeling and drug development
    • Serrels, A. et al. Real-time study of E-cadherin and membrane dynamics in living animals: implications for disease modeling and drug development. Cancer Res. 69, 2714-2719 (2009).
    • (2009) Cancer Res. , vol.69 , pp. 2714-2719
    • Serrels, A.1
  • 74
    • 0031755756 scopus 로고    scopus 로고
    • The vitronectin receptor associates with clathrin-coated membrane domains via the cytoplasmic domain of its (35 subunit)
    • De Deyne, P. G. et al. The vitronectin receptor associates with clathrin-coated membrane domains via the cytoplasmic domain of its (35 subunit J. Cell Sci. 111, 2729-2740 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 2729-2740
    • De Deyne, P.G.1    Al, E.2
  • 75
    • 35748975965 scopus 로고    scopus 로고
    • Tetraspanin CD151 promotes cell migration by regulating integrin trafficking
    • Liu, L. et al. Tetraspanin CD151 promotes cell migration by regulating integrin trafficking. J. Biol. Chem. 282, 31631-31642 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 31631-31642
    • Liu, L.1    Al, E.2
  • 76
    • 29144457439 scopus 로고    scopus 로고
    • Endocytosis of (31 integrins is an early event in migration promoted by the cell adhesion molecule L1
    • Panicker, A. K., Buhusi, M., Erickson, A. & Maness, P. F Endocytosis of (31 integrins is an early event in migration promoted by the cell adhesion molecule L1. Exp. Cell Res. 312, 299-307 (2006).
    • (2006) Exp. Cell Res. , vol.312 , pp. 299-307
    • Panicker, A.K.1    Buhusi, M.2    Erickson, A.3    Maness, P.F.4
  • 77
    • 18444412912 scopus 로고    scopus 로고
    • Site-directed perturbation of protein kinase C-integrin interaction blocks carcinoma cell chemotaxis
    • Parsons, M. et al. Site-directed perturbation of protein kinase C-integrin interaction blocks carcinoma cell chemotaxis. Mol. Cell. Biol. 22, 5897-5911 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5897-5911
    • Parsons, M.1    Al, E.2
  • 78
    • 0028925156 scopus 로고
    • Fibronectin receptor internalization and AP-2 complex reorganization in potassium-depleted fibroblasts
    • Altankov, G. & Grinnell, F Fibronectin receptor internalization and AP-2 complex reorganization in potassium-depleted fibroblasts. Exp. Cell Res. 216, 299-309 (1995).
    • (1995) Exp. Cell Res. , vol.216 , pp. 299-309
    • Altankov, G.1    Grinnell, F.2
  • 79
    • 61949276292 scopus 로고    scopus 로고
    • JAM-A promotes neutrophil chemotaxis by controlling integrin internalization and recycling
    • Cera, M. R. et al. JAM-A promotes neutrophil chemotaxis by controlling integrin internalization and recycling. J. Cell Sci. 122, 268-277 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 268-277
    • Cera, M.R.1
  • 80
    • 31944442964 scopus 로고    scopus 로고
    • The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of (31 integrins)
    • Dunphy, J. L. et al. The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of (31 integrins. Curr. Biol. 16, 315-320 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 315-320
    • Dunphy, J.L.1    Al, E.2
  • 81
    • 3342906957 scopus 로고    scopus 로고
    • PKD1/PKC|a promotes av(33 integrin recycling and delivery to nascent focal adhesions
    • Woods, A. J., White, D. P., Caswell, P. T & Norman, J. C. PKD1/PKC|a promotes av(33 integrin recycling and delivery to nascent focal adhesions. EMBO J. 23, 2531-2543 (2004).
    • (2004) EMBO J. , vol.23 , pp. 2531-2543
    • Woods, A.J.1    White, D.P.2    Caswell, P.T.3    Norman, J.C.4
  • 82
    • 33846002380 scopus 로고    scopus 로고
    • The Rab4A effector protein Rabip4 is involved in migration of NIH 3T3 fibroblasts
    • Vukmirica, J., Monzo, P., Le Marchand-Brustel, Y. & Cormont, M. The Rab4A effector protein Rabip4 is involved in migration of NIH 3T3 fibroblasts. J. Biol. Chem. 281, 36360-36368 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 36360-36368
    • Vukmirica, J.1    Monzo, P.2    Le Marchand-Brustel, Y.3    Cormont, M.4
  • 83
    • 27844444696 scopus 로고    scopus 로고
    • PKCs-mediated phosphorylation of vimentin controls integrin recycling and motility
    • Ivaska, J. et al. PKCs-mediated phosphorylation of vimentin controls integrin recycling and motility. EMBO J. 24, 3834-3845 (2005).
    • (2005) EMBO J. , vol.24 , pp. 3834-3845
    • Ivaska, J.1
  • 84
    • 0037099313 scopus 로고    scopus 로고
    • PKCs controls the traffic of (31 integrins in motile cells
    • Ivaska, J., Whelan, R. D., Watson, R. & Parker, P. J. PKCs controls the traffic of (31 integrins in motile cells. EMBO J. 21, 3608-3619 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3608-3619
    • Ivaska, J.1    Whelan, R.D.2    Watson, R.3    Parker, P.J.4
  • 85
    • 34047155597 scopus 로고    scopus 로고
    • EHD1 regulates (31 integrin endosomal transport: Effects on focal adhesions, cell spreading and migration
    • Jovic, M., Naslavsky, N., Rapaport, D., Horowitz, M. & Caplan, S. EHD1 regulates (31 integrin endosomal transport: effects on focal adhesions, cell spreading and migration. J. Cell Sci. 120, 802-814 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 802-814
    • Jovic, M.1    Naslavsky, N.2    Rapaport, D.3    Horowitz, M.4    Caplan, S.5
  • 86
    • 15044350673 scopus 로고    scopus 로고
    • Inhibition of SNARE-mediated membrane traffic impairs cell migration
    • Tayeb, M. A. et al. Inhibition of SNARE-mediated membrane traffic impairs cell migration. Exp. Cell Res. 305, 63-73 (2005).
    • (2005) Exp. Cell Res. , vol.305 , pp. 63-73
    • Tayeb, M.A.1    Al, E.2
  • 87
    • 27644528406 scopus 로고    scopus 로고
    • Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin (31 to control cell migration
    • Li, J. et al. Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin (31 to control cell migration. Dev. Cell 9, 663-673 (2005).
    • (2005) Dev. Cell , vol.9 , pp. 663-673
    • Li, J.1    Al, E.2


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