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Volumn 190, Issue 6, 2010, Pages 1053-1065

Phosphoinositide 3-kinase δ regulates membrane fission of Golgi carriers for selective cytokine secretion

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIN II; LIPOPOLYSACCHARIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE DELTA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; DYNAMIN; ISOENZYME; PIK3CD PROTEIN, MOUSE; SMALL INTERFERING RNA;

EID: 77957194863     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201001028     Document Type: Article
Times cited : (53)

References (67)
  • 2
    • 33751168961 scopus 로고    scopus 로고
    • The formation of TGN-to-plasma-membrane transport carriers
    • doi:10.1146/annurev.cellbio.21.012704.133126
    • Bard, F., and V. Malhotra. 2006. The formation of TGN-to-plasma-membrane transport carriers. Annu. Rev. Cell Dev. Biol. 22:439-455. doi:10.1146/annurev. cellbio.21.012704.133126
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 439-455
    • Bard, F.1    Malhotra, V.2
  • 3
    • 0032922359 scopus 로고    scopus 로고
    • The role of tumor necrosis factor in health and disease
    • Beutler, B.A. 1999. The role of tumor necrosis factor in health and disease. J. Rheumatol. Suppl. 57:16-21.
    • (1999) J. Rheumatol. Suppl. , vol.57 , pp. 16-21
    • Beutler, B.A.1
  • 4
    • 37049004196 scopus 로고    scopus 로고
    • AP-1 and ARF1 control endosomal dynamics at sites of FcR mediated phagocytosis
    • doi:10.1091/mbc.E07-04-0392
    • Braun, V., C. Deschamps, G. Raposo, P. Benaroch, A. Benmerah, P. Chavrier, and F. Niedergang. 2007. AP-1 and ARF1 control endosomal dynamics at sites of FcR mediated phagocytosis. Mol. Biol. Cell. 18:4921-4931. doi:10.1091/mbc.E07-04-0392
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4921-4931
    • Braun, V.1    Deschamps, C.2    Raposo, G.3    Benaroch, P.4    Benmerah, A.5    Chavrier, P.6    Niedergang, F.7
  • 5
    • 0034094514 scopus 로고    scopus 로고
    • Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin
    • Cao, H., H.M. Thompson, E.W. Krueger, and M.A. McNiven. 2000. Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin. J. Cell Sci. 113:1993-2002.
    • (2000) J. Cell Sci. , vol.113 , pp. 1993-2002
    • Cao, H.1    Thompson, H.M.2    Krueger, E.W.3    McNiven, M.A.4
  • 6
    • 0030840865 scopus 로고    scopus 로고
    • Phospholipase D stimulates release of nascent secretory vesicles from the trans-Golgi network
    • doi:10.1083/jcb.138.3.495
    • Chen, Y.G., A. Siddhanta, C.D. Austin, S.M. Hammond, T.C. Sung, M.A. Frohman, A.J. Morris, and D. Shields. 1997. Phospholipase D stimulates release of nascent secretory vesicles from the trans-Golgi network. J. Cell Biol. 138:495-504. doi:10.1083/jcb.138.3.495
    • (1997) J. Cell Biol. , vol.138 , pp. 495-504
    • Chen, Y.G.1    Siddhanta, A.2    Austin, C.D.3    Hammond, S.M.4    Sung, T.C.5    Frohman, M.A.6    Morris, A.J.7    Shields, D.8
  • 8
    • 0033048782 scopus 로고    scopus 로고
    • Membrane tubule-mediated reassembly and maintenance of the Golgi complex is disrupted by phospholipase A2 antagonists
    • de Figueiredo, P., R.S. Polizotto, D. Drecktrah, and W.J. Brown. 1999. Membrane tubule-mediated reassembly and maintenance of the Golgi complex is disrupted by phospholipase A2 antagonists. Mol. Biol. Cell. 10:1763-1782.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1763-1782
    • De Figueiredo, P.1    Polizotto, R.S.2    Drecktrah, D.3    Brown, W.J.4
  • 9
    • 41149148605 scopus 로고    scopus 로고
    • Exiting the Golgi complex
    • doi:10.1038/nrm2378
    • De Matteis, M.A., and A. Luini. 2008. Exiting the Golgi complex. Nat. Rev. Mol. Cell Biol. 9:273-284. doi:10.1038/nrm2378
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 273-284
    • De Matteis, M.A.1    Luini, A.2
  • 10
    • 1342292522 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: Diverse roles in immune cell activation
    • doi:10.1146/annurev.immunol.22.012703.104721
    • Deane, J.A., and D.A. Fruman. 2004. Phosphoinositide 3-kinase: diverse roles in immune cell activation. Annu. Rev. Immunol. 22:563-598. doi:10.1146/annurev.immunol.22.012703.104721
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 563-598
    • Deane, J.A.1    Fruman, D.A.2
  • 11
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • doi:10.1038/nature05185
    • Di Paolo, G., and P. De Camilli. 2006. Phosphoinositides in cell regulation and membrane dynamics. Nature. 443:651-657. doi:10.1038/nature05185
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 12
    • 67349280350 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-kinase p110 delta in TLR4- and TLR9-mediated B cell cytokine production and differentiation
    • doi:10.1016/j.molimm.2009.03.010
    • Dil, N., and A.J. Marshall. 2009. Role of phosphoinositide 3-kinase p110 delta in TLR4- and TLR9-mediated B cell cytokine production and differentiation. Mol. Immunol. 46:1970-1978. doi:10.1016/j.molimm.2009.03.010
    • (2009) Mol. Immunol. , vol.46 , pp. 1970-1978
    • Dil, N.1    Marshall, A.J.2
  • 13
    • 0034697119 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles
    • doi:10.1074/jbc.275.16.11943
    • Domin, J., I. Gaidarov, M.E. Smith, J.H. Keen, and M.D. Waterfield. 2000. The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles. J. Biol. Chem. 275:11943-11950. doi:10.1074/jbc.275.16.11943
    • (2000) J. Biol. Chem. , vol.275 , pp. 11943-11950
    • Domin, J.1    Gaidarov, I.2    Smith, M.E.3    Keen, J.H.4    Waterfield, M.D.5
  • 14
    • 0031663503 scopus 로고    scopus 로고
    • Phosphoinositide kinases
    • doi:10.1146/annurev.biochem.67.1.481
    • Fruman, D.A., R.E. Meyers, and L.C. Cantley. 1998. Phosphoinositide kinases. Annu. Rev. Biochem. 67:481-507. doi:10.1146/annurev.biochem.67.1.481
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 481-507
    • Fruman, D.A.1    Meyers, R.E.2    Cantley, L.C.3
  • 15
    • 0035103107 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking
    • doi:10.1016/S1097-2765(01)00191-5
    • Gaidarov, I., M.E. Smith, J. Domin, and J.H. Keen. 2001. The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking. Mol. Cell. 7:443-449. doi:10.1016/S1097-2765(01)00191-5
    • (2001) Mol. Cell , vol.7 , pp. 443-449
    • Gaidarov, I.1    Smith, M.E.2    Domin, J.3    Keen, J.H.4
  • 16
    • 2442717709 scopus 로고    scopus 로고
    • Domains of the TGN: Coats, tethers and G proteins
    • doi:10.1111/j.1398-9219.2004.00182.x
    • Gleeson, P.A., J.G. Lock, M.R. Luke, and J.L. Stow. 2004. Domains of the TGN: coats, tethers and G proteins. Traffic. 5:315-326. doi:10.1111/j.1398-9219. 2004.00182.x
    • (2004) Traffic , vol.5 , pp. 315-326
    • Gleeson, P.A.1    Lock, J.G.2    Luke, M.R.3    Stow, J.L.4
  • 17
    • 0033194151 scopus 로고    scopus 로고
    • ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex
    • doi:10.1038/12993
    • Godi, A., P. Pertile, R. Meyers, P. Marra, G. Di Tullio, C. Iurisci, A. Luini, D. Corda, and M.A. De Matteis. 1999. ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex. Nat. Cell Biol. 1:280-287. doi:10.1038/12993
    • (1999) Nat. Cell Biol. , vol.1 , pp. 280-287
    • Godi, A.1    Pertile, P.2    Meyers, R.3    Marra, P.4    Di Tullio, G.5    Iurisci, C.6    Luini, A.7    Corda, D.8    De Matteis, M.A.9
  • 19
    • 36249032544 scopus 로고    scopus 로고
    • The macrophage: Past, present and future
    • doi:10.1002/eji.200737638
    • Gordon, S. 2007. The macrophage: past, present and future. Eur. J. Immunol. 37(Suppl 1):S9-S17. doi:10.1002/eji.200737638
    • (2007) Eur. J. Immunol. , vol.37 , Issue.SUPPL. 1
    • Gordon, S.1
  • 20
    • 26944446652 scopus 로고    scopus 로고
    • Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex
    • doi:10.1038/ncb1289
    • Hausser, A., P. Storz, S. Märtens, G. Link, A. Toker, and K. Pfizenmaier. 2005. Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex. Nat. Cell Biol. 7:880-886. doi:10.1038/ncb1289
    • (2005) Nat. Cell Biol. , vol.7 , pp. 880-886
    • Hausser, A.1    Storz, P.2    Märtens, S.3    Link, G.4    Toker, A.5    Pfizenmaier, K.6
  • 21
    • 0033574528 scopus 로고    scopus 로고
    • Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles
    • doi:10.1074/jbc.274.16.10743
    • Heimann, K., J.M. Percival, R. Weinberger, P. Gunning, and J.L. Stow. 1999. Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles. J. Biol. Chem. 274:10743-10750. doi:10.1074/jbc.274.16. 10743
    • (1999) J. Biol. Chem. , vol.274 , pp. 10743-10750
    • Heimann, K.1    Percival, J.M.2    Weinberger, R.3    Gunning, P.4    Stow, J.L.5
  • 22
    • 0031457328 scopus 로고    scopus 로고
    • Association of a phosphatidylinositol-specific 3-kinase with a human trans-Golgi network resident protein
    • doi:10.1016/S0960-9822(06)00418-0
    • Hickinson, D.M., J.M. Lucocq, M.C. Towler, S. Clough, J. James, S.R. James, C.P. Downes, and S. Ponnambalam. 1997. Association of a phosphatidylinositol-specific 3-kinase with a human trans-Golgi network resident protein. Curr. Biol. 7:987-990. doi:10.1016/S0960-9822(06)00418-0
    • (1997) Curr. Biol. , vol.7 , pp. 987-990
    • Hickinson, D.M.1    Lucocq, J.M.2    Towler, M.C.3    Clough, S.4    James, J.5    James, S.R.6    Downes, C.P.7    Ponnambalam, S.8
  • 23
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells
    • doi:10.1083/jcb.143.6.1485
    • Hirschberg, K., C.M. Miller, J. Ellenberg, J.F. Presley, E.D. Siggia, R.D. Phair, and J. Lippincott-Schwartz. 1998. Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143:1485-1503. doi:10.1083/jcb.143. 6.1485
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6    Lippincott-Schwartz, J.7
  • 24
    • 0021044136 scopus 로고
    • Optimal conditions for proliferation of bone marrow-derived mouse macrophages in culture: The roles of CSF-1, serum, Ca2+, and adherence
    • doi:10.1002/jcp.1041170209
    • Hume, D.A., and S. Gordon. 1983. Optimal conditions for proliferation of bone marrow-derived mouse macrophages in culture: the roles of CSF-1, serum, Ca2+, and adherence. J. Cell. Physiol. 117:189-194. doi:10.1002/jcp.1041170209
    • (1983) J. Cell. Physiol. , vol.117 , pp. 189-194
    • Hume, D.A.1    Gordon, S.2
  • 26
    • 67549134810 scopus 로고    scopus 로고
    • Exocytosis of post-Golgi vesicles is regulated by components of the endocytic machinery
    • doi:10.1016/j.cell.2009.04.064
    • Jaiswal, J.K., V.M. Rivera, and S.M. Simon. 2009. Exocytosis of post-Golgi vesicles is regulated by components of the endocytic machinery. Cell. 137:1308-1319. doi:10.1016/j.cell.2009.04.064
    • (2009) Cell , vol.137 , pp. 1308-1319
    • Jaiswal, J.K.1    Rivera, V.M.2    Simon, S.M.3
  • 27
    • 0033538345 scopus 로고    scopus 로고
    • Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D
    • doi:10.1016/S0092-8674(00)80606-6
    • Jamora, C., N. Yamanouye, J. Van Lint, J. Laudenslager, J.R. Vandenheede, D.J. Faulkner, and V. Malhotra. 1999. Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D. Cell. 98:59-68. doi:10.1016/S0092-8674(00)80606-6
    • (1999) Cell , vol.98 , pp. 59-68
    • Jamora, C.1    Yamanouye, N.2    Van Lint, J.3    Laudenslager, J.4    Vandenheede, J.R.5    Faulkner, D.J.6    Malhotra, V.7
  • 28
    • 0030720512 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN
    • doi:10.1083/jcb.139.2.339
    • Jones, S.M., and K.E. Howell. 1997. Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN. J. Cell Biol. 139:339-349. doi:10.1083/jcb.139.2.339
    • (1997) J. Cell Biol. , vol.139 , pp. 339-349
    • Jones, S.M.1    Howell, K.E.2
  • 29
    • 0027240379 scopus 로고
    • A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network
    • doi:10.1083/jcb.122.4.775
    • Jones, S.M., J.R. Crosby, J. Salamero, and K.E. Howell. 1993. A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. J. Cell Biol. 122:775-788. doi:10.1083/jcb.122.4.775
    • (1993) J. Cell Biol. , vol.122 , pp. 775-788
    • Jones, S.M.1    Crosby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 30
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • doi:10.1126/science.279.5350.573
    • Jones, S.M., K.E. Howell, J.R. Henley, H. Cao, and M.A. McNiven. 1998. Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science. 279:573-577. doi:10.1126/science.279.5350.573
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 31
    • 0037695593 scopus 로고    scopus 로고
    • Essential, nonredundant role for the phosphoinositide 3-kinase p110delta in signaling by the B-cell receptor complex
    • doi:10.1128/MCB.22.24.8580-8591.2002
    • Jou, S.T., N. Carpino, Y. Takahashi, R. Piekorz, J.R. Chao, N. Carpino, D. Wang, and J.N. Ihle. 2002. Essential, nonredundant role for the phosphoinositide 3-kinase p110delta in signaling by the B-cell receptor complex. Mol. Cell. Biol. 22:8580-8591. doi:10.1128/MCB.22.24.8580-8591.2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8580-8591
    • Jou, S.T.1    Carpino, N.2    Takahashi, Y.3    Piekorz, R.4    Chao, J.R.5    Carpino, N.6    Wang, D.7    Ihle, J.N.8
  • 32
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • doi:10.1038/35055042
    • Keller, P., D. Toomre, E. Díaz, J. White, and K. Simons. 2001. Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat. Cell Biol. 3:140-149. doi:10.1038/35055042
    • (2001) Nat. Cell Biol. , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Díaz, E.3    White, J.4    Simons, K.5
  • 33
    • 36148992966 scopus 로고    scopus 로고
    • The p110delta catalytic isoform of PI3K is a key player in NK-cell development and cytokine secretion
    • doi:10.1182/blood-2007-02-075366
    • Kim, N., A. Saudemont, L. Webb, M. Camps, T. Ruckle, E. Hirsch, M. Turner, and F. Colucci. 2007. The p110delta catalytic isoform of PI3K is a key player in NK-cell development and cytokine secretion. Blood. 110:3202-3208. doi:10.1182/blood-2007-02-075366
    • (2007) Blood , vol.110 , pp. 3202-3208
    • Kim, N.1    Saudemont, A.2    Webb, L.3    Camps, M.4    Ruckle, T.5    Hirsch, E.6    Turner, M.7    Colucci, F.8
  • 34
    • 0033794484 scopus 로고    scopus 로고
    • Kinesin and dynamin are required for post-Golgi transport of a plasma-membrane protein
    • doi:10.1038/35000081
    • Kreitzer, G., A. Marmorstein, P. Okamoto, R. Vallee, and E. Rodriguez-Boulan. 2000. Kinesin and dynamin are required for post-Golgi transport of a plasma-membrane protein. Nat. Cell Biol. 2:125-127. doi:10.1038/35000081
    • (2000) Nat. Cell Biol. , vol.2 , pp. 125-127
    • Kreitzer, G.1    Marmorstein, A.2    Okamoto, P.3    Vallee, R.4    Rodriguez-Boulan, E.5
  • 35
    • 42149168460 scopus 로고    scopus 로고
    • A trans-Golgi network golgin is required for the regulated secretion of TNF in activated macrophages in vivo
    • doi:10.1073/pnas.0800137105
    • Lieu, Z.Z., J.G. Lock, L.A. Hammond, N.L. La Gruta, J.L. Stow, and P.A. Gleeson. 2008. A trans-Golgi network golgin is required for the regulated secretion of TNF in activated macrophages in vivo. Proc. Natl. Acad. Sci. USA. 105:3351-3356. doi:10.1073/pnas.0800137105
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3351-3356
    • Lieu, Z.Z.1    Lock, J.G.2    Hammond, L.A.3    La Gruta, N.L.4    Stow, J.L.5    Gleeson, P.A.6
  • 36
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • doi:10.1016/S0092-8674(01)00228-8
    • Liljedahl, M., Y. Maeda, A. Colanzi, I. Ayala, J. Van Lint, and V. Malhotra. 2001. Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell. 104:409-420. doi:10.1016/S0092-8674(01)00228-8
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 37
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • doi:10.1242/jcs.02855
    • Lindmo, K., and H. Stenmark. 2006. Regulation of membrane traffic by phosphoinositide 3-kinases. J. Cell Sci. 119:605-614. doi:10.1242/jcs.02855
    • (2006) J. Cell Sci. , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 38
    • 27744468751 scopus 로고    scopus 로고
    • E-cadherin transport from the trans-Golgi network in tubulovesicular carriers is selectively regulated by golgin-97
    • doi:10.1111/j.1600-0854.2005.00349.x
    • Lock, J.G., L.A. Hammond, F. Houghton, P.A. Gleeson, and J.L. Stow. 2005. E-cadherin transport from the trans-Golgi network in tubulovesicular carriers is selectively regulated by golgin-97. Traffic. 6:1142-1156. doi:10.1111/j.1600-0854.2005.00349.x
    • (2005) Traffic , vol.6 , pp. 1142-1156
    • Lock, J.G.1    Hammond, L.A.2    Houghton, F.3    Gleeson, P.A.4    Stow, J.L.5
  • 39
    • 33646892646 scopus 로고    scopus 로고
    • Dynasore, a cell-permeable inhibitor of dynamin
    • doi:10.1016/j.devcel.2006.04.002
    • Macia, E., M. Ehrlich, R. Massol, E. Boucrot, C. Brunner, and T. Kirchhausen. 2006. Dynasore, a cell-permeable inhibitor of dynamin. Dev. Cell. 10:839-850. doi:10.1016/j.devcel.2006.04.002
    • (2006) Dev. Cell , vol.10 , pp. 839-850
    • Macia, E.1    Ehrlich, M.2    Massol, R.3    Boucrot, E.4    Brunner, C.5    Kirchhausen, T.6
  • 40
    • 34347399793 scopus 로고    scopus 로고
    • Subcompartments of the macrophage recycling endosome direct the differential secretion of IL-6 and TNFalpha
    • doi:10.1083/jcb.200612131
    • Manderson, A.P., J.G. Kay, L.A. Hammond, D.L. Brown, and J.L. Stow. 2007. Subcompartments of the macrophage recycling endosome direct the differential secretion of IL-6 and TNFalpha. J. Cell Biol. 178:57-69. doi:10.1083/jcb. 200612131
    • (2007) J. Cell Biol. , vol.178 , pp. 57-69
    • Manderson, A.P.1    Kay, J.G.2    Hammond, L.A.3    Brown, D.L.4    Stow, J.L.5
  • 41
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • doi:10.1146/annurev.cellbio.14.1.231
    • Martin, T.F. 1998. Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu. Rev. Cell Dev. Biol. 14:231-264. doi:10.1146/annurev.cellbio. 14.1.231
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 231-264
    • Martin, T.F.1
  • 42
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • doi:10.1016/S0092-8674(00)81687-6
    • Mellman, I., and G. Warren. 2000. The road taken: past and future foundations of membrane traffic. Cell. 100:99-112. doi:10.1016/S0092-8674(00) 81687-6
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 43
    • 26244461921 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase C2alpha is essential for ATP-dependent priming of neurosecretory granule exocytosis
    • doi:10.1091/mbc.E05-02-0171
    • Meunier, F.A., S.L. Osborne, G.R. Hammond, F.T. Cooke, P.J. Parker, J. Domin, and G. Schiavo. 2005. Phosphatidylinositol 3-kinase C2alpha is essential for ATP-dependent priming of neurosecretory granule exocytosis. Mol. Biol. Cell. 16:4841-4851. doi:10.1091/mbc.E05-02-0171
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4841-4851
    • Meunier, F.A.1    Osborne, S.L.2    Hammond, G.R.3    Cooke, F.T.4    Parker, P.J.5    Domin, J.6    Schiavo, G.7
  • 44
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain - A novel Golgi-targeting domain found in several coiled-coil proteins
    • doi:10.1016/S0960-9822(99)80166-3
    • Munro, S., and B.J. Nichols. 1999. The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins. Curr. Biol. 9:377-380. doi:10.1016/S0960-9822(99)80166-3
    • (1999) Curr. Biol. , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 45
    • 28544452195 scopus 로고    scopus 로고
    • A role for the phagosome in cytokine secretion
    • doi:10.1126/science.1120225
    • Murray, R.Z., J.G. Kay, D.G. Sangermani, and J.L. Stow. 2005a. A role for the phagosome in cytokine secretion. Science. 310:1492-1495. doi:10.1126/science.1120225
    • (2005) Science , vol.310 , pp. 1492-1495
    • Murray, R.Z.1    Kay, J.G.2    Sangermani, D.G.3    Stow, J.L.4
  • 46
    • 15444379089 scopus 로고    scopus 로고
    • Syntaxin 6 and Vti1b form a novel SNARE complex, which is up-regulated in activated macrophages to facilitate exocytosis of tumor necrosis Factor-alpha
    • doi:10.1074/jbc.M414420200
    • Murray, R.Z., F.G. Wylie, T. Khromykh, D.A. Hume, and J.L. Stow. 2005b. Syntaxin 6 and Vti1b form a novel SNARE complex, which is up-regulated in activated macrophages to facilitate exocytosis of tumor necrosis Factor-alpha. J. Biol. Chem. 280:10478-10483. doi:10.1074/jbc.M414420200
    • (2005) J. Biol. Chem. , vol.280 , pp. 10478-10483
    • Murray, R.Z.1    Wylie, F.G.2    Khromykh, T.3    Hume, D.A.4    Stow, J.L.5
  • 47
    • 0038549067 scopus 로고    scopus 로고
    • PI3K in lymphocyte development, differentiation and activation
    • doi:10.1038/nri1056
    • Okkenhaug, K., and B. Vanhaesebroeck. 2003. PI3K in lymphocyte development, differentiation and activation. Nat. Rev. Immunol. 3:317-330. doi:10.1038/nri1056
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 317-330
    • Okkenhaug, K.1    Vanhaesebroeck, B.2
  • 49
    • 0347786911 scopus 로고    scopus 로고
    • The t-SNARE syntaxin 4 is regulated during macrophage activation to function in membrane traffic and cytokine secretion
    • doi:10.1016/S0960-9822(03)00006-X
    • Pagan, J.K., F.G. Wylie, S. Joseph, C. Widberg, N.J. Bryant, D.E. James, and J.L. Stow. 2003. The t-SNARE syntaxin 4 is regulated during macrophage activation to function in membrane traffic and cytokine secretion. Curr. Biol. 13:156-160. doi:10.1016/S0960-9822(03)00006-X
    • (2003) Curr. Biol. , vol.13 , pp. 156-160
    • Pagan, J.K.1    Wylie, F.G.2    Joseph, S.3    Widberg, C.4    Bryant, N.J.5    James, D.E.6    Stow, J.L.7
  • 50
    • 34447299716 scopus 로고    scopus 로고
    • The p110delta isoform of PI 3-kinase negatively controls RhoA and PTEN
    • doi:10.1038/sj.emboj.7601763
    • Papakonstanti, E.A., A.J. Ridley, and B. Vanhaesebroeck. 2007. The p110delta isoform of PI 3-kinase negatively controls RhoA and PTEN. EMBO J. 26:3050-3061. doi:10.1038/sj.emboj.7601763
    • (2007) EMBO J. , vol.26 , pp. 3050-3061
    • Papakonstanti, E.A.1    Ridley, A.J.2    Vanhaesebroeck, B.3
  • 51
    • 0031587403 scopus 로고    scopus 로고
    • Wortmannin, a specific inhibitor of phosphatidylinositol-3-kinase, enhances LPS-induced NO production from murine peritoneal macrophages
    • doi:10.1006/bbrc.1997.7722
    • Park, Y.C., C.H. Lee, H.S. Kang, H.T. Chung, and H.D. Kim. 1997. Wortmannin, a specific inhibitor of phosphatidylinositol-3-kinase, enhances LPS-induced NO production from murine peritoneal macrophages. Biochem. Biophys. Res. Commun. 240:692-696. doi:10.1006/bbrc.1997.7722
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 692-696
    • Park, Y.C.1    Lee, C.H.2    Kang, H.S.3    Chung, H.T.4    Kim, H.D.5
  • 52
    • 0034627793 scopus 로고    scopus 로고
    • Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane
    • doi:10.1083/jcb.148.1.45
    • Polishchuk, R.S., E.V. Polishchuk, P. Marra, S. Alberti, R. Buccione, A. Luini, and A.A. Mironov. 2000. Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane. J. Cell Biol. 148:45-58. doi:10.1083/jcb.148.1.45
    • (2000) J. Cell Biol. , vol.148 , pp. 45-58
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Marra, P.3    Alberti, S.4    Buccione, R.5    Luini, A.6    Mironov, A.A.7
  • 54
    • 0037369696 scopus 로고    scopus 로고
    • Essential role of phosphoinositide 3-kinase delta in neutrophil directional movement
    • Sadhu, C., B. Masinovsky, K. Dick, C.G. Sowell, and D.E. Staunton. 2003. Essential role of phosphoinositide 3-kinase delta in neutrophil directional movement. J. Immunol. 170:2647-2654.
    • (2003) J. Immunol. , vol.170 , pp. 2647-2654
    • Sadhu, C.1    Masinovsky, B.2    Dick, K.3    Sowell, C.G.4    Staunton, D.E.5
  • 55
    • 0034071125 scopus 로고    scopus 로고
    • Localization and post-Golgi trafficking of tumor necrosis factor-alpha in macrophages
    • doi:10.1089/107999000312379
    • Shurety, W., A. Merino-Trigo, D. Brown, D.A. Hume, and J.L. Stow. 2000. Localization and post-Golgi trafficking of tumor necrosis factor-alpha in macrophages. J. Interferon Cytokine Res. 20:427-438. doi:10.1089/107999000312379
    • (2000) J. Interferon Cytokine Res. , vol.20 , pp. 427-438
    • Shurety, W.1    Merino-Trigo, A.2    Brown, D.3    Hume, D.A.4    Stow, J.L.5
  • 56
    • 0032516854 scopus 로고    scopus 로고
    • Vesicle budding on Golgi membranes: Regulation by G proteins and myosin motors
    • doi:10.1016/S0167-4889(98)00055-X
    • Stow, J.L., and K. Heimann. 1998. Vesicle budding on Golgi membranes: regulation by G proteins and myosin motors. Biochim. Biophys. Acta. 1404:161-171. doi:10.1016/S0167-4889(98)00055-X
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 161-171
    • Stow, J.L.1    Heimann, K.2
  • 57
    • 33845210867 scopus 로고    scopus 로고
    • SNAREing immunity: The role of SNAREs in the immune system
    • doi:10.1038/nri1980
    • Stow, J.L., A.P. Manderson, and R.Z. Murray. 2006. SNAREing immunity: the role of SNAREs in the immune system. Nat. Rev. Immunol. 6:919-929. doi:10.1038/nri1980
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 919-929
    • Stow, J.L.1    Manderson, A.P.2    Murray, R.Z.3
  • 58
    • 68349117545 scopus 로고    scopus 로고
    • Cytokine secretion in macrophages and other cells: Pathways and mediators
    • doi:10.1016/j.imbio.2008.11.005
    • Stow, J.L., P.C. Low, C. Offenhäuser, and D. Sangermani. 2009. Cytokine secretion in macrophages and other cells: pathways and mediators. Immunobiology. 214:601-612. doi:10.1016/j.imbio.2008.11.005
    • (2009) Immunobiology , vol.214 , pp. 601-612
    • Stow, J.L.1    Low, P.C.2    Offenhäuser, C.3    Sangermani, D.4
  • 59
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • doi:10.1006/excr.1999.4701
    • Vanhaesebroeck, B., and M.D. Waterfield. 1999. Signaling by distinct classes of phosphoinositide 3-kinases. Exp. Cell Res. 253:239-254. doi:10.1006/excr.1999.4701
    • (1999) Exp. Cell Res. , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 62
    • 16244393685 scopus 로고    scopus 로고
    • Signalling by PI3K isoforms: Insights from gene-targeted mice
    • doi:10.1016/j.tibs.2005.02.008
    • Vanhaesebroeck, B., K. Ali, A. Bilancio, B. Geering, and L.C. Foukas. 2005. Signalling by PI3K isoforms: insights from gene-targeted mice. Trends Biochem. Sci. 30:194-204. doi:10.1016/j.tibs.2005.02.008
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 194-204
    • Vanhaesebroeck, B.1    Ali, K.2    Bilancio, A.3    Geering, B.4    Foukas, L.C.5
  • 63
    • 0033061480 scopus 로고    scopus 로고
    • GAIP, a Galphai-3-binding protein, is associated with Golgi-derived vesicles and protein trafficking
    • Wylie, F., K. Heimann, T.L. Le, D. Brown, G. Rabnott, and J.L. Stow. 1999. GAIP, a Galphai-3-binding protein, is associated with Golgi-derived vesicles and protein trafficking. Am. J. Physiol. 276:C497-C506.
    • (1999) Am. J. Physiol. , vol.276
    • Wylie, F.1    Heimann, K.2    Le, T.L.3    Brown, D.4    Rabnott, G.5    Stow, J.L.6
  • 64
    • 0038444235 scopus 로고    scopus 로고
    • GAIP participates in budding of membrane carriers at the trans- Golgi network
    • Wylie, F.G., J.G. Lock, L. Jamriska, T. Khromykh, D.L. Brown, and J.L. Stow. 2003. GAIP participates in budding of membrane carriers at the trans- Golgi network. Traffic. 4:175-189.
    • (2003) Traffic , vol.4 , pp. 175-189
    • Wylie, F.G.1    Lock, J.G.2    Jamriska, L.3    Khromykh, T.4    Brown, D.L.5    Stow, J.L.6
  • 65
    • 0035830862 scopus 로고    scopus 로고
    • Dynamin II regulates hormone secretion in neuroendocrine cells
    • doi:10.1074/jbc.M006371200
    • Yang, Z., H. Li, Z. Chai, M.J. Fullerton, Y. Cao, B.H. Toh, J.W. Funder, and J.P. Liu. 2001. Dynamin II regulates hormone secretion in neuroendocrine cells. J. Biol. Chem. 276:4251-4260. doi:10.1074/jbc.M006371200
    • (2001) J. Biol. Chem. , vol.276 , pp. 4251-4260
    • Yang, Z.1    Li, H.2    Chai, Z.3    Fullerton, M.J.4    Cao, Y.5    Toh, B.H.6    Funder, J.W.7    Liu, J.P.8
  • 66
    • 28644440953 scopus 로고    scopus 로고
    • A role for BARS at the fission step of COPI vesicle formation from Golgi membrane
    • doi:10.1038/sj.emboj.7600873
    • Yang, J.S., S.Y. Lee, S. Spanò, H. Gad, L. Zhang, Z. Nie, M. Bonazzi, D. Corda, A. Luini, and V.W. Hsu. 2005. A role for BARS at the fission step of COPI vesicle formation from Golgi membrane. EMBO J. 24:4133-4143. doi:10.1038/sj.emboj.7600873
    • (2005) EMBO J. , vol.24 , pp. 4133-4143
    • Yang, J.S.1    Lee, S.Y.2    Spanò, S.3    Gad, H.4    Zhang, L.5    Nie, Z.6    Bonazzi, M.7    Corda, D.8    Luini, A.9    Hsu, V.W.10


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