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Volumn 289, Issue 3, 2014, Pages 1355-1363

Regulated assembly of vacuolar ATPase is increased during cluster disruption-induced maturation of dendritic cells through a phosphatidylinositol 3-Kinase/mTOR-dependent pathway

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN PROCESSING; IMMUNE TOLERANCES; MURINE DENDRITIC CELLS; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 3-KINASE; PROTEIN SYNTHESIS; REGULATORY MECHANISM; TOLL-LIKE RECEPTORS;

EID: 84892639521     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.524561     Document Type: Article
Times cited : (61)

References (48)
  • 2
    • 0029148878 scopus 로고
    • Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products
    • Sallusto, F., Cella, M., Danieli, C., and Lanzavecchia, A. (1995) Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: downregulation by cytokines and bacterial products. J. Exp. Med. 182, 389-400
    • (1995) J. Exp. Med. , vol.182 , pp. 389-400
    • Sallusto, F.1    Cella, M.2    Danieli, C.3    Lanzavecchia, A.4
  • 3
    • 77249145443 scopus 로고    scopus 로고
    • TLR signaling regulated antigen presentation in dendritic cells
    • Watts, C., West, M. A., and Zaru, R. (2010) TLR signaling regulated antigen presentation in dendritic cells. Curr. Opin. Immunol. 22, 124-130
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 124-130
    • Watts, C.1    West, M.A.2    Zaru, R.3
  • 4
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signaling
    • Akira, S., and Takeda, K. (2004) Toll-like receptor signaling. Nat. Rev. Immunol. 4, 499-511
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 5
    • 79954577277 scopus 로고    scopus 로고
    • TLRsignaling networks: An integration of adaptor molecules, kinases, and cross-talk
    • Brown, J., Wang, H., Hajishengallis, G. N., and Martin, M. (2011) TLRsignaling networks: an integration of adaptor molecules, kinases, and cross-talk. J. Dent. Res. 90, 417-427
    • (2011) J. Dent. Res. , vol.90 , pp. 417-427
    • Brown, J.1    Wang, H.2    Hajishengallis, G.N.3    Martin, M.4
  • 6
    • 0038491296 scopus 로고    scopus 로고
    • Presentation of exogenous antigens on major histocompatibility complex (MHC) class I and MHC class II molecules is differentially regulated during dendritic cell maturation
    • DOI 10.1084/jem.20021542
    • Delamarre, L., Holcombe, H., and Mellman, I. (2003) Presentation of exogenous antigens on major histocompatibility complex (MHC) class I and MHC class II molecules is differentially regulated during dendritic cell maturation. J. Exp. Med. 198, 111-122 (Pubitemid 36870191)
    • (2003) Journal of Experimental Medicine , vol.198 , Issue.1 , pp. 111-122
    • Delamarre, L.1    Holcombe, H.2    Mellman, I.3
  • 7
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • DOI 10.1038/32588
    • Banchereau, J., and Steinman, R. M. (1998) Dendritic cells and the control of immunity. Nature 392, 245-252 (Pubitemid 28155090)
    • (1998) Nature , vol.392 , Issue.6673 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 8
    • 0036715411 scopus 로고    scopus 로고
    • Immature, semi-mature and fully mature dendritic cells: Which signals induce tolerance or immunity?
    • DOI 10.1016/S1471-4906(02)02281-0, PII S1471490602022810
    • Lutz, M. B., and Schuler, G. (2002) Immature, semi-mature and fully mature dendritic cells: which signals induce tolerance or immunity? Trends Immunol. 23, 445-449 (Pubitemid 35015188)
    • (2002) Trends in Immunology , vol.23 , Issue.9 , pp. 445-449
    • Lutz, M.B.1    Schuler, G.2
  • 9
    • 84878089880 scopus 로고    scopus 로고
    • SWAP-70 restricts spontaneous maturation of dendritic cells
    • Ocaña-Morgner, C., Götz, A., Wahren, C., and Jessberger, R. (2013) SWAP-70 restricts spontaneous maturation of dendritic cells. J. Immunol. 190, 5545-5558
    • (2013) J. Immunol. , vol.190 , pp. 5545-5558
    • Ocaña-Morgner, C.1    Götz, A.2    Wahren, C.3    Jessberger, R.4
  • 11
    • 79956327230 scopus 로고    scopus 로고
    • TGF-β suppresses β-catenin-dependent tolerogenic activation program in dendritic cells
    • Vander Lugt, B., Beck, Z. T., Fuhlbrigge, R. C., Hacohen, N., Campbell, J. J., and Boes, M. (2011) TGF-β suppresses β-catenin-dependent tolerogenic activation program in dendritic cells. PLoS One 6, e20099
    • (2011) PLoS One , vol.6
    • Vander Lugt, B.1    Beck, Z.T.2    Fuhlbrigge, R.C.3    Hacohen, N.4    Campbell, J.J.5    Boes, M.6
  • 13
    • 0034672339 scopus 로고    scopus 로고
    • Ligation of E-cadherin on in vitro-generated immature Langerhans-type dendritic cells inhibits their maturation
    • Riedl, E., Stöckl, J., Majdic, O., Scheinecker, C., Knapp, W., and Strobl, H. (2000) Ligation of E-cadherin on in vitro-generated immature Langerhans-type dendritic cells inhibits their maturation. Blood 96, 4276-4284
    • (2000) Blood , vol.96 , pp. 4276-4284
    • Riedl, E.1    Stöckl, J.2    Majdic, O.3    Scheinecker, C.4    Knapp, W.5    Strobl, H.6
  • 14
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • DOI 10.1126/science.1080106
    • Trombetta, E. S., Ebersold, M., Garrett, W., Pypaert, M., and Mellman, I. (2003) Activation of lysosomal function during dendritic cell maturation. Science 299, 1400-1403 (Pubitemid 36254654)
    • (2003) Science , vol.299 , Issue.5611 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 15
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • DOI 10.1038/nrm2272, PII NRM2272
    • Forgac, M. (2007) Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929 (Pubitemid 47622561)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.11 , pp. 917-929
    • Forgac, M.1
  • 16
    • 62949218373 scopus 로고    scopus 로고
    • The yeast lysosome-like vacuole: Endpoint and crossroads
    • Li, S. C., and Kane, P. M. (2009) The yeast lysosome-like vacuole: endpoint and crossroads. Biochim. Biophys. Acta 1793, 650-663
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 650-663
    • Li, S.C.1    Kane, P.M.2
  • 17
    • 66449088593 scopus 로고    scopus 로고
    • Regulation of the V-ATPase in kidney epithelial cells: Dual role in acid-base homeostasis and vesicle trafficking
    • Brown, D., Paunescu, T. G., Breton, S., and Marshansky, V. (2009) Regulation of the V-ATPase in kidney epithelial cells: dual role in acid-base homeostasis and vesicle trafficking. J. Exp. Biol. 212, 1762-1772
    • (2009) J. Exp. Biol. , vol.212 , pp. 1762-1772
    • Brown, D.1    Paunescu, T.G.2    Breton, S.3    Marshansky, V.4
  • 19
    • 0038606551 scopus 로고    scopus 로고
    • Subunit rotation of vacuolar-type proton pumping ATPase. Relative rotation of the G and c subunits
    • DOI 10.1074/jbc.M302756200
    • Hirata, T., Iwamoto-Kihara, A., Sun-Wada, G. H., Okajima, T., Wada, Y., and Futai, M. (2003) Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and C subunits. J. Biol. Chem. 278, 23714-23719 (Pubitemid 36830195)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23714-23719
    • Hirata, T.1    Iwamoto-Kihara, A.2    Sun-Wada, G.-H.3    Okajima, T.4    Wada, Y.5    Futai, M.6
  • 21
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • Toei, M., Saum, R., and Forgac, M. (2010) Regulation and isoform function of the V-ATPases. Biochemistry 49, 4715-4723
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 22
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H+- ATPase in vivo
    • Kane, P. M. (1995) Disassembly and reassembly of the yeast vacuolar H+- ATPase in vivo. J. Biol. Chem. 270, 17025-17032
    • (1995) J. Biol. Chem. , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 23
    • 0031597366 scopus 로고    scopus 로고
    • +-ATPase is an unconventional glucose-induced effect
    • Parra, K. J., and Kane, P. M. (1998) Reversible association between the V1 and V0 domains of yeast vacuolar H+-ATPase is an unconventional glucose-induced effect. Mol. Cell Biol. 18, 7064-7074 (Pubitemid 28533026)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.12 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 24
    • 33644935227 scopus 로고    scopus 로고
    • The V-type H+ ATPase: Molecular structure and function, physiological roles and regulation
    • Beyenbach, K. W., and Wieczorek, H. (2006) The V-type H+ ATPase: molecular structure and function, physiological roles and regulation. J. Exp. Biol. 209, 577-589
    • (2006) J. Exp. Biol. , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 25
    • 11844260070 scopus 로고    scopus 로고
    • +-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells
    • DOI 10.1128/MCB.25.2.575-589.2005
    • Sautin, Y. Y., Lu, M., Gaugler, A., Zhang, L., and Gluck, S. L. (2005) Phosphatidylinositol 3-kinase-mediated effects of glucose on vacuolar H+-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells. Mol. Cell Biol. 25, 575-589 (Pubitemid 40096580)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.2 , pp. 575-589
    • Sautin, Y.Y.1    Lu, M.2    Gaugler, A.3    Zhang, L.4    Gluck, S.L.5
  • 26
    • 84864388778 scopus 로고    scopus 로고
    • Epidermal growth factor-induced vacuolar (H+)-ATPase assembly: A role in signaling via mTORC1 activation
    • Xu, Y., Parmar, A., Roux, E., Balbis, A., Dumas, V., Chevalier, S., and Posner, B. I. (2012) Epidermal growth factor-induced vacuolar (H+)-ATPase assembly: a role in signaling via mTORC1 activation. J. Biol. Chem. 287, 26409-26422
    • (2012) J. Biol. Chem. , vol.287 , pp. 26409-26422
    • Xu, Y.1    Parmar, A.2    Roux, E.3    Balbis, A.4    Dumas, V.5    Chevalier, S.6    Posner, B.I.7
  • 27
    • 0027322674 scopus 로고
    • Inhibitory effect of modified bafilomycins and concanamycins on P- and V- type adenosinetriphosphatases
    • Dröse, S., Bindseil, K. U., Bowman, E. J., Siebers, A., Zeeck, A., and Altendorf, K. (1993) Inhibitory effect of modified bafilomycins and concanamycins on P- and V-type adenosinetriphosphatases. Biochemistry 32, 3902-3906 (Pubitemid 23126977)
    • (1993) Biochemistry , vol.32 , Issue.15 , pp. 3902-3906
    • Drose, S.1    Bindseil, K.U.2    Bowman, E.J.3    Siebers, A.4    Zeeck, A.5    Altendorf, K.6
  • 30
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K., and Osborn, M. (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 32
    • 0034662239 scopus 로고    scopus 로고
    • Cutting edge: Repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2
    • Hirschfeld, M., Ma, Y., Weis, J. H., Vogel, S. N., and Weis, J. J. (2000) Cutting edge: repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2. J. Immunol. 165, 618-622 (Pubitemid 30484724)
    • (2000) Journal of Immunology , vol.165 , Issue.2 , pp. 618-622
    • Hirschfeld, M.1    Ma, Y.2    Weis, J.H.3    Vogel, S.N.4    Weis, J.J.5
  • 33
    • 41649115159 scopus 로고    scopus 로고
    • TLR2 promiscuous or specific? a critical re-evaluation of a receptor expressing apparent broad specificity
    • Zähringer, U., Lindner, B., Inamura, S., Heine, H., and Alexander, C. (2008) TLR2 promiscuous or specific? A critical re-evaluation of a receptor expressing apparent broad specificity. Immunobiology. 213, 205-224
    • (2008) Immunobiology. , vol.213 , pp. 205-224
    • Zähringer, U.1    Lindner, B.2    Inamura, S.3    Heine, H.4    Alexander, C.5
  • 34
    • 35348968837 scopus 로고    scopus 로고
    • Disruption of E-Cadherin-Mediated Adhesion Induces a Functionally Distinct Pathway of Dendritic Cell Maturation
    • DOI 10.1016/j.immuni.2007.08.015, PII S1074761307004463
    • Jiang, A., Bloom, O., Ono, S., Cui, W., Unternaehrer, J., Jiang, S., Whitney, J. A., Connolly, J., Banchereau, J., and Mellman, I. (2007) Disruption of E-cadherin-mediated adhesion induces a functionally distinct pathway of dendritic cell maturation. Immunity 27, 610-624 (Pubitemid 47615505)
    • (2007) Immunity , vol.27 , Issue.4 , pp. 610-624
    • Jiang, A.1    Bloom, O.2    Ono, S.3    Cui, W.4    Unternaehrer, J.5    Jiang, S.6    Whitney, J.A.7    Connolly, J.8    Banchereau, J.9    Mellman, I.10
  • 35
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • Legate, K. R., Wickström, S. A., and Fässler, R. (2009) Genetic and cell biological analysis of integrin outside-in signaling. Genes Dev. 23, 397-418
    • (2009) Genes Dev. , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickström, S.A.2    Fässler, R.3
  • 36
    • 63849141545 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase: A key regulator in adherens junction formation and function
    • (Landmark Ed.)
    • Rivard, N. (2009) Phosphatidylinositol 3-kinase: a key regulator in adherens junction formation and function. Front. Biosci. (Landmark Ed.) 14, 510-522
    • (2009) Front. Biosci. , vol.14 , pp. 510-522
    • Rivard, N.1
  • 38
    • 2642714927 scopus 로고    scopus 로고
    • Heterogeneity of mouse spleen dendritic cells: In vivo phagocytic activity, expression of macrophage markers, and subpopulation turnover
    • Leenen, P. J., Radosević, K., Voerman, J. S., Salomon, B., van Rooijen, N., Klatzmann, D., and van Ewijk, W. (1998) Heterogeneity of mouse spleen dendritic cells: in vivo phagocytic activity, expression of macrophage markers, and subpopulation turnover. J. Immunol. 160, 2166-2173 (Pubitemid 28119895)
    • (1998) Journal of Immunology , vol.160 , Issue.5 , pp. 2166-2173
    • Leenen, P.J.M.1    Radosevic, K.2    Voerman, J.S.A.3    Salomon, B.4    Van Rooijen, N.5    Klatzmann, D.6    Van Ewijk, W.7
  • 39
    • 0016240723 scopus 로고
    • Identification of a novel cell type in peripheral lymphoid organs of mice: III. Functional properties in vivo
    • Steinman, R. M., Lustig, D. S., and Cohn, Z. A. (1974) Identification of a novel cell type in peripheral lymphoid organs of mice: III. Functional properties in vivo. J. Exp. Med. 139, 1431-1445
    • (1974) J. Exp. Med. , vol.139 , pp. 1431-1445
    • Steinman, R.M.1    Lustig, D.S.2    Cohn, Z.A.3
  • 43
    • 0035839499 scopus 로고    scopus 로고
    • Interaction between aldolase and vacuolar H+-ATPase: Evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump
    • Lu, M., Holliday, L. S., Zhang, L., Dunn, W. A., Jr, and Gluck, S. L. (2001) Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J. Biol. Chem. 276, 30407-30413
    • (2001) J. Biol. Chem. , vol.276 , pp. 30407-30413
    • Lu, M.1    Holliday, L.S.2    Zhang, L.3    Dunn Jr., W.A.4    Gluck, S.L.5
  • 44
    • 1542365368 scopus 로고    scopus 로고
    • +-ATPase
    • DOI 10.1074/jbc.M303871200
    • Lu, M., Sautin, Y. Y., Holliday, L. S., and Gluck, S. L. (2004) The glycolytic enzyme aldolase mediates assembly, expression, and activity of vacuolar H+-ATPase. J. Biol. Chem. 279, 8732-8739 (Pubitemid 38295929)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8732-8739
    • Lu, M.1    Sautin, Y.Y.2    Holliday, L.S.3    Gluck, S.L.4
  • 45
    • 0038165450 scopus 로고    scopus 로고
    • +-ATPase interacts with phosphofructokinase-1 in humans
    • DOI 10.1074/jbc.M210077200
    • Su, Y., Zhou, A., Al-Lamki, R. S., and Karet, F. E. (2003) The a-subunit of the V-type H+-ATPase interacts with phosphofructokinase-1 in humans. J. Biol. Chem. 278, 20013-20018 (Pubitemid 36799194)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20013-20018
    • Su, Y.1    Zhou, A.2    Al-Lamki, R.S.3    Karet, F.E.4
  • 46
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an insideout mechanism that requires the vacuolar H+-ATPase
    • Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., and Sabatini, D. M. (2011) mTORC1 senses lysosomal amino acids through an insideout mechanism that requires the vacuolar H+-ATPase. Science 334, 678-683
    • (2011) Science , vol.334 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6
  • 47
    • 0035955425 scopus 로고    scopus 로고
    • The plasticity of dendritic cell responses to pathogens and their components
    • DOI 10.1126/science.294.5543.870
    • Huang, Q., Liu, D., Majewski, P., Schulte, L. C., Korn, J. M., Young, R. A., Lander, E. S., and Hacohen, N. (2001) The plasticity of dendritic cell responses to pathogens and their components. Science 294, 870-875 (Pubitemid 33032108)
    • (2001) Science , vol.294 , Issue.5543 , pp. 870-875
    • Huang, Q.1    Liu, D.2    Majewski, P.3    Schulte, L.C.4    Korn, J.M.5    Young, R.A.6    Lander, E.S.7    Hacohen, N.8
  • 48
    • 71849100670 scopus 로고    scopus 로고
    • Uncoupling of induced protein processing from maturation in dendritic cells exposed to a highly antigenic preparation from a helminth parasite
    • Marshall, F. A., and Pearce, E. J. (2008) Uncoupling of induced protein processing from maturation in dendritic cells exposed to a highly antigenic preparation from a helminth parasite. J. Immunol. 181, 7562-7570
    • (2008) J. Immunol. , vol.181 , pp. 7562-7570
    • Marshall, F.A.1    Pearce, E.J.2


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