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Volumn 12, Issue 7, 2011, Pages 799-805

The unconventional secretory machinery of fibroblast growth factor 2

Author keywords

Acb1; AcbA; Acyl CoA binding protein; Annexin A2; Fibroblast growth factor 2; Heparan sulfate proteoglycans; HIV Tat; Interleukin 1 ; Non classical export; Phosphoinositides; PI(4,5)P2; Unconventional protein secretion

Indexed keywords

FIBROBLAST GROWTH FACTOR 2; INTERLEUKIN 1BETA; SECRETORY PROTEIN; UNCLASSIFIED DRUG; UNCONVENTIONAL SECRETORY PROTEIN;

EID: 79958771663     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2011.01187.x     Document Type: Review
Times cited : (60)

References (87)
  • 2
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence
    • Rubartelli A, Cozzolino F, Talio M, Sitia R. A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence. EMBO J 1990;9:1503-1510.
    • (1990) EMBO J , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 3
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper DN, Barondes SH. Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J Cell Biol 1990;110:1681-1691.
    • (1990) J Cell Biol , vol.110 , pp. 1681-1691
    • Cooper, D.N.1    Barondes, S.H.2
  • 5
    • 0026086635 scopus 로고
    • Release of basic fibroblast growth factor, an angiogenic factor devoid of secretory signal sequence: a trivial phenomenon or a novel secretion mechanism?
    • Mignatti P, Rifkin DB. Release of basic fibroblast growth factor, an angiogenic factor devoid of secretory signal sequence: a trivial phenomenon or a novel secretion mechanism? J Cell Biochem 1991;47:201-207.
    • (1991) J Cell Biochem , vol.47 , pp. 201-207
    • Mignatti, P.1    Rifkin, D.B.2
  • 6
    • 0026548976 scopus 로고
    • Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex
    • Mignatti P, Morimoto T, Rifkin DB. Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex. J Cell Physiol 1992;151:81-93.
    • (1992) J Cell Physiol , vol.151 , pp. 81-93
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 7
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel W, Rabouille C. Mechanisms of regulated unconventional protein secretion. Nat Rev Mol Cell Biol 2009;10:148-155.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 8
    • 55849145075 scopus 로고    scopus 로고
    • Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells
    • Nickel W, Seedorf M. Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells. Annu Rev Cell Dev Biol 2008;24:287-308.
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 287-308
    • Nickel, W.1    Seedorf, M.2
  • 9
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface
    • Deora AB, Kreitzer G, Jacovina AT, Hajjar KA. An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface. J Biol Chem 2004;279:43411-43418.
    • (2004) J Biol Chem , vol.279 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 10
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli A, Bajetto A, Allavena G, Wollman E, Sitia R. Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J Biol Chem 1992;267:24161-24164.
    • (1992) J Biol Chem , vol.267 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 12
    • 0036775236 scopus 로고    scopus 로고
    • The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway
    • Gardella S, Andrei C, Ferrera D, Lotti LV, Torrisi MR, Bianchi ME, Rubartelli A. The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway. EMBO Rep 2002;3:995-1001.
    • (2002) EMBO Rep , vol.3 , pp. 995-1001
    • Gardella, S.1    Andrei, C.2    Ferrera, D.3    Lotti, L.V.4    Torrisi, M.R.5    Bianchi, M.E.6    Rubartelli, A.7
  • 14
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • Scaffidi P, Misteli T, Bianchi ME. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 2002;418: 191-195.
    • (2002) Nature , vol.418 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 16
    • 34547604776 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP is required for unconventional protein secretion during development
    • Kinseth MA, Anjard C, Fuller D, Guizzunti G, Loomis WF, Malhotra V. The Golgi-associated protein GRASP is required for unconventional protein secretion during development. Cell 2007;130:524-534.
    • (2007) Cell , vol.130 , pp. 524-534
    • Kinseth, M.A.1    Anjard, C.2    Fuller, D.3    Guizzunti, G.4    Loomis, W.F.5    Malhotra, V.6
  • 17
    • 77149152566 scopus 로고    scopus 로고
    • Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation
    • Manjithaya R, Anjard C, Loomis WF, Subramani S. Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation. J Cell Biol 2010;188:537-546.
    • (2010) J Cell Biol , vol.188 , pp. 537-546
    • Manjithaya, R.1    Anjard, C.2    Loomis, W.F.3    Subramani, S.4
  • 18
    • 0030862924 scopus 로고    scopus 로고
    • HIV-1 Tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region
    • Chang HC, Samaniego F, Nair BC, Buonaguro L, Ensoli B. HIV-1 Tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region. AIDS 1997;11:1421-1431.
    • (1997) AIDS , vol.11 , pp. 1421-1431
    • Chang, H.C.1    Samaniego, F.2    Nair, B.C.3    Buonaguro, L.4    Ensoli, B.5
  • 20
    • 62649139025 scopus 로고    scopus 로고
    • Immunological and inflammatory functions of the interleukin-1 family
    • Dinarello CA. Immunological and inflammatory functions of the interleukin-1 family. Annu Rev Immunol 2009;27:519-550.
    • (2009) Annu Rev Immunol , vol.27 , pp. 519-550
    • Dinarello, C.A.1
  • 21
    • 0037465251 scopus 로고    scopus 로고
    • The interleukin-1 receptor/Toll-like receptor superfamily: signal transduction during inflammation and host defense
    • Dunne A, O'Neill LA. The interleukin-1 receptor/Toll-like receptor superfamily: signal transduction during inflammation and host defense. Sci STKE 2003;2003:re3.
    • (2003) Sci STKE , vol.2003
    • Dunne, A.1    O'Neill, L.A.2
  • 22
    • 61649100307 scopus 로고    scopus 로고
    • The FGF family: biology, pathophysiology and therapy
    • Beenken A, Mohammadi M. The FGF family: biology, pathophysiology and therapy. Nat Rev Drug Discov 2009;8:235-253.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 235-253
    • Beenken, A.1    Mohammadi, M.2
  • 23
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M. Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Cell 2000;101:413-424.
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 24
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov AN, Schlessinger J, Hubbard SR, Mohammadi M. Structural basis for FGF receptor dimerization and activation. Cell 1999;98: 641-650.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 26
    • 67349258025 scopus 로고    scopus 로고
    • Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation
    • Rabinovich GA, Toscano MA. Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat Rev Immunol 2009;9:338-352.
    • (2009) Nat Rev Immunol , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 28
    • 67649795958 scopus 로고    scopus 로고
    • Galectin-3 regulates T-cell functions
    • Hsu DK, Chen HY, Liu FT. Galectin-3 regulates T-cell functions. Immunol Rev 2009;230:114-127.
    • (2009) Immunol Rev , vol.230 , pp. 114-127
    • Hsu, D.K.1    Chen, H.Y.2    Liu, F.T.3
  • 30
    • 79151470481 scopus 로고    scopus 로고
    • Autophagy: a broad role in unconventional protein secretion?
    • Manjithaya R, Subramani S. Autophagy: a broad role in unconventional protein secretion? Trends Cell Biol 2011;21:67-73.
    • (2011) Trends Cell Biol , vol.21 , pp. 67-73
    • Manjithaya, R.1    Subramani, S.2
  • 32
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: linking Ca2+ signalling to membrane dynamics
    • Gerke V, Creutz CE, Moss SE. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 2005;6:449-461.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 33
    • 77957329900 scopus 로고    scopus 로고
    • Pathways of unconventional protein secretion
    • Nickel W. Pathways of unconventional protein secretion. Curr Opin Biotechnol 2010;21:621-626.
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 621-626
    • Nickel, W.1
  • 35
    • 0028939001 scopus 로고
    • Quantitative export of FGF-2 occurs through an alternative, energy- dependent, non-ER/Golgi pathway
    • Florkiewicz RZ, Majack RA, Buechler RD, Florkiewicz E. Quantitative export of FGF-2 occurs through an alternative, energy- dependent, non-ER/Golgi pathway. J Cell Physiol 1995;162:388-399.
    • (1995) J Cell Physiol , vol.162 , pp. 388-399
    • Florkiewicz, R.Z.1    Majack, R.A.2    Buechler, R.D.3    Florkiewicz, E.4
  • 37
    • 0033795350 scopus 로고    scopus 로고
    • Translocation of FGF2 to the cell surface without release into conditioned media [In Process Citation]
    • Trudel C, Faure-Desire V, Florkiewicz RZ, Baird A. Translocation of FGF2 to the cell surface without release into conditioned media [In Process Citation]. J Cell Physiol 2000;185260-268.
    • (2000) J Cell Physiol , vol.185 , pp. 260-268
    • Trudel, C.1    Faure-Desire, V.2    Florkiewicz, R.Z.3    Baird, A.4
  • 38
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel W. The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur J Biochem 2003;270:2109-2119.
    • (2003) Eur J Biochem , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 39
    • 1342325441 scopus 로고    scopus 로고
    • Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells
    • Schafer T, Zentgraf H, Zehe C, Brugger B, Bernhagen J, Nickel W. Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells. J Biol Chem 2004;279:6244-6251.
    • (2004) J Biol Chem , vol.279 , pp. 6244-6251
    • Schafer, T.1    Zentgraf, H.2    Zehe, C.3    Brugger, B.4    Bernhagen, J.5    Nickel, W.6
  • 40
    • 21844468743 scopus 로고    scopus 로고
    • Unconventional secretory routes: direct protein export across the plasma membrane of mammalian cells
    • Nickel W. Unconventional secretory routes: direct protein export across the plasma membrane of mammalian cells. Traffic 2005; 6:607-614.
    • (2005) Traffic , vol.6 , pp. 607-614
    • Nickel, W.1
  • 41
    • 46349098379 scopus 로고    scopus 로고
    • A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2
    • Temmerman K, Ebert AD, Muller HM, Sinning I, Tews I, Nickel W. A direct role for phosphatidylinositol-4, 5-bisphosphate in unconventional secretion of fibroblast growth factor 2. Traffic 2008;9: 1204-1217.
    • (2008) Traffic , vol.9 , pp. 1204-1217
    • Temmerman, K.1    Ebert, A.D.2    Muller, H.M.3    Sinning, I.4    Tews, I.5    Nickel, W.6
  • 42
    • 67649844238 scopus 로고    scopus 로고
    • A novel flow cytometric assay to quantify interactions between proteins and membrane lipids
    • Temmerman K, Nickel W. A novel flow cytometric assay to quantify interactions between proteins and membrane lipids. J Lipid Res 2009;50:1245-1254.
    • (2009) J Lipid Res , vol.50 , pp. 1245-1254
    • Temmerman, K.1    Nickel, W.2
  • 45
    • 0030890997 scopus 로고    scopus 로고
    • Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor
    • Moy FJ, Safran M, Seddon AP, Kitchen D, Bohlen P, Aviezer D, Yayon A, Powers R. Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor. Biochemistry 1997;36:4782-4791.
    • (1997) Biochemistry , vol.36 , pp. 4782-4791
    • Moy, F.J.1    Safran, M.2    Seddon, A.P.3    Kitchen, D.4    Bohlen, P.5    Aviezer, D.6    Yayon, A.7    Powers, R.8
  • 46
    • 0001452803 scopus 로고    scopus 로고
    • Heparin-induced self-association of fibroblast growth factor-2. Evidence for two oligomerization processes
    • Herr AB, Ornitz DM, Sasisekharan R, Venkataraman G, Waksman G. Heparin-induced self-association of fibroblast growth factor-2. Evidence for two oligomerization processes. J Biol Chem 1997;272:16382-16389.
    • (1997) J Biol Chem , vol.272 , pp. 16382-16389
    • Herr, A.B.1    Ornitz, D.M.2    Sasisekharan, R.3    Venkataraman, G.4    Waksman, G.5
  • 47
    • 0033178348 scopus 로고    scopus 로고
    • Oligomeric self-association of basic fibroblast growth factor in the absence of heparin-like glycosaminoglycans
    • Davis JC, Venkataraman G, Shriver Z, Raj PA, Sasisekharan R. Oligomeric self-association of basic fibroblast growth factor in the absence of heparin-like glycosaminoglycans. Biochem J 1999; 341:613-620.
    • (1999) Biochem J , vol.341 , pp. 613-620
    • Davis, J.C.1    Venkataraman, G.2    Shriver, Z.3    Raj, P.A.4    Sasisekharan, R.5
  • 48
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport TA. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 2007;450:663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 49
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W, Herrmann JM. Translocation of proteins into mitochondria. Annu Rev Biochem 2007;76:723-749.
    • (2007) Annu Rev Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 50
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway
    • Holland IB, Schmitt L, Young J. Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway. Mol Membr Biol 2005;22:29-39.
    • (2005) Mol Membr Biol , vol.22 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 51
    • 2342443941 scopus 로고    scopus 로고
    • Unconventional protein secretion: membrane translocation of FGF-2 does not require protein unfolding
    • Backhaus R, Zehe C, Wegehingel S, Kehlenbach A, Schwappach B, Nickel W. Unconventional protein secretion: membrane translocation of FGF-2 does not require protein unfolding. J Cell Sci 2004;117:1727-1736.
    • (2004) J Cell Sci , vol.117 , pp. 1727-1736
    • Backhaus, R.1    Zehe, C.2    Wegehingel, S.3    Kehlenbach, A.4    Schwappach, B.5    Nickel, W.6
  • 52
    • 70350400642 scopus 로고    scopus 로고
    • An intrinsic quality-control mechanism ensures unconventional secretion of fibroblast growth factor 2 in a folded conformation
    • Torrado LC, Temmerman K, Muller HM, Mayer MP, Seelenmeyer C, Backhaus R, Nickel W. An intrinsic quality-control mechanism ensures unconventional secretion of fibroblast growth factor 2 in a folded conformation. J Cell Sci 2009;122:3322-3329.
    • (2009) J Cell Sci , vol.122 , pp. 3322-3329
    • Torrado, L.C.1    Temmerman, K.2    Muller, H.M.3    Mayer, M.P.4    Seelenmeyer, C.5    Backhaus, R.6    Nickel, W.7
  • 53
    • 27744523622 scopus 로고    scopus 로고
    • Peroxisomal matrix protein import: the transient pore model
    • Erdmann R, Schliebs W. Peroxisomal matrix protein import: the transient pore model. Nat Rev Mol Cell Biol 2005;6:738-742.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 738-742
    • Erdmann, R.1    Schliebs, W.2
  • 54
    • 78649403829 scopus 로고    scopus 로고
    • Peroxisomal protein import and ERAD: variations on a common theme
    • Schliebs W, Girzalsky W, Erdmann R. Peroxisomal protein import and ERAD: variations on a common theme. Nat Rev Mol Cell Biol 2010;11:885-890.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 885-890
    • Schliebs, W.1    Girzalsky, W.2    Erdmann, R.3
  • 55
    • 60349123961 scopus 로고    scopus 로고
    • Protein transport in organelles: Protein transport into and across the thylakoid membrane
    • Aldridge C, Cain P, Robinson C. Protein transport in organelles: Protein transport into and across the thylakoid membrane. FEBS J 2009;276:1177-1186.
    • (2009) FEBS J , vol.276 , pp. 1177-1186
    • Aldridge, C.1    Cain, P.2    Robinson, C.3
  • 56
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: moving folded proteins across membranes
    • Sargent F. The twin-arginine transport system: moving folded proteins across membranes. Biochem Soc Trans 2007;35:835-847.
    • (2007) Biochem Soc Trans , vol.35 , pp. 835-847
    • Sargent, F.1
  • 57
    • 34547743839 scopus 로고    scopus 로고
    • Unconventional secretion: an extracellular trap for export of fibroblast growth factor 2
    • Nickel W. Unconventional secretion: an extracellular trap for export of fibroblast growth factor 2. J Cell Sci 2007;120:2295-2299.
    • (2007) J Cell Sci , vol.120 , pp. 2295-2299
    • Nickel, W.1
  • 58
    • 33750299160 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2
    • Zehe C, Engling A, Wegehingel S, Schafer T, Nickel W. Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2. Proc Natl Acad Sci U S A 2006;103:15479-15484.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15479-15484
    • Zehe, C.1    Engling, A.2    Wegehingel, S.3    Schafer, T.4    Nickel, W.5
  • 59
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes RC. Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta 1999;1473: 172-185.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 60
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller M, Ruegg A, Werner S, Beer HD. Active caspase-1 is a regulator of unconventional protein secretion. Cell 2008;132:818-831.
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.D.4
  • 62
    • 77952299611 scopus 로고    scopus 로고
    • The Src, Syk, and Tec family kinases: distinct types of molecular switches
    • Bradshaw JM. The Src, Syk, and Tec family kinases: distinct types of molecular switches. Cell Signal 2010;22:1175-1184.
    • (2010) Cell Signal , vol.22 , pp. 1175-1184
    • Bradshaw, J.M.1
  • 63
    • 61849110214 scopus 로고    scopus 로고
    • Tec kinases regulate T-lymphocyte development and function: new insights into the roles of Itk and Rlk/Txk
    • Readinger JA, Mueller KL, Venegas AM, Horai R, Schwartzberg PL. Tec kinases regulate T-lymphocyte development and function: new insights into the roles of Itk and Rlk/Txk. Immunol Rev 2009;228:93-114.
    • (2009) Immunol Rev , vol.228 , pp. 93-114
    • Readinger, J.A.1    Mueller, K.L.2    Venegas, A.M.3    Horai, R.4    Schwartzberg, P.L.5
  • 64
    • 67949123338 scopus 로고    scopus 로고
    • Chloroplast biogenesis: diversity and regulation of the protein import apparatus
    • Kessler F, Schnell D. Chloroplast biogenesis: diversity and regulation of the protein import apparatus. Curr Opin Cell Biol 2009;21:494-500.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 494-500
    • Kessler, F.1    Schnell, D.2
  • 65
    • 0036883476 scopus 로고    scopus 로고
    • Protein import into chloroplasts
    • Soll J. Protein import into chloroplasts. Curr Opin Plant Biol 2002;5:529-535.
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 529-535
    • Soll, J.1
  • 66
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles
    • Andrei C, Dazzi C, Lotti L, Torrisi MR, Chimini G, Rubartelli A. The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles. Mol Biol Cell 1999;10:1463-1475.
    • (1999) Mol Biol Cell , vol.10 , pp. 1463-1475
    • Andrei, C.1    Dazzi, C.2    Lotti, L.3    Torrisi, M.R.4    Chimini, G.5    Rubartelli, A.6
  • 67
    • 34548614009 scopus 로고    scopus 로고
    • Nonclassical IL-1 beta secretion stimulated by P2X7 receptors is dependent on inflammasome activation and correlated with exosome release in murine macrophages
    • Qu Y, Franchi L, Nunez G, Dubyak GR. Nonclassical IL-1 beta secretion stimulated by P2X7 receptors is dependent on inflammasome activation and correlated with exosome release in murine macrophages. J Immunol 2007;179:1913-1925.
    • (2007) J Immunol , vol.179 , pp. 1913-1925
    • Qu, Y.1    Franchi, L.2    Nunez, G.3    Dubyak, G.R.4
  • 69
    • 77956791062 scopus 로고    scopus 로고
    • Unconventional secretion of AcbA in Dictyostelium discoideum through a vesicular intermediate
    • Cabral M, Anjard C, Malhotra V, Loomis WF, Kuspa A. Unconventional secretion of AcbA in Dictyostelium discoideum through a vesicular intermediate. Eukaryot Cell 2010;9:1009-1017.
    • (2010) Eukaryot Cell , vol.9 , pp. 1009-1017
    • Cabral, M.1    Anjard, C.2    Malhotra, V.3    Loomis, W.F.4    Kuspa, A.5
  • 70
    • 77955464395 scopus 로고    scopus 로고
    • Role of autophagy in unconventional protein secretion
    • Manjithaya R, Subramani S. Role of autophagy in unconventional protein secretion. Autophagy 2010;6:650-651.
    • (2010) Autophagy , vol.6 , pp. 650-651
    • Manjithaya, R.1    Subramani, S.2
  • 71
    • 0037157841 scopus 로고    scopus 로고
    • The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export
    • Prudovsky I, Bagala C, Tarantini F, Mandinova A, Soldi R, Bellum S, Maciag T. The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export. J Cell Biol 2002;158:201-208.
    • (2002) J Cell Biol , vol.158 , pp. 201-208
    • Prudovsky, I.1    Bagala, C.2    Tarantini, F.3    Mandinova, A.4    Soldi, R.5    Bellum, S.6    Maciag, T.7
  • 74
    • 0027458469 scopus 로고
    • Release, uptake, and effects of extracellular human immunodeficiency virus type 1 Tat protein on cell growth and viral transactivation
    • Ensoli B, Buonaguro L, Barillari G, Fiorelli V, Gendelman R, Morgan RA, Wingfield P, Gallo RC. Release, uptake, and effects of extracellular human immunodeficiency virus type 1 Tat protein on cell growth and viral transactivation. J Virol 1993;67:277-287.
    • (1993) J Virol , vol.67 , pp. 277-287
    • Ensoli, B.1    Buonaguro, L.2    Barillari, G.3    Fiorelli, V.4    Gendelman, R.5    Morgan, R.A.6    Wingfield, P.7    Gallo, R.C.8
  • 75
    • 0037821650 scopus 로고    scopus 로고
    • Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2
    • Peterson EA, Sutherland MR, Nesheim ME, Pryzdial EL. Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2. J Cell Sci 2003;116:2399-2408.
    • (2003) J Cell Sci , vol.116 , pp. 2399-2408
    • Peterson, E.A.1    Sutherland, M.R.2    Nesheim, M.E.3    Pryzdial, E.L.4
  • 76
    • 0035253824 scopus 로고    scopus 로고
    • Plasminogen-mediated matrix invasion and degradation by macrophages is dependent on surface expression of annexin II
    • Falcone DJ, Borth W, Khan KM, Hajjar KA. Plasminogen-mediated matrix invasion and degradation by macrophages is dependent on surface expression of annexin II. Blood 2001;97:777-784.
    • (2001) Blood , vol.97 , pp. 777-784
    • Falcone, D.J.1    Borth, W.2    Khan, K.M.3    Hajjar, K.A.4
  • 77
    • 0025740387 scopus 로고
    • Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland
    • Christmas P, Callaway J, Fallon J, Jones J, Haigler HT. Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland. J Biol Chem 1991;266:2499-2507.
    • (1991) J Biol Chem , vol.266 , pp. 2499-2507
    • Christmas, P.1    Callaway, J.2    Fallon, J.3    Jones, J.4    Haigler, H.T.5
  • 78
    • 3242887228 scopus 로고    scopus 로고
    • Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes
    • Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V. Annexin 2 is a phosphatidylinositol (4, 5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J Cell Sci 2004;117:3473-3480.
    • (2004) J Cell Sci , vol.117 , pp. 3473-3480
    • Rescher, U.1    Ruhe, D.2    Ludwig, C.3    Zobiack, N.4    Gerke, V.5
  • 80
    • 67349253082 scopus 로고    scopus 로고
    • Annexin A2 at the interface between F-actin and membranes enriched in phosphatidylinositol 4,5,-bisphosphate
    • Hayes MJ, Shao DM, Grieve A, Levine T, Bailly M, Moss SE. Annexin A2 at the interface between F-actin and membranes enriched in phosphatidylinositol 4, 5, -bisphosphate. Biochim Biophys Acta 2009;1793:1086-1095.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1086-1095
    • Hayes, M.J.1    Shao, D.M.2    Grieve, A.3    Levine, T.4    Bailly, M.5    Moss, S.E.6
  • 81
    • 28044469061 scopus 로고    scopus 로고
    • Phosphatidylserine membrane domain clustering induced by annexin A2/S100A10 heterotetramer
    • Menke M, Gerke V, Steinem C. Phosphatidylserine membrane domain clustering induced by annexin A2/S100A10 heterotetramer. Biochemistry 2005;44:15296-15303.
    • (2005) Biochemistry , vol.44 , pp. 15296-15303
    • Menke, M.1    Gerke, V.2    Steinem, C.3
  • 82
    • 30044431601 scopus 로고    scopus 로고
    • Phosphoinositide specificity of and mechanism of lipid domain formation by annexin A2-p11 heterotetramer
    • Gokhale NA, Abraham A, Digman MA, Gratton E, Cho W. Phosphoinositide specificity of and mechanism of lipid domain formation by annexin A2-p11 heterotetramer. J Biol Chem 2005;280:42831-42840.
    • (2005) J Biol Chem , vol.280 , pp. 42831-42840
    • Gokhale, N.A.1    Abraham, A.2    Digman, M.A.3    Gratton, E.4    Cho, W.5
  • 83
    • 0032564344 scopus 로고    scopus 로고
    • A transmembrane form of annexin XII detected by site-directed spin labeling
    • Langen R, Isas JM, Hubbell WL, Haigler HT. A transmembrane form of annexin XII detected by site-directed spin labeling. Proc Natl Acad Sci U S A 1998;95:14060-14065.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14060-14065
    • Langen, R.1    Isas, J.M.2    Hubbell, W.L.3    Haigler, H.T.4
  • 84
    • 0021272948 scopus 로고
    • Phosphorylation at a tyrosine residue of lipomodulin in mitogen-stimulated murine thymocytes
    • Hirata F, Matsuda K, Notsu Y, Hattori T. del Carmine R. Phosphorylation at a tyrosine residue of lipomodulin in mitogen-stimulated murine thymocytes. Proc Natl Acad Sci U S A 1984;81:4717-4721.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 4717-4721
    • Hirata, F.1    Matsuda, K.2    Notsu, Y.3    Hattori, T.4    del Carmine, R.5
  • 85
    • 0028972270 scopus 로고
    • "In vitro" phosphorylation of annexin 2 heterotetramer by protein kinase C. Comparative properties of the unphosphorylated and phosphorylated annexin 2 on the aggregation and fusion of chromaffin granule membranes
    • Regnouf F, Sagot I, Delouche B, Devilliers G, Cartaud J, Henry JP, Pradel LA. "In vitro" phosphorylation of annexin 2 heterotetramer by protein kinase C. Comparative properties of the unphosphorylated and phosphorylated annexin 2 on the aggregation and fusion of chromaffin granule membranes. J Biol Chem 1995;270:27143-27150.
    • (1995) J Biol Chem , vol.270 , pp. 27143-27150
    • Regnouf, F.1    Sagot, I.2    Delouche, B.3    Devilliers, G.4    Cartaud, J.5    Henry, J.P.6    Pradel, L.A.7
  • 86
    • 48049120845 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion
    • Rescher U, Ludwig C, Konietzko V, Kharitonenkov A, Gerke V. Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion. J Cell Sci 2008;121:2177-2185.
    • (2008) J Cell Sci , vol.121 , pp. 2177-2185
    • Rescher, U.1    Ludwig, C.2    Konietzko, V.3    Kharitonenkov, A.4    Gerke, V.5


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