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Volumn 427, Issue 6, 2015, Pages 1202-1210

Unconventional secretion of fibroblast growth factor 2 - A novel type of protein translocation across membranes?

Author keywords

fibroblast growth factor 2; formation of lipidic membrane pores; interleukin 1 ; phosphoinositide induced protein oligomerization; unconventional protein secretion

Indexed keywords

CYTOPLASM PROTEIN; FIBROBLAST GROWTH FACTOR 2; SIGNAL RECOGNITION PARTICLE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE;

EID: 84924270143     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.07.012     Document Type: Review
Times cited : (55)

References (68)
  • 1
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • J.E. Rothman, and F.T. Wieland Protein sorting by transport vesicles Science 272 1996 227 234
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 2
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • R. Schekman, and L. Orci Coat proteins and vesicle budding Science 271 1996 1526 1533
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 3
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 5
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • E. Park, and T.A. Rapoport Mechanisms of Sec61/SecY-mediated protein translocation across membranes Annu Rev Biophys 41 2012 21 40
    • (2012) Annu Rev Biophys , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 6
    • 77955049339 scopus 로고    scopus 로고
    • Quality and quantity control at the endoplasmic reticulum
    • R.S. Hegde, and H.L. Ploegh Quality and quantity control at the endoplasmic reticulum Curr Opin Cell Biol 22 2010 437 446
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 437-446
    • Hegde, R.S.1    Ploegh, H.L.2
  • 7
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • R. Sitia, and I. Braakman Quality control in the endoplasmic reticulum protein factory Nature 426 2003 891 894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 8
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • J.E. Rothman Mechanisms of intracellular protein transport Nature 372 1994 55 63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 10
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • W. Nickel The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes Eur J Biochem 270 2003 2109 2119
    • (2003) Eur J Biochem , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 11
    • 0037106614 scopus 로고    scopus 로고
    • Biosynthetic FGF-2 is targeted to non-lipid raft microdomains following translocation to the extracellular surface of CHO cells
    • A. Engling, R. Backhaus, C. Stegmayer, C. Zehe, C. Seelenmeyer, and A. Kehlenbach Biosynthetic FGF-2 is targeted to non-lipid raft microdomains following translocation to the extracellular surface of CHO cells J Cell Sci 115 2002 3619 3631
    • (2002) J Cell Sci , vol.115 , pp. 3619-3631
    • Engling, A.1    Backhaus, R.2    Stegmayer, C.3    Zehe, C.4    Seelenmeyer, C.5    Kehlenbach, A.6
  • 12
    • 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
    • P. Mignatti, T. Morimoto, and D.B. Rifkin 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 151 1992 81 93
    • (1992) J Cell Physiol , vol.151 , pp. 81-93
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 13
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence
    • A. Rubartelli, F. Cozzolino, M. Talio, and R. Sitia A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence EMBO J 9 1990 1503 1510
    • (1990) EMBO J , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 14
    • 0033795350 scopus 로고    scopus 로고
    • Translocation of FGF2 to the cell surface without release into conditioned media [in process citation]
    • C. Trudel, V. Faure-Desire, R.Z. Florkiewicz, and A. Baird Translocation of FGF2 to the cell surface without release into conditioned media [in process citation] J Cell Physiol 185 2000 260 268
    • (2000) J Cell Physiol , vol.185 , pp. 260-268
    • Trudel, C.1    Faure-Desire, V.2    Florkiewicz, R.Z.3    Baird, A.4
  • 16
    • 84890235827 scopus 로고    scopus 로고
    • The interleukin-1 family: Back to the future
    • C. Garlanda, C.A. Dinarello, and A. Mantovani The interleukin-1 family: back to the future Immunity 39 2013 1003 1018
    • (2013) Immunity , vol.39 , pp. 1003-1018
    • Garlanda, C.1    Dinarello, C.A.2    Mantovani, A.3
  • 17
    • 62649139025 scopus 로고    scopus 로고
    • Immunological and inflammatory functions of the interleukin-1 family
    • C.A. Dinarello Immunological and inflammatory functions of the interleukin-1 family Annu Rev Immunol 27 2009 519 550
    • (2009) Annu Rev Immunol , vol.27 , pp. 519-550
    • Dinarello, C.A.1
  • 18
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • L. Pellegrini, D.F. Burke, F. von Delft, B. Mulloy, and T.L. Blundell Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin Nature 407 2000 1029 1034
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 19
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • A.N. Plotnikov, S.R. Hubbard, J. Schlessinger, and M. Mohammadi Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity Cell 101 2000 413 424
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 20
    • 0033635299 scopus 로고    scopus 로고
    • Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization
    • J. Schlessinger, A.N. Plotnikov, O.A. Ibrahimi, A.V. Eliseenkova, B.K. Yeh, and A. Yayon Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization Mol Cell 6 2000 743 750
    • (2000) Mol Cell , vol.6 , pp. 743-750
    • Schlessinger, J.1    Plotnikov, A.N.2    Ibrahimi, O.A.3    Eliseenkova, A.V.4    Yeh, B.K.5    Yayon, A.6
  • 21
    • 0030998098 scopus 로고    scopus 로고
    • Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1 beta
    • G.P.A. Vigers, L.J. Anderson, P. Caffes, and B.J. Brandhuber Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1 beta Nature 386 1997 190 194
    • (1997) Nature , vol.386 , pp. 190-194
    • Vigers, G.P.A.1    Anderson, L.J.2    Caffes, P.3    Brandhuber, B.J.4
  • 22
    • 21844468743 scopus 로고    scopus 로고
    • Unconventional secretory routes: Direct protein export across the plasma membrane of mammalian cells
    • W. Nickel Unconventional secretory routes: direct protein export across the plasma membrane of mammalian cells Traffic 6 2005 607 614
    • (2005) Traffic , vol.6 , pp. 607-614
    • Nickel, W.1
  • 23
    • 1342325441 scopus 로고    scopus 로고
    • Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells
    • T. Schäfer, H. Zentgraf, C. Zehe, B. Brugger, J. Bernhagen, and W. Nickel Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells J Biol Chem 279 2004 6244 6251
    • (2004) J Biol Chem , vol.279 , pp. 6244-6251
    • Schäfer, T.1    Zentgraf, H.2    Zehe, C.3    Brugger, B.4    Bernhagen, J.5    Nickel, W.6
  • 24
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles
    • C. Andrei, C. Dazzi, L. Lotti, M.R. Torrisi, G. Chimini, and A. Rubartelli The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles Mol Biol Cell 10 1999 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
  • 25
    • 84879464160 scopus 로고    scopus 로고
    • Unconventional protein secretion: An evolving mechanism
    • V. Malhotra Unconventional protein secretion: an evolving mechanism EMBO J 32 2013 1660 1664
    • (2013) EMBO J , vol.32 , pp. 1660-1664
    • Malhotra, V.1
  • 26
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta
    • N. Dupont, S. Jiang, M. Pilli, W. Ornatowski, D. Bhattacharya, and V. Deretic Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta EMBO J 30 2011 4701 4711
    • (2011) EMBO J , vol.30 , pp. 4701-4711
    • Dupont, N.1    Jiang, S.2    Pilli, M.3    Ornatowski, W.4    Bhattacharya, D.5    Deretic, V.6
  • 27
    • 3042800587 scopus 로고    scopus 로고
    • Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion: Implications for inflammatory processes
    • C. Andrei, P. Margiocco, A. Poggi, L.V. Lotti, M.R. Torrisi, and A. Rubartelli Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion: implications for inflammatory processes Proc Natl Acad Sci U S A 101 2004 9745 9750
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9745-9750
    • Andrei, C.1    Margiocco, P.2    Poggi, A.3    Lotti, L.V.4    Torrisi, M.R.5    Rubartelli, A.6
  • 28
    • 84892856957 scopus 로고    scopus 로고
    • The secretion of IL-1beta and options for release
    • P. Piccioli, and A. Rubartelli The secretion of IL-1beta and options for release Semin Immunol 25 2013 425 429
    • (2013) Semin Immunol , vol.25 , pp. 425-429
    • Piccioli, P.1    Rubartelli, A.2
  • 29
    • 84855490021 scopus 로고    scopus 로고
    • Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion
    • C. Bruns, J.M. McCaffery, A.J. Curwin, J.M. Duran, and V. Malhotra Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion J Cell Biol 195 2011 979 992
    • (2011) J Cell Biol , vol.195 , pp. 979-992
    • Bruns, C.1    McCaffery, J.M.2    Curwin, A.J.3    Duran, J.M.4    Malhotra, V.5
  • 30
    • 77149155386 scopus 로고    scopus 로고
    • Unconventional secretion of Acb1 is mediated by autophagosomes
    • J.M. Duran, C. Anjard, C. Stefan, W.F. Loomis, and V. Malhotra Unconventional secretion of Acb1 is mediated by autophagosomes J Cell Biol 188 2010 527 536
    • (2010) J Cell Biol , vol.188 , pp. 527-536
    • Duran, J.M.1    Anjard, C.2    Stefan, C.3    Loomis, W.F.4    Malhotra, V.5
  • 31
    • 34547604776 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP is required for unconventional protein secretion during development
    • M.A. Kinseth, C. Anjard, D. Fuller, G. Guizzunti, W.F. Loomis, and V. Malhotra The Golgi-associated protein GRASP is required for unconventional protein secretion during development Cell 130 2007 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
  • 33
    • 84877342306 scopus 로고    scopus 로고
    • Cell biology. Unconventional secretion, unconventional solutions
    • M. Zhang, and R. Schekman Cell biology. Unconventional secretion, unconventional solutions Science 340 2013 559 561
    • (2013) Science , vol.340 , pp. 559-561
    • Zhang, M.1    Schekman, R.2
  • 34
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • E. Latz, T.S. Xiao, and A. Stutz Activation and regulation of the inflammasomes Nat Rev Immunol 13 2013 397 411
    • (2013) Nat Rev Immunol , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 35
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • M. Keller, A. Ruegg, S. Werner, and H.D. Beer Active caspase-1 is a regulator of unconventional protein secretion Cell 132 2008 818 831
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.D.4
  • 36
    • 46349098379 scopus 로고    scopus 로고
    • A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2
    • K. Temmerman, A.D. Ebert, H.M. Muller, I. Sinning, I. Tews, and W. Nickel A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2 Traffic 9 2008 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
  • 37
    • 67649844238 scopus 로고    scopus 로고
    • A novel flow cytometric assay to quantify interactions between proteins and membrane lipids
    • K. Temmerman, and W. Nickel A novel flow cytometric assay to quantify interactions between proteins and membrane lipids J Lipid Res 50 2009 1245 1254
    • (2009) J Lipid Res , vol.50 , pp. 1245-1254
    • Temmerman, K.1    Nickel, W.2
  • 38
    • 79958771663 scopus 로고    scopus 로고
    • The unconventional secretory machinery of fibroblast growth factor 2
    • W. Nickel The unconventional secretory machinery of fibroblast growth factor 2 Traffic 12 2011 799 805
    • (2011) Traffic , vol.12 , pp. 799-805
    • Nickel, W.1
  • 39
    • 84864980066 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-dependent oligomerization of fibroblast growth factor 2 (FGF2) triggers the formation of a lipidic membrane pore implicated in unconventional secretion
    • J.P. Steringer, S. Bleicken, H. Andreas, S. Zacherl, M. Laussmann, and K. Temmerman Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-dependent oligomerization of fibroblast growth factor 2 (FGF2) triggers the formation of a lipidic membrane pore implicated in unconventional secretion J Biol Chem 287 2012 27659 27669
    • (2012) J Biol Chem , vol.287 , pp. 27659-27669
    • Steringer, J.P.1    Bleicken, S.2    Andreas, H.3    Zacherl, S.4    Laussmann, M.5    Temmerman, K.6
  • 40
    • 3142746012 scopus 로고    scopus 로고
    • Lipidic pore formation by the concerted action of proapoptotic BAX and tBID
    • O. Terrones, B. Antonsson, H. Yamaguchi, H.G. Wang, J. Liu, and R.M. Lee Lipidic pore formation by the concerted action of proapoptotic BAX and tBID J Biol Chem 279 2004 30081 30091
    • (2004) J Biol Chem , vol.279 , pp. 30081-30091
    • Terrones, O.1    Antonsson, B.2    Yamaguchi, H.3    Wang, H.G.4    Liu, J.5    Lee, R.M.6
  • 41
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • S. Qian, W. Wang, L. Yang, and H.W. Huang Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores Proc Natl Acad Sci U S A 105 2008 17379 17383
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 42
    • 34547743839 scopus 로고    scopus 로고
    • Unconventional secretion: An extracellular trap for export of fibroblast growth factor 2
    • W. Nickel Unconventional secretion: an extracellular trap for export of fibroblast growth factor 2 J Cell Sci 120 2007 2295 2299
    • (2007) J Cell Sci , vol.120 , pp. 2295-2299
    • Nickel, W.1
  • 43
    • 33750299160 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2
    • C. Zehe, A. Engling, S. Wegehingel, T. Schafer, and W. Nickel Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2 Proc Natl Acad Sci U S A 103 2006 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
  • 44
    • 2342443941 scopus 로고    scopus 로고
    • Unconventional protein secretion: Membrane translocation of FGF-2 does not require protein unfolding
    • R. Backhaus, C. Zehe, S. Wegehingel, A. Kehlenbach, B. Schwappach, and W. Nickel Unconventional protein secretion: membrane translocation of FGF-2 does not require protein unfolding J Cell Sci 117 2004 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
  • 45
    • 70350400642 scopus 로고    scopus 로고
    • An intrinsic quality-control mechanism ensures unconventional secretion of fibroblast growth factor 2 in a folded conformation
    • L.C. Torrado, K. Temmerman, H.M. Muller, M.P. Mayer, C. Seelenmeyer, and R. Backhaus An intrinsic quality-control mechanism ensures unconventional secretion of fibroblast growth factor 2 in a folded conformation J Cell Sci 122 2009 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
  • 46
    • 0033696009 scopus 로고    scopus 로고
    • Tec kinases: A family with multiple roles in immunity
    • W.C. Yang, Y. Collette, J.A. Nunes, and D. Olive Tec kinases: a family with multiple roles in immunity Immunity 12 2000 373 382
    • (2000) Immunity , vol.12 , pp. 373-382
    • Yang, W.C.1    Collette, Y.2    Nunes, J.A.3    Olive, D.4
  • 47
    • 77953367251 scopus 로고    scopus 로고
    • Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion
    • A.D. Ebert, M. Laussmann, S. Wegehingel, L. Kaderali, H. Erfle, and J. Reichert Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion Traffic 11 2010 813 826
    • (2010) Traffic , vol.11 , pp. 813-826
    • Ebert, A.D.1    Laussmann, M.2    Wegehingel, S.3    Kaderali, L.4    Erfle, H.5    Reichert, J.6
  • 48
    • 77957329900 scopus 로고    scopus 로고
    • Pathways of unconventional protein secretion
    • W. Nickel Pathways of unconventional protein secretion Curr Opin Biotechnol 21 2010 621 626
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 621-626
    • Nickel, W.1
  • 49
    • 77952299611 scopus 로고    scopus 로고
    • The Src, Syk, and Tec family kinases: Distinct types of molecular switches
    • J.M. Bradshaw The Src, Syk, and Tec family kinases: distinct types of molecular switches Cell Signal 22 2010 1175 1184
    • (2010) Cell Signal , vol.22 , pp. 1175-1184
    • Bradshaw, J.M.1
  • 50
    • 68249093818 scopus 로고    scopus 로고
    • Targeting the phosphoinositide 3-kinase pathway in cancer
    • P. Liu, H. Cheng, T.M. Roberts, and J.J. Zhao Targeting the phosphoinositide 3-kinase pathway in cancer Nat Rev Drug Discov 8 2009 627 644
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 627-644
    • Liu, P.1    Cheng, H.2    Roberts, T.M.3    Zhao, J.J.4
  • 51
    • 55849145075 scopus 로고    scopus 로고
    • Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells
    • W. Nickel, and M. Seedorf Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells Annu Rev Cell Dev Biol 24 2008 287 308
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 287-308
    • Nickel, W.1    Seedorf, M.2
  • 52
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • W. Nickel, and C. Rabouille Mechanisms of regulated unconventional protein secretion Nat Rev Mol Cell Biol 10 2009 148 155
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 53
    • 84873531806 scopus 로고    scopus 로고
    • Diversity in unconventional protein secretion
    • C. Rabouille, V. Malhotra, and W. Nickel Diversity in unconventional protein secretion J Cell Sci 125 2012 5251 5255
    • (2012) J Cell Sci , vol.125 , pp. 5251-5255
    • Rabouille, C.1    Malhotra, V.2    Nickel, W.3
  • 54
    • 0024375860 scopus 로고
    • The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein
    • J.P. McGrath, and A. Varshavsky The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein Nature 340 1989 400 404
    • (1989) Nature , vol.340 , pp. 400-404
    • McGrath, J.P.1    Varshavsky, A.2
  • 55
    • 0027546252 scopus 로고
    • STE6, the yeast a-factor transporter
    • S. Michaelis STE6, the yeast a-factor transporter Semin Cell Biol 4 1993 17 27
    • (1993) Semin Cell Biol , vol.4 , pp. 17-27
    • Michaelis, S.1
  • 56
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • S. Faham, R.E. Hileman, J.R. Fromm, R.J. Linhardt, and D.C. Rees Heparin structure and interactions with basic fibroblast growth factor Science 271 1996 1116 1120
    • (1996) Science , vol.271 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, J.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 57
    • 45549099915 scopus 로고    scopus 로고
    • Rerouting of fibroblast growth factor 2 to the classical secretory pathway results in post-translational modifications that block binding to heparan sulfate proteoglycans
    • S. Wegehingel, C. Zehe, and W. Nickel Rerouting of fibroblast growth factor 2 to the classical secretory pathway results in post-translational modifications that block binding to heparan sulfate proteoglycans FEBS Lett 582 2008 2387 2392
    • (2008) FEBS Lett , vol.582 , pp. 2387-2392
    • Wegehingel, S.1    Zehe, C.2    Nickel, W.3
  • 58
    • 38149134409 scopus 로고    scopus 로고
    • Functional evolutionary history of the mouse Fgf gene family
    • N. Itoh, and D.M. Ornitz Functional evolutionary history of the mouse Fgf gene family Dev Dyn 237 2008 18 27
    • (2008) Dev Dyn , vol.237 , pp. 18-27
    • Itoh, N.1    Ornitz, D.M.2
  • 59
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim Biophys Acta 1462 1999 55 70
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 60
    • 33644946679 scopus 로고    scopus 로고
    • Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores
    • A.J. Garcia-Saez, M. Coraiola, M.D. Serra, I. Mingarro, P. Muller, and J. Salgado Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores FEBS J 273 2006 971 981
    • (2006) FEBS J , vol.273 , pp. 971-981
    • Garcia-Saez, A.J.1    Coraiola, M.2    Serra, M.D.3    Mingarro, I.4    Muller, P.5    Salgado, J.6
  • 61
    • 0032855497 scopus 로고    scopus 로고
    • Multifaceted activities of the HIV-1 transactivator of transcription, Tat
    • K.T. Jeang, H. Xiao, and E.A. Rich Multifaceted activities of the HIV-1 transactivator of transcription, Tat J Biol Chem 274 1999 28837 28840
    • (1999) J Biol Chem , vol.274 , pp. 28837-28840
    • Jeang, K.T.1    Xiao, H.2    Rich, E.A.3
  • 62
    • 0025344596 scopus 로고
    • Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients
    • B. Ensoli, G. Barillari, S.Z. Salahuddin, R.C. Gallo, and F. Wong-Staal Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients Nature 345 1990 84 86
    • (1990) Nature , vol.345 , pp. 84-86
    • Ensoli, B.1    Barillari, G.2    Salahuddin, S.Z.3    Gallo, R.C.4    Wong-Staal, F.5
  • 63
    • 0027458469 scopus 로고
    • Release, uptake, and effects of extracellular human immunodeficiency virus type 1 Tat protein on cell growth and viral transactivation
    • B. Ensoli, L. Buonaguro, G. Barillari, V. Fiorelli, R. Gendelman, and R.A. Morgan Release, uptake, and effects of extracellular human immunodeficiency virus type 1 Tat protein on cell growth and viral transactivation J Virol 67 1993 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
  • 64
    • 0034633618 scopus 로고    scopus 로고
    • Selective CXCR4 antagonism by Tat: Implications for in vivo expansion of coreceptor use by HIV-1
    • H. Xiao, C. Neuveut, H.L. Tiffany, M. Benkirane, E.A. Rich, and P.M. Murphy Selective CXCR4 antagonism by Tat: implications for in vivo expansion of coreceptor use by HIV-1 Proc Natl Acad Sci U S A 97 2000 11466 11471
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11466-11471
    • Xiao, H.1    Neuveut, C.2    Tiffany, H.L.3    Benkirane, M.4    Rich, E.A.5    Murphy, P.M.6
  • 65
    • 77953934642 scopus 로고    scopus 로고
    • HIV-1 Tat is unconventionally secreted through the plasma membrane
    • F. Rayne, S. Debaisieux, A. Bonhoure, and B. Beaumelle HIV-1 Tat is unconventionally secreted through the plasma membrane Cell Biol Int 34 2010 409 413
    • (2010) Cell Biol Int , vol.34 , pp. 409-413
    • Rayne, F.1    Debaisieux, S.2    Bonhoure, A.3    Beaumelle, B.4
  • 66
    • 77951498245 scopus 로고    scopus 로고
    • Phosphatidylinositol-(4,5)-bisphosphate enables efficient secretion of HIV-1 Tat by infected T-cells
    • F. Rayne, S. Debaisieux, H. Yezid, Y.L. Lin, C. Mettling, and K. Konate Phosphatidylinositol-(4,5)-bisphosphate enables efficient secretion of HIV-1 Tat by infected T-cells EMBO J 29 2010 1348 1362
    • (2010) EMBO J , vol.29 , pp. 1348-1362
    • Rayne, F.1    Debaisieux, S.2    Yezid, H.3    Lin, Y.L.4    Mettling, C.5    Konate, K.6


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