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Volumn 63, Issue 11, 2011, Pages 1009-1017

Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling

Author keywords

Actin cytoskeleton; Annexin A6; Calcium mediated signaling; Cholesterol; Epidermal growth factor; Membrane domains; T cell activation

Indexed keywords

ANNEXIN; CALCIUM CHANNEL; CALCIUM ION; CALPHOBINDIN II; CHOLESTEROL; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; F ACTIN; PHOSPHOLIPID; T LYMPHOCYTE RECEPTOR;

EID: 84055193693     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.540     Document Type: Review
Times cited : (50)

References (124)
  • 2
    • 0030700638 scopus 로고    scopus 로고
    • Identification of cytoskeleton-associated proteins in isolated rat liver endosomes
    • Pol, A., Ortega, D., and Enrich, C. (1997) Identification of cytoskeleton-associated proteins in isolated rat liver endosomes. Biochem. J. 327 (Pt 3), 741-746. (Pubitemid 27487680)
    • (1997) Biochemical Journal , vol.327 , Issue.3 , pp. 741-746
    • Pol, A.1    Ortega, D.2    Enrich, C.3
  • 8
    • 0025120226 scopus 로고
    • 2+-binding protein
    • DOI 10.1016/0014-5793(90)80576-5
    • Moss, S. E. and Crumpton, M. J. (1990) Alternative splicing gives rise to two forms of the p68 Ca2 (+)-binding protein. FEBS Lett. 261, 299-302. (Pubitemid 20074978)
    • (1990) FEBS Letters , vol.261 , Issue.2 , pp. 299-302
    • Moss, S.E.1    Crumpton, M.J.2
  • 10
    • 0028844289 scopus 로고
    • Functional and genetic analysis of annexin VI
    • Edwards, H. C. and Moss, S. E. (1995) Functional and genetic analysis of annexin VI. Mol. Cell. Biochem. 149-150, 293-299.
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 293-299
    • Edwards, H.C.1    Moss, S.E.2
  • 12
    • 77957120846 scopus 로고    scopus 로고
    • Role of annexin A6 isoforms in catecholamine secretion by PC12 cells: Distinct influence on calcium response
    • Podszywalow-Bartnicka, P., Kosiorek, M., Piwocka, K., Sikora, E., Zablocki, K., and Pikula, S. (2010) Role of annexin A6 isoforms in catecholamine secretion by PC12 cells: distinct influence on calcium response. J. Cell. Biochem. 111, 168-178.
    • (2010) J. Cell. Biochem. , vol.111 , pp. 168-178
    • Podszywalow-Bartnicka, P.1    Kosiorek, M.2    Piwocka, K.3    Sikora, E.4    Zablocki, K.5    Pikula, S.6
  • 13
    • 0025909529 scopus 로고
    • Ca (2+)-dependent phospholipid and arachidonic acid binding by the placental annexins VI and IV
    • Edwards, H. C. and Crumpton, M. J. (1991) Ca (2+)-dependent phospholipid and arachidonic acid binding by the placental annexins VI and IV. Eur. J. Biochem. 198, 121-129.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 121-129
    • Edwards, H.C.1    Crumpton, M.J.2
  • 15
    • 4143070134 scopus 로고    scopus 로고
    • Structure of human annexin A6 at the air-water interface and in a membrane-bound state
    • DOI 10.1529/biophysj.103.038240
    • Golczak, M., Kirilenko, A., Bandorowicz-Pikula, J., Desbat, B., and Pikula, S. (2004) Structure of human annexin A6 at the air-water interface and in a membrane-bound state. Biophys. J. 87, 1215-1226. (Pubitemid 39095098)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1215-1226
    • Golczak, M.1    Kirilenko, A.2    Bandorowicz-Pikula, J.3    Desbat, B.4    Pikula, S.5
  • 19
    • 0034721867 scopus 로고    scopus 로고
    • Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment
    • Grewal, T., Heeren, J., Mewawala, D., Schnitgerhans, T., Wendt, D., Salomon, G., Enrich, C., Beisiegel, U., and Jäckle, S. (2000) Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment. J. Biol. Chem. 275, 33806-33813.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33806-33813
    • Grewal, T.1    Heeren, J.2    Mewawala, D.3    Schnitgerhans, T.4    Wendt, D.5    Salomon, G.6    Enrich, C.7    Beisiegel, U.8    Jäckle, S.9
  • 20
    • 77649338648 scopus 로고    scopus 로고
    • Annexin A6-regulator of the EGFR/Ras signalling pathway and cholesterol homeostasis
    • Grewal, T., Koese, M., Rentero, C., and Enrich, C. (2010) Annexin A6-regulator of the EGFR/Ras signalling pathway and cholesterol homeostasis. Int. J. Biochem. Cell Biol. 42, 580-584.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 580-584
    • Grewal, T.1    Koese, M.2    Rentero, C.3    Enrich, C.4
  • 21
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. and Simons, K. (2010) Lipid rafts as a membrane-organizing principle. Science 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 22
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: A report on the Keystone symposium on lipid rafts and cell function
    • DOI 10.1194/jlr.E600002-JLR200
    • Pike, L. J. (2006) Rafts defined: a report on the keystone symposium on lipid rafts and cell function. J. Lipid Res. 47, 1597-1598. (Pubitemid 44079915)
    • (2006) Journal of Lipid Research , vol.47 , Issue.7 , pp. 1597-1598
    • Pike, L.J.1
  • 23
    • 62049084949 scopus 로고    scopus 로고
    • Accumulation of raft lipids in T-cell plasma membrane domains engaged in TCR signalling
    • Zech, T., Ejsing, C. S., Gaus, K., de Wet, B., Shevchenko, A., Simons, K., and Harder, T. (2009) Accumulation of raft lipids in T-cell plasma membrane domains engaged in TCR signalling EMBO J. 28, 466-476.
    • (2009) EMBO J. , vol.28 , pp. 466-476
    • Zech, T.1    Ejsing, C.S.2    Gaus, K.3    De Wet, B.4    Shevchenko, A.5    Simons, K.6    Harder, T.7
  • 24
    • 0033778020 scopus 로고    scopus 로고
    • Biochemical analysis of a caveolaeenriched plasma membrane fraction from rat liver
    • Calvo, M. and Enrich, C. (2000) Biochemical analysis of a caveolaeenriched plasma membrane fraction from rat liver. Electrophoresis 21, 3386-3395.
    • (2000) Electrophoresis , vol.21 , pp. 3386-3395
    • Calvo, M.1    Enrich, C.2
  • 25
    • 1042291979 scopus 로고    scopus 로고
    • Comparative proteomics of human endothelial cell caveolae and rafts using two-dimensional gel electrophoresis and mass spectrometry
    • DOI 10.1002/elps.200305675
    • Sprenger, R. R., Speijer, D., Back, J. W., De Koster, C. G., Pannekoek, H., and Horrevoets, A. J. G. (2004) Comparative proteomics of human endothelial cell caveolae and rafts using two-dimensional gel electrophoresis and mass spectrometry. Electrophoresis 25, 156-172. (Pubitemid 38196135)
    • (2004) Electrophoresis , vol.25 , Issue.1 , pp. 156-172
    • Sprenger, R.R.1    Speijer, D.2    Back, J.W.3    De Koster, C.G.4    Pannekoek, H.5    Horrevoets, A.J.G.6
  • 26
    • 0034605044 scopus 로고    scopus 로고
    • Annexins in cell membrane dynamics. Ca (2+)-regulated association of lipid microdomains
    • Babiychuk, E. B. and Draeger, A. (2000) Annexins in cell membrane dynamics. Ca (2+)-regulated association of lipid microdomains. J. Cell Biol. 150, 1113-1124.
    • (2000) J. Cell Biol. , vol.150 , pp. 1113-1124
    • Babiychuk, E.B.1    Draeger, A.2
  • 28
    • 0035339832 scopus 로고    scopus 로고
    • Calcium-dependent association of annexin VI, protein kinase Cα, and neurocalcinα on the raft fraction derived from the synaptic plasma membrane of rat brain
    • DOI 10.1002/jnr.1071
    • Orito, A., Kumanogoh, H., Yasaka, K., Sokawa, J., Hidaka, H., Sokawa, Y., and Maekawa, S. (2001) Calcium-dependent association of annexin VI, protein kinase C alpha, and neurocalcin alpha on the raft fraction derived from the synaptic plasma membrane of rat brain. J. Neurosci. Res. 64, 235-241. (Pubitemid 32385691)
    • (2001) Journal of Neuroscience Research , vol.64 , Issue.3 , pp. 235-241
    • Orito, A.1    Kumanogoh, H.2    Yasaka, K.3    Sokawa, J.4    Hidaka, H.5    Sokawa, Y.6    Maekawa, S.7
  • 30
    • 0026708526 scopus 로고
    • Ca (2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: Identification as a homologue for annexin VI and intracellular localization
    • Hosoya, H., Kobayashi, R., Tsukita, S., and Matsumura, F. (1992) Ca (2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: identification as a homologue for annexin VI and intracellular localization. Cell Motil. Cytoskeleton 22, 200-210.
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 200-210
    • Hosoya, H.1    Kobayashi, R.2    Tsukita, S.3    Matsumura, F.4
  • 31
    • 0032563573 scopus 로고    scopus 로고
    • Annexin VI-mediated loss of spectrin during coated pit budding is coupled to delivery of LDL to lysosomes
    • DOI 10.1083/jcb.142.4.937
    • Kamal, A., Ying, Y., and Anderson, R. G. (1998) Annexin VI-mediated loss of spectrin during coated pit budding is coupled to delivery of LDL to lysosomes. J. Cell Biol. 142, 937-947. (Pubitemid 28402050)
    • (1998) Journal of Cell Biology , vol.142 , Issue.4 , pp. 937-947
    • Kamal, A.1    Ying, Y.-S.2    Anderson, R.G.W.3
  • 32
    • 33846794209 scopus 로고    scopus 로고
    • Annexins as intracellular calcium sensors
    • DOI 10.1016/j.ceca.2006.06.008, PII S0143416006001291
    • Monastyrskaya, K., Babiychuk, E. B., Hostettler, A., Rescher, U., and Draeger, A. (2007) Annexins as intracellular calcium sensors. Cell Calcium 41, 207-219. (Pubitemid 46201502)
    • (2007) Cell Calcium , vol.41 , Issue.3 , pp. 207-219
    • Monastyrskaya, K.1    Babiychuk, E.B.2    Hostettler, A.3    Rescher, U.4    Draeger, A.5
  • 33
    • 0033034002 scopus 로고    scopus 로고
    • The 'early-sorting' endocytic compartment of rat hepatocytes is involved in the intracellular pathway of caveolin-1 (VIP-21)
    • DOI 10.1002/hep.510290602
    • Pol, A., Calvo, M., Lu, A., and Enrich, C. (1999) The "early-sorting" endocytic compartment of rat hepatocytes is involved in the intracellular pathway of caveolin-1 (VIP-21). Hepatology 29, 1848-1857. (Pubitemid 29247060)
    • (1999) Hepatology , vol.29 , Issue.6 , pp. 1848-1857
    • Pol, A.1    Calvo, M.2    Lu, A.3    Enrich, C.4
  • 34
    • 39549110022 scopus 로고    scopus 로고
    • Heterogeneity and timing of translocation and membrane-mediated assembly of different annexins
    • Skrahina, T., Piljić, A., and Schultz, C. (2008) Heterogeneity and timing of translocation and membrane-mediated assembly of different annexins. Exp. Cell Res. 314, 1039-1047.
    • (2008) Exp. Cell Res. , vol.314 , pp. 1039-1047
    • Skrahina, T.1    Piljić, A.2    Schultz, C.3
  • 35
    • 0028087187 scopus 로고
    • Endocytosis occurs independently of annexin VI in human A431 cells
    • Smythe, E., Smith, P. D., Jacob, S. M., Theobald, J., and Moss, S. E. (1994) Endocytosis occurs independently of annexin VI in human A431 cells. J. Cell Biol. 124, 301-306. (Pubitemid 24050348)
    • (1994) Journal of Cell Biology , vol.124 , Issue.3 , pp. 301-306
    • Smythe, E.1    Smith, P.D.2    Jacob, S.M.3    Theobald, J.4    Moss, S.E.5
  • 37
    • 0035840266 scopus 로고    scopus 로고
    • Evidence for the involvement of annexin 6 in the trafficking between the endocytic compartment and lysosomes
    • DOI 10.1006/excr.2001.5268
    • Pons, M., Grewal, T., Rius, E., Schnitgerhans, T., Jäckle, S., and Enrich, C. (2001) Evidence for the involvement of annexin 6 in the trafficking between the endocytic compartment and lysosomes. Exp. Cell Res. 269, 13-22. (Pubitemid 32848485)
    • (2001) Experimental Cell Research , vol.269 , Issue.1 , pp. 13-22
    • Pons, M.1    Grewal, T.2    Rius, E.3    Schnitgerhans, T.4    Jackle, S.5    Enrich, C.6
  • 38
    • 0028237273 scopus 로고
    • Annexin VI-binding proteins in brain. Interaction of annexin VI with a membrane skeletal protein, calspectin (brain spectrin or fodrin)
    • Watanabe, T., Inui, M., Chen, B. Y., Iga, M., and Sobue, K. (1994) Annexin VI-binding proteins in brain. Interaction of annexin VI with a membrane skeletal protein, calspectin (brain spectrin or fodrin). J. Biol. Chem. 269, 17656-17662.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17656-17662
    • Watanabe, T.1    Inui, M.2    Chen, B.Y.3    Iga, M.4    Sobue, K.5
  • 39
    • 0024549533 scopus 로고
    • Crystallization of p68 on lipid monolayers and as three-dimensional single crystals
    • DOI 10.1016/0022-2836(89)90534-2
    • Newman, R., Tucker, A., Ferguson, C., Tsernoglou, D., Leonard, K., and Crumpton, M. J. (1989) Crystallization of p68 on lipid monolayers and as three-dimensional single crystals. J. Mol. Biol. 206, 213-219. (Pubitemid 19095551)
    • (1989) Journal of Molecular Biology , vol.206 , Issue.1 , pp. 213-219
    • Newman, R.1    Tucker, A.2    Ferguson, C.3    Tsernoglou, D.4    Leonard, K.5    Crumpton, M.J.6
  • 40
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • DOI 10.1038/nbt790
    • Blagoev, B., Kratchmarova, I., Ong, S.-E., Nielsen, M., Foster, L. J., and Mann, M. (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21, 315-318. (Pubitemid 36314817)
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.-E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 42
    • 0034598996 scopus 로고    scopus 로고
    • Identification of a novel protein complex containing annexin VI, Fyn, Pyk2, and the p120(GAP) C2 domain
    • DOI 10.1016/S0014-5793(00)01252-7, PII S0014579300012527
    • Chow, A., Davis, A. J., and Gawler, D. J. (2000) Identification of a novel protein complex containing annexin VI, Fyn, Pyk2, and the p120 (GAP) C2 domain. FEBS Lett. 469, 88-92. (Pubitemid 30119875)
    • (2000) FEBS Letters , vol.469 , Issue.1 , pp. 88-92
    • Chow, A.1    Davis, A.J.2    Gawler, D.J.3
  • 43
    • 0030568906 scopus 로고    scopus 로고
    • 2+-dependent membrane-binding proteins
    • DOI 10.1074/jbc.271.40.24333
    • Davis, A. J., Butt, J. T., Walker, J. H., Moss, S. E., and Gawler, D. J. (1996) The Ca2+-dependent lipid binding domain of P120GAP mediates protein-protein interactions with Ca2+-dependent membrane-binding proteins. Evidence for a direct interaction between annexin VI and P120GAP. J. Biol. Chem. 271, 24333-24336. (Pubitemid 26333161)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.40 , pp. 24333-24336
    • Davisk, A.J.1    Butt, J.T.2    Walker, J.H.3    Moss, S.E.4    Gawler, D.J.5
  • 48
    • 0032031576 scopus 로고    scopus 로고
    • Activated protein kinase C α associates with annexin VI from skeletal muscle
    • Schmitz-Peiffer, C., Browne, C. L., Walker, J. H., and Biden, T. J. (1998) Activated protein kinase C alpha associates with annexin VI from skeletal muscle. Biochem. J. 330 (Pt 2), 675-681. (Pubitemid 28111961)
    • (1998) Biochemical Journal , vol.330 , Issue.2 , pp. 675-681
    • Schmitz-Peiffer, C.1    Browne, C.L.2    Walker, J.H.3    Biden, T.J.4
  • 49
    • 0035854784 scopus 로고    scopus 로고
    • Activation of Raf-1 is defective in annexin 6 overexpressing Chinese hamster ovary cells
    • PII S0014579301026357
    • Pons, M., Tebar, F., Kirchhoff, M., Peiró, S., de Diego, I., Grewal, T., and Enrich, C. (2001) Activation of Raf-1 is defective in annexin 6 overexpressing Chinese hamster ovary cells. FEBS Lett. 501, 69-73. (Pubitemid 33712489)
    • (2001) FEBS Letters , vol.501 , Issue.1-3 , pp. 69-73
    • Pons, M.1    Tebar, F.2    Kirchhoff, M.3    Peiro, S.4    De Diego, I.5    Grewal, T.6    Enrich, C.7
  • 51
    • 35348847785 scopus 로고    scopus 로고
    • Annexin a6-Induced alterations in cholesterol transport and caveolin export from the Golgi complex
    • DOI 10.1111/j.1600-0854.2007.00640.x
    • Cubells, L., Vilà De Muga, S., Tebar, F., Wood, P., Evans, R., Ingelmo-Torres, M., Calvo, M., Gaus, K., Pol, A., Grewal, T., and Enrich, C. (2007) Annexin A6-induced alterations in cholesterol transport and caveolin export from the Golgi complex. Traffic 8, 1568-1589. (Pubitemid 47578362)
    • (2007) Traffic , vol.8 , Issue.11 , pp. 1568-1589
    • Cubells, L.1    Vila De Muga, S.2    Tebar, F.3    Wood, P.4    Evans, R.5    Ingelmo-torres, M.6    Calvo, M.7    Gaus, K.8    Pol, A.9    Grewal, T.10    Enrich, C.11
  • 52
    • 44349160147 scopus 로고    scopus 로고
    • Annexin A6-induced inhibition of cytoplasmic phospholipase A2 is linked to caveolin-1 export from the Golgi
    • Cubells, L., de Muga, S. V., Tebar, F., Bonventre, J. V., Balsinde, J., Pol, A., Grewal, T., and Enrich, C. (2008) Annexin A6-induced inhibition of cytoplasmic phospholipase A2 is linked to caveolin-1 export from the Golgi. J. Biol. Chem. 283, 10174-10183.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10174-10183
    • Cubells, L.1    De Muga, S.V.2    Tebar, F.3    Bonventre, J.V.4    Balsinde, J.5    Pol, A.6    Grewal, T.7    Enrich, C.8
  • 54
    • 0034713256 scopus 로고    scopus 로고
    • Late endocytic compartments are major sites of annexin VI localization in NRK fibroblasts and polarized WIF-B hepatoma cells
    • DOI 10.1006/excr.2000.4861
    • Pons, M., Ihrke, G., Koch, S., Biermer, M., Pol, A., Grewal, T., Jäckle, S., and Enrich, C. (2000) Late endocytic compartments are major sites of annexin VI localization in NRK fibroblasts and polarized WIF-B hepatoma cells. Exp. Cell Res. 257, 33-47. (Pubitemid 30324642)
    • (2000) Experimental Cell Research , vol.257 , Issue.1 , pp. 33-47
    • Pons, M.1    Ihrke, G.2    Koch, S.3    Biermer, M.4    Pol, A.5    Grewal, T.6    Jackle, S.7    Enrich, C.8
  • 55
    • 34447543021 scopus 로고    scopus 로고
    • Annexins and endocytosis
    • DOI 10.1111/j.1600-0854.2007.00590.x
    • Futter, C. E. and White, I. J. (2007) Annexins and endocytosis. Traffic 8, 951-958. (Pubitemid 47074030)
    • (2007) Traffic , vol.8 , Issue.8 , pp. 951-958
    • Futter, C.E.1    White, I.J.2
  • 59
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke, V. and Moss, S. E. (2002) Annexins: from structure to function. Physiol. Rev. 82, 331-371. (Pubitemid 34654456)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 60
    • 4344667769 scopus 로고    scopus 로고
    • Annexin-Actin interactions
    • DOI 10.1111/j.1600-0854.2004.00210.x
    • Hayes, M. J., Rescher, U., Gerke, V., and Moss, S. E. (2004) Annexin-actin interactions. Traffic 5, 571-576. (Pubitemid 39144487)
    • (2004) Traffic , vol.5 , Issue.8 , pp. 571-576
    • Hayes, M.J.1    Rescher, U.2    Gerke, V.3    Moss, S.E.4
  • 61
    • 3242877433 scopus 로고    scopus 로고
    • Annexins - Unique membrane binding proteins with diverse functions
    • DOI 10.1242/jcs.01245
    • Rescher, U. and Gerke, V. (2004) Annexins-unique membrane binding proteins with diverse functions. J. Cell Sci. 117, 2631-2639. (Pubitemid 38997247)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 62
    • 3242887228 scopus 로고    scopus 로고
    • Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes
    • DOI 10.1242/jcs.01208
    • Rescher, U., Ruhe, D., Ludwig, C., Zobiack, N., and Gerke, V. (2004) Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J. Cell Sci. 117, 3473-3480. (Pubitemid 39206387)
    • (2004) Journal of Cell Science , vol.117 , Issue.16 , pp. 3473-3480
    • Rescher, U.1    Ruhe, D.2    Ludwig, C.3    Zobiack, N.4    Gerke, V.5
  • 63
    • 54049089919 scopus 로고    scopus 로고
    • Annexin A6 at the cardiac myocyte sarcolemma-evidence for selfassociation and binding to actin
    • Locate, S., Colyer, J., Gawler, D. J., and Walker, J. H. (2008) Annexin A6 at the cardiac myocyte sarcolemma-evidence for selfassociation and binding to actin. Cell Biol. Int. 32, 1388-1396.
    • (2008) Cell Biol. Int. , vol.32 , pp. 1388-1396
    • Locate, S.1    Colyer, J.2    Gawler, D.J.3    Walker, J.H.4
  • 64
    • 0033520911 scopus 로고    scopus 로고
    • Annexin VI participates in the formation of a reversible, membrane-cytoskeleton complex in smooth muscle cells
    • Babiychuk, E. B., Palstra, R. J., Schaller, J., Kämpfer, U., and Draeger, A. (1999) Annexin VI participates in the formation of a reversible, membrane-cytoskeleton complex in smooth muscle cells. J. Biol. Chem. 274, 35191-35195. (Pubitemid 129509576)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 35191-35195
    • Babiychuk, E.B.1    Palstra, R.-J.T.S.2    Schaller, J.3    Kampfer, U.4    Draeger, A.5
  • 65
    • 0025214339 scopus 로고
    • Purification, biological properties and partial sequence analysis of 67-kDa calcimedin and its 34-kDa fragment from chicken gizzard
    • Kobayashi, R. and Tashima, Y. (1990) Purification, biological properties and partial sequence analysis of 67-kDa calcimedin and its 34-kDa fragment from chicken gizzard. Eur. J. Biochem. 188, 447-453. (Pubitemid 20106260)
    • (1990) European Journal of Biochemistry , vol.188 , Issue.2 , pp. 447-453
    • Kobayashi, R.1    Tashima, Y.2
  • 66
    • 0026622890 scopus 로고
    • Annexin VI is required for budding of clathrin-coated pits
    • Lin, H. C., Südhof, T. C., and Anderson, R. G. (1992) Annexin VI is required for budding of clathrin-coated pits. Cell 70, 283-291.
    • (1992) Cell. , vol.70 , pp. 283-291
    • Lin, H.C.1    Südhof, T.C.2    Anderson, R.G.3
  • 67
    • 67650532174 scopus 로고    scopus 로고
    • Plasma membrane-associated annexin A6 reduces Ca2+ entry by stabilizing the cortical actin cytoskeleton
    • Monastyrskaya, K., Babiychuk, E. B., Hostettler, A., Wood, P., Grewal, T., and Draeger, A. (2009) Plasma membrane-associated annexin A6 reduces Ca2+ entry by stabilizing the cortical actin cytoskeleton. J. Biol. Chem. 284, 17227-17242.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17227-17242
    • Monastyrskaya, K.1    Babiychuk, E.B.2    Hostettler, A.3    Wood, P.4    Grewal, T.5    Draeger, A.6
  • 68
    • 33845951914 scopus 로고    scopus 로고
    • Requirement for annexin A1 in plasma membrane repair
    • DOI 10.1074/jbc.M606406200
    • McNeil, A. K., Rescher, U., Gerke, V., and McNeil, P. L. (2006) Requirement for annexin A1 in plasma membrane repair. J. Biol. Chem. 281, 35202-35207. (Pubitemid 46036558)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35202-35207
    • McNeil, A.K.1    Rescher, U.2    Gerke, V.3    McNeil, P.L.4
  • 71
    • 79951952737 scopus 로고    scopus 로고
    • Plasma membrane repair and cellular damage control: The annexin survival kit
    • Draeger, A., Monastyrskaya, K., and Babiychuk, E. B. (2011) Plasma membrane repair and cellular damage control: the annexin survival kit. Biochem. Pharmacol. 81, 703-712.
    • (2011) Biochem. Pharmacol. , vol.81 , pp. 703-712
    • Draeger, A.1    Monastyrskaya, K.2    Babiychuk, E.B.3
  • 72
    • 77951923713 scopus 로고    scopus 로고
    • Hierarchical organization of the plasma membrane: Investigations by single-molecule tracking vs. fluorescence correlation spectroscopy
    • Kusumi, A., Shirai, Y. M., Koyama-Honda, I., Suzuki, K. G., and Fujiwara, T. K. (2010) Hierarchical organization of the plasma membrane: investigations by single-molecule tracking vs. fluorescence correlation spectroscopy. FEBS Lett. 584, 1814-1823.
    • (2010) FEBS Lett. , vol.584 , pp. 1814-1823
    • Kusumi, A.1    Shirai, Y.M.2    Koyama-Honda, I.3    Suzuki, K.G.4    Fujiwara, T.K.5
  • 74
    • 6344225446 scopus 로고    scopus 로고
    • Protein kinaseCδ-calmodulin crosstalk regulates epidermal growth factor receptor exit from early endosomes
    • DOI 10.1091/mbc.E04-02-0127
    • Lladó, A., Tebar, F., Calvo, M., Moretó, J., Sorkin, A., and Enrich, C. (2004) Protein kinaseCdelta-calmodulin crosstalk regulates epidermal growth factor receptor exit from early endosomes. Mol. Biol. Cell 15, 4877-4891. (Pubitemid 39392204)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.11 , pp. 4877-4891
    • Llado, A.1    Tebar, F.2    Calvo, M.3    Moreto, J.4    Sorkin, A.5    Enrich, C.6
  • 75
    • 38749091259 scopus 로고    scopus 로고
    • Protein kinase Cδ and calmodulin regulate epidermal growth factor receptor recycling from early endosomes through Arp2/3 complex and cortactin
    • DOI 10.1091/mbc.E07-05-0411
    • Lladó, A., Timpson, P., Vilà de Muga, S., Moretó, J., Pol, A., Grewal, T., Daly, R. J., Enrich, C., and Tebar, F. (2008) Protein kinase Cdelta and calmodulin regulate epidermal growth factor receptor recycling from early endosomes through Arp2/3 complex and cortactin. Mol. Biol. Cell 19, 17-29. (Pubitemid 351186129)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.1 , pp. 17-29
    • Llado, A.1    Timpson, P.2    Vila De Muga, S.3    Moreto, J.4    Pol, A.5    Grewal, T.6    Daly, R.J.7    Enrich, C.8    Tebar, F.9
  • 76
    • 0344420213 scopus 로고    scopus 로고
    • Actin microfilaments et al. - The many components, effectors and regulators of epithelial cell endocytosis
    • DOI 10.1016/j.addr.2003.07.011
    • da Costa, S. R., Okamoto, C. T., and Hamm-Alvarez, S. F. (2003) Actin microfilaments et al. - The many components, effectors and regulators of epithelial cell endocytosis. Adv. Drug Delivery. Rev. 55, 1359-1383. (Pubitemid 37464568)
    • (2003) Advanced Drug Delivery Reviews , vol.55 , Issue.11 , pp. 1359-1383
    • Da Costa, S.R.1    Okamoto, C.T.2    Hamm-Alvarez, S.F.3
  • 77
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • DOI 10.1038/nrm1940, PII NRM1940
    • Kaksonen, M., Toret, C. P., and Drubin, D. G. (2006) Harnessing actin dynamics for clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 7, 404-414. (Pubitemid 44050094)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.6 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 78
    • 0036468381 scopus 로고    scopus 로고
    • Coupling actin dynamics and membrane dynamics during endocytosis
    • DOI 10.1016/S0955-0674(01)00297-6
    • Schafer, D. A. (2002) Coupling actin dynamics and membrane dynamics during endocytosis. Curr. Opin. Cell Biol. 14, 76-81. (Pubitemid 34131660)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.1 , pp. 76-81
    • Schafer, D.A.1
  • 79
    • 33845699085 scopus 로고    scopus 로고
    • Actin regulation in endocytosis
    • DOI 10.1242/jcs.03247
    • Smythe, E. and Ayscough, K. R. (2006) Actin regulation in endocytosis. J. Cell Sci. 119, 4589-4598. (Pubitemid 44964255)
    • (2006) Journal of Cell Science , vol.119 , Issue.22 , pp. 4589-4598
    • Smythe, E.1    Ayscough, K.R.2
  • 80
    • 60549110938 scopus 로고    scopus 로고
    • Lipid rafts and caveolae in signaling by growth factor receptors
    • de Laurentiis, A., Donovan, L., and Arcaro, A. (2007) Lipid rafts and caveolae in signaling by growth factor receptors. Open Biochem. J. 1, 12-32.
    • (2007) Open Biochem. J. , vol.1 , pp. 12-32
    • De Laurentiis, A.1    Donovan, L.2    Arcaro, A.3
  • 81
    • 0037087555 scopus 로고    scopus 로고
    • Cholesterol is important in control of EGF receptor kinase activity but EGF receptors are not concentrated in caveolae
    • Ringerike, T., Blystad, F. D., Levy, F. O., Madshus, I. H., and Stang, E. (2002) Cholesterol is important in control of EGF receptor kinase activity but EGF receptors are not concentrated in caveolae. J. Cell Sci. 115, 1331-1340. (Pubitemid 34272497)
    • (2002) Journal of Cell Science , vol.115 , Issue.6 , pp. 1331-1340
    • Ringerike, T.1    Blystad, F.D.2    Levy, F.O.3    Madshus, I.H.4    Stang, E.5
  • 82
    • 0037147320 scopus 로고    scopus 로고
    • Cholesterol depletion from the plasma membrane triggers ligand-independent activation of the epidermal growth factor receptor
    • DOI 10.1074/jbc.M208327200
    • Chen, X. and Resh, M. D. (2002) Cholesterol depletion from the plasma membrane triggers ligand-independent activation of the epidermal growth factor receptor. J. Biol. Chem. 277, 49631-49637. (Pubitemid 36014404)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.51 , pp. 49631-49637
    • Chen, X.1    Resh, M.D.2
  • 83
    • 0037072273 scopus 로고    scopus 로고
    • Cholesterol levels modulate EGF receptor-mediated signaling by altering receptor function and trafficking
    • DOI 10.1021/bi025943i
    • Pike, L. J. and Casey, L. (2002) Cholesterol levels modulate EGF receptor-mediated signaling by altering receptor function and trafficking. Biochemistry 41, 10315-10322. (Pubitemid 34856457)
    • (2002) Biochemistry , vol.41 , Issue.32 , pp. 10315-10322
    • Pike, L.J.1    Casey, L.2
  • 84
    • 0037166323 scopus 로고    scopus 로고
    • Sequestration of epidermal growth factor receptors in non-caveolar lipid rafts inhibits ligand binding
    • DOI 10.1074/jbc.M201422200
    • Roepstorff, K., Thomsen, P., Sandvig, K., and van Deurs, B. (2002) Sequestration of epidermal growth factor receptors in non-caveolar lipid rafts inhibits ligand binding. J. Biol. Chem. 277, 18954-18960. (Pubitemid 34959960)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18954-18960
    • Roepstorff, K.1    Thomsen, P.2    Sandvig, K.3    Van Deurs, B.4
  • 86
    • 33845533562 scopus 로고    scopus 로고
    • Involvement of targeting and scaffolding proteins in the regulation of the EGFR/Ras/MAPK pathway in oncogenesis
    • Grewal, T., Tebar, F., Pol, A., and Enrich, C. (2006) Involvement of targeting and scaffolding proteins in the regulation of the EGFR/Ras/MAPK pathway in oncogenesis. Curr. Signal Trans. Ther. 1, 147-167.
    • (2006) Curr. Signal Trans. Ther. , vol.1 , pp. 147-167
    • Grewal, T.1    Tebar, F.2    Pol, A.3    Enrich, C.4
  • 87
    • 33749525656 scopus 로고    scopus 로고
    • EGF-induced activation of the EGF receptor does not trigger mobilization of caveolae
    • DOI 10.1111/j.1600-0854.2006.00487.x
    • Kazazic, M., Roepstorff, K., Johannessen, L. E., Pedersen, N. M., van Deurs, B., Stang, E., and Madshus, I. H. (2006) EGF-induced activation of the EGF receptor does not trigger mobilization of caveolae. Traffic 7, 1518-27. (Pubitemid 44524524)
    • (2006) Traffic , vol.7 , Issue.11 , pp. 1518-1527
    • Kazazic, M.1    Roepstorff, K.2    Johannessen, L.E.3    Pedersen, N.M.4    Van Deurs, B.5    Stang, E.6    Madshus, I.H.7
  • 89
    • 25444503249 scopus 로고    scopus 로고
    • Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis
    • DOI 10.1074/jbc.M503833200
    • Zhu, J.-X., Goldoni, S., Bix, G., Owens, R. T., McQuillan, D. J., Reed, C. C., and Iozzo, R. V. (2005) Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis. J. Biol. Chem. 280, 32468-32479. (Pubitemid 41361859)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32468-32479
    • Zhu, J.-X.1    Goldoni, S.2    Bix, G.3    Owens, R.T.4    McQuillan, D.J.5    Reed, C.6    Iozzo, R.V.7
  • 90
    • 0346435104 scopus 로고    scopus 로고
    • Cholesterol depletion results in site-specific increases in epidermal growth factor receptor phosphorylation due to membrane level effects: Studies with cholesterol enantiomers
    • DOI 10.1074/jbc.M304332200
    • Westover, E. J., Covey, D. F., Brockman, H. L., Brown, R. E., and Pike, L. J. (2003) Cholesterol depletion results in site-specific increases in epidermal growth factor receptor phosphorylation due to membrane level effects. Studies with cholesterol enantiomers. J. Biol. Chem. 278, 51125-51133. (Pubitemid 38020348)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51125-51133
    • Westover, E.J.1    Covey, D.F.2    Brockman, H.L.3    Brown, R.E.4    Pike, L.J.5
  • 91
    • 33845540298 scopus 로고    scopus 로고
    • Molecular mechanisms involved in Ras inactivation: The annexin A6-p120GAP complex
    • DOI 10.1002/bies.20503
    • Grewal, T. and Enrich, C. (2006) Molecular mechanisms involved in Ras inactivation: the annexin A6-p120GAP complex. BioEssays 28, 1211-1220. (Pubitemid 44925441)
    • (2006) BioEssays , vol.28 , Issue.12 , pp. 1211-1220
    • Grewal, T.1    Enrich, C.2
  • 92
    • 62749112560 scopus 로고    scopus 로고
    • Annexins-modulators of EGF receptor signalling and trafficking
    • Grewal, T. and Enrich, C. (2009) Annexins-modulators of EGF receptor signalling and trafficking. Cell. Signal. 21, 847-858.
    • (2009) Cell. Signal , vol.21 , pp. 847-858
    • Grewal, T.1    Enrich, C.2
  • 93
    • 0028920470 scopus 로고
    • Annexin VI has tumour-suppressor activity in human A431 squamous epithelial carcinoma cells
    • Theobald, J., Hanby, A., Patel, K., and Moss, S. E. (1995) Annexin VI has tumour-suppressor activity in human A431 squamous epithelial carcinoma cells. Br. J. Cancer 71, 786-788.
    • (1995) Br. J. Cancer , vol.71 , pp. 786-788
    • Theobald, J.1    Hanby, A.2    Patel, K.3    Moss, S.E.4
  • 96
    • 0034714277 scopus 로고    scopus 로고
    • Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome
    • Bao, J., Alroy, I., Waterman, H., Schejter, E. D., Brodie, C., Gruenberg, J., and Yarden, Y. (2000) Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome. J. Biol. Chem. 275, 26178-26186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26178-26186
    • Bao, J.1    Alroy, I.2    Waterman, H.3    Schejter, E.D.4    Brodie, C.5    Gruenberg, J.6    Yarden, Y.7
  • 97
    • 79952325707 scopus 로고    scopus 로고
    • Involvement of protein kinase C and rhoA in protease-activated receptor 1-mediated F-actin reorganization and cell growth in rat cardiomyocytes
    • Otani, H., Yoshioka, K., Nishikawa, H., Inagaki, C., and Nakamura, T. (2011) Involvement of protein kinase C and rhoA in protease-activated receptor 1-mediated F-actin reorganization and cell growth in rat cardiomyocytes. J. Pharmacol. Sci. 115, 135-143.
    • (2011) J. Pharmacol. Sci. , vol.115 , pp. 135-143
    • Otani, H.1    Yoshioka, K.2    Nishikawa, H.3    Inagaki, C.4    Nakamura, T.5
  • 98
    • 0030033689 scopus 로고    scopus 로고
    • Association of P120 Ras GAP with endocytic components and colocalization with epidermal growth factor (EGF) receptor in response to EGF stimulation
    • Wang, Z., Tung, P. S., and Moran, M. F. (1996) Association of p120 ras GAP with endocytic components and colocalization with epidermal growth factor (EGF) receptor in response to EGF stimulation. Cell Growth Differ. 7, 123-133. (Pubitemid 26022100)
    • (1996) Cell Growth and Differentiation , vol.7 , Issue.1 , pp. 123-133
    • Wang, Z.1    Tung, P.S.2    Moran, M.F.3
  • 100
    • 0026048811 scopus 로고
    • Expression of annexin VI (p 68, 67 κDa-calelectrin) in normal human tissues: Evidence for developmental regulation in B-and T-lymphocytes
    • Clark, D. M., Moss, S. E., Wright, N. A., and Crumpton, M. J. (1991) Expression of annexin VI (p 68, 67 κDa-calelectrin) in normal human tissues: evidence for developmental regulation in B-and T-lymphocytes. Histochemistry 96, 405-412.
    • (1991) Histochemistry , vol.96 , pp. 405-412
    • Clark, D.M.1    Moss, S.E.2    Wright, N.A.3    Crumpton, M.J.4
  • 101
    • 0346244099 scopus 로고    scopus 로고
    • T-cell-antigen recognition and the immunological synapse
    • Huppa, J. B. and Davis, M. M. (2003) T-cell-antigen recognition and the immunological synapse. Nat. Rev. Immunol. 3, 973-983. (Pubitemid 37521539)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.12 , pp. 973-983
    • Huppa, J.B.1    Davis, M.M.2
  • 102
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • DOI 10.1146/annurev.immunol.20.092601.111357
    • Samelson, L. E. (2002) Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20, 371-394. (Pubitemid 34293429)
    • (2002) Annual Review of Immunology , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 103
    • 27544441784 scopus 로고    scopus 로고
    • Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • Campi, G., Varma, R., and Dustin, M. L. (2005) Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J. Exp. Med. 202, 1031-1036.
    • (2005) J. Exp. Med. , vol.202 , pp. 1031-1036
    • Campi, G.1    Varma, R.2    Dustin, M.L.3
  • 104
    • 33746011209 scopus 로고    scopus 로고
    • T Cell Receptor-Proximal Signals Are Sustained in Peripheral Microclusters and Terminated in the Central Supramolecular Activation Cluster
    • DOI 10.1016/j.immuni.2006.04.010, PII S1074761306002974
    • Varma, R., Campi, G., Yokosuka, T., Saito, T., and Dustin, M. L. (2006) T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity 25, 117-127. (Pubitemid 44066825)
    • (2006) Immunity , vol.25 , Issue.1 , pp. 117-127
    • Varma, R.1    Campi, G.2    Yokosuka, T.3    Saito, T.4    Dustin, M.L.5
  • 105
    • 30044441433 scopus 로고    scopus 로고
    • Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76
    • DOI 10.1038/ni1272, PII N1272
    • Yokosuka, T., Sakata-Sogawa, K., Kobayashi, W., Hiroshima, M., Hashimoto-Tane, A., Tokunaga, M., Dustin, M. L., and Saito, T. (2005) Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76. Nat. Immunol. 6, 1253-1262. (Pubitemid 43045637)
    • (2005) Nature Immunology , vol.6 , Issue.12 , pp. 1253-1262
    • Yokosuka, T.1    Sakata-Sogawa, K.2    Kobayashi, W.3    Hiroshima, M.4    Hashimoto-Tane, A.5    Tokunaga, M.6    Dustin, M.L.7    Saito, T.8
  • 106
    • 33846626054 scopus 로고    scopus 로고
    • Regulation of T-cell activation by the cytoskeleton
    • DOI 10.1038/nri2021, PII NRI2021
    • Billadeau, D. D., Nolz, J. C., and Gomez, T. S. (2007) Regulation of T-cell activation by the cytoskeleton. Nat. Rev. Immunol. 7, 131-143. (Pubitemid 46174860)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.2 , pp. 131-143
    • Billadeau, D.D.1    Nolz, J.C.2    Gomez, T.S.3
  • 107
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • DOI 10.1038/25764
    • Monks, C. R., Freiberg, B. A., Kupfer, H., Sciaky, N., and Kupfer, A. (1998) Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 395, 82-86. (Pubitemid 28420234)
    • (1998) Nature , vol.395 , Issue.6697 , pp. 82-86
    • Monks, C.R.F.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 108
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • DOI 10.1126/science.285.5425.221
    • Grakoui, A., Bromley, S. K., Sumen, C., Davis, M. M., Shaw, A. S., Allen, P. M., and Dustin, M. L. (1999) The immunological synapse: a molecular machine controlling T cell activation. Science 285, 221-227. (Pubitemid 29329988)
    • (1999) Science , vol.285 , Issue.5425 , pp. 221-227
    • Grakoui, A.1    Bromley, S.K.2    Sumen, C.3    Davis, M.M.4    Shaw, A.S.5    Allen, P.M.6    Dustin, M.L.7
  • 109
    • 67349114397 scopus 로고    scopus 로고
    • T cell antigen receptor signaling and immunological synapse stability require myosin IIA
    • Ilani, T., Vasiliver-Shamis, G., Vardhana, S., Bretscher, A., and Dustin, M. L. (2009) T cell antigen receptor signaling and immunological synapse stability require myosin IIA. Nat. Immunol. 10, 531-539.
    • (2009) Nat. Immunol. , vol.10 , pp. 531-539
    • Ilani, T.1    Vasiliver-Shamis, G.2    Vardhana, S.3    Bretscher, A.4    Dustin, M.L.5
  • 110
    • 38049136514 scopus 로고    scopus 로고
    • Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells
    • Kaizuka, Y., Douglass, A. D., Varma, R., Dustin, M. L., and Vale, R. D. (2007) Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells. Proc. Natl. Acad. Sci. USA 104, 20296-20301.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 112
    • 0037154747 scopus 로고    scopus 로고
    • T cell receptor signaling precedes immunological synapse formation
    • DOI 10.1126/science.1067710
    • Lee, K.-H., Holdorf, A. D., Dustin, M. L., Chan, A. C., Allen, P. M., and Shaw, A. S. (2002) T cell receptor signaling precedes immunological synapse formation. Science 295, 1539-1542. (Pubitemid 34174012)
    • (2002) Science , vol.295 , Issue.5559 , pp. 1539-1542
    • Lee, K.-H.1    Holdorf, A.D.2    Dustin, M.L.3    Chan, A.C.4    Allen, P.M.5    Shaw, A.S.6
  • 113
    • 34548012864 scopus 로고    scopus 로고
    • Plasma membrane segregation during T cell activation: probing the order of domains
    • DOI 10.1016/j.coi.2007.05.002, PII S0952791507000970
    • Harder, T., Rentero, C., Zech, T., and Gaus, K. (2007) Plasma membrane segregation during T cell activation: probing the order of domains. Curr. Opin. Immunol. 19, 470-475. (Pubitemid 47284850)
    • (2007) Current Opinion in Immunology , vol.19 , Issue.4 , pp. 470-475
    • Harder, T.1    Rentero, C.2    Zech, T.3    Gaus, K.4
  • 114
  • 115
    • 67649871991 scopus 로고    scopus 로고
    • Quantitative microscopy: Protein dynamics and membrane organisation
    • Owen, D. M., Williamson, D., Rentero, C., and Gaus, K. (2009) Quantitative microscopy: protein dynamics and membrane organisation. Traffic 10, 962-971.
    • (2009) Traffic , vol.10 , pp. 962-971
    • Owen, D.M.1    Williamson, D.2    Rentero, C.3    Gaus, K.4
  • 116
    • 26444452661 scopus 로고    scopus 로고
    • Condensation of the plasma membrane at the site of T lymphocyte activation
    • DOI 10.1083/jcb.200505047
    • Gaus, K., Chklovskaia, E., Fazekas de St Groth, B., Jessup, W., and Harder, T. (2005) Condensation of the plasma membrane at the site of T lymphocyte activation. J. Cell Biol. 171, 121-131. (Pubitemid 41434607)
    • (2005) Journal of Cell Biology , vol.171 , Issue.1 , pp. 121-131
    • Gaus, K.1    Chklovskaia, E.2    Fazekas De St. Groth, B.3    Jessup, W.4    Harder, T.5
  • 118
    • 44049096985 scopus 로고    scopus 로고
    • T Cell Activation and the Cytoskeleton: You Can't Have One Without the Other
    • DOI 10.1016/S0065-2776(08)00001-1, PII S0065277608000011
    • Gomez, T. S. and Billadeau, D. D. (2008) T cell activation and the cytoskeleton: you can't have one without the other. Adv. Immunol. 97, 1-64. (Pubitemid 351711631)
    • (2008) Advances in Immunology , vol.97 , pp. 1-64
    • Gomez, T.S.1    Billadeau, D.D.2
  • 120
    • 0035851918 scopus 로고    scopus 로고
    • Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells
    • Villalba, M., Bi, K., Rodriguez, F., Tanaka, Y., Schoenberger, S., and Altman, A. (2001) Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells. J. Cell Biol. 155, 331-338. (Pubitemid 34289325)
    • (2001) Journal of Cell Biology , vol.155 , Issue.4 , pp. 331-338
    • Villalba, M.1    Bi, K.2    Rodriguez, F.3    Tanaka, Y.4    Schoenberger, S.5    Altman, A.6
  • 121
    • 33750533178 scopus 로고    scopus 로고
    • CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse
    • DOI 10.1038/ncb1492, PII NCB1492
    • Tavano, R., Contento, R. L., Baranda, S. J., Soligo, M., Tuosto, L., Manes, S., and Viola, A. (2006) CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nat. Cell Biol. 8, 1270-1276. (Pubitemid 44660592)
    • (2006) Nature Cell Biology , vol.8 , Issue.11 , pp. 1270-1276
    • Tavano, R.1    Contento, R.L.2    Baranda, S.J.3    Soligo, M.4    Tuosto, L.5    Manes, S.6    Viola, A.7
  • 122
    • 35548942611 scopus 로고    scopus 로고
    • Tether and trap: Regulation of membrane-raft dynamics by actin-binding proteins
    • DOI 10.1038/nri2193, PII NRI2193
    • Viola, A. and Gupta, N. (2007) Tether and trap: regulation of membrane-raft dynamics by actin-binding proteins. Nat. Rev. Immunol. 7, 889-896. (Pubitemid 350006240)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.11 , pp. 889-896
    • Viola, A.1    Gupta, N.2
  • 123
    • 33646061085 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome
    • DOI 10.1016/j.jaci.2006.02.005, PII S0091674906003162
    • Ochs, H. D. and Thrasher, A. J. (2006) The Wiskott-Aldrich syndrome. J. Allergy Clin. Immunol. 117, 725-738; quiz 739. (Pubitemid 44313817)
    • (2006) Journal of Allergy and Clinical Immunology , vol.117 , Issue.4 , pp. 725-738
    • Ochs, H.D.1    Thrasher, A.J.2


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