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Volumn 290, Issue 45, 2015, Pages 27360-27369

Amino acid availability modulates vacuolar H+-ATPase assembly

Author keywords

[No Author keywords available]

Indexed keywords

PHYSIOLOGY;

EID: 84946569689     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.659128     Document Type: Article
Times cited : (113)

References (24)
  • 1
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007) Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 2
    • 84883442790 scopus 로고    scopus 로고
    • Regulation of luminal acidification by the V-ATPase
    • Bethesda
    • Breton, S., and Brown, D. (2013) Regulation of luminal acidification by the V-ATPase. Physiology (Bethesda) 28, 318-329.
    • (2013) Physiology , vol.28 , pp. 318-329
    • Breton, S.1    Brown, D.2
  • 3
    • 84860815342 scopus 로고    scopus 로고
    • Targeting reversible disassembly as a mechanism of controlling V-ATPase activity
    • Kane, P. M. (2012) Targeting reversible disassembly as a mechanism of controlling V-ATPase activity. Curr. Protein Pept. Sci. 13, 117-123.
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 117-123
    • Kane, P.M.1
  • 4
    • 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
  • 5
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner, J. P., Dow, J. A., Earley, F. G., Klein, U., Jäger, D., and Wieczorek, H. (1995) Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem. 270, 5649-5653.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5649-5653
    • Sumner, J.P.1    Dow, J.A.2    Earley, F.G.3    Klein, U.4    Jäger, D.5    Wieczorek, H.6
  • 6
    • 0026612693 scopus 로고
    • Characterization of the V0 domain of the coated vesicle (H+)-ATPase
    • Zhang, J., Myers, M., and Forgac, M. (1992) Characterization of the V0 domain of the coated vesicle (H+)-ATPase. J. Biol. Chem. 267, 9773-9778.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9773-9778
    • Zhang, J.1    Myers, M.2    Forgac, M.3
  • 7
    • 0025071147 scopus 로고
    • Functional reassembly of the coated vesicle proton pump
    • Puopolo, K., and Forgac, M. (1990) Functional reassembly of the coated vesicle proton pump. J. Biol. Chem. 265, 14836-14841.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14836-14841
    • Puopolo, K.1    Forgac, M.2
  • 8
    • 11844260070 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-mediated effects of glucose on vacuolar H+- ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells
    • 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.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 575-589
    • Sautin, Y.Y.1    Lu, M.2    Gaugler, A.3    Zhang, L.4    Gluck, S.L.5
  • 9
    • 79952664121 scopus 로고    scopus 로고
    • Influenza A virusinduced early activation of ERK and PI3K mediates V-ATPase-dependent intracellular pH change required for fusion
    • Marjuki, H., Gornitzky, A., Marathe, B. M., Ilyushina, N. A., Aldridge, J. R., Desai, G., Webby, R. J., and Webster, R. G. (2011) Influenza A virusinduced early activation of ERK and PI3K mediates V-ATPase-dependent intracellular pH change required for fusion. Cell Microbiol. 13, 587-601.
    • (2011) Cell Microbiol , vol.13 , pp. 587-601
    • Marjuki, H.1    Gornitzky, A.2    Marathe, B.M.3    Ilyushina, N.A.4    Aldridge, J.R.5    Desai, G.6    Webby, R.J.7    Webster, R.G.8
  • 10
    • 84882878219 scopus 로고    scopus 로고
    • Glycolytic control of vacuolartype ATPase activity: A mechanism to regulate influenza viral infection
    • Kohio, H. P., and Adamson, A. L. (2013) Glycolytic control of vacuolartype ATPase activity: A mechanism to regulate influenza viral infection. Virology 444, 301-309.
    • (2013) Virology , vol.444 , pp. 301-309
    • Kohio, H.P.1    Adamson, A.L.2
  • 11
    • 84892639521 scopus 로고    scopus 로고
    • Regulated assembly of the V-ATPase is increased during cluster disruption-induced maturation of dendritic cells through a PI-3 kinase/mTOR-dependent pathway
    • Liberman, R., Bond, S., Shainheit, M. G., Stadecker, M. J., and Forgac, M. (2014) Regulated assembly of the V-ATPase is increased during cluster disruption-induced maturation of dendritic cells through a PI-3 kinase/mTOR-dependent pathway. J. Biol. Chem. 289, 1355-1363.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1355-1363
    • Liberman, R.1    Bond, S.2    Shainheit, M.G.3    Stadecker, M.J.4    Forgac, M.5
  • 12
    • 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
  • 13
    • 84866431363 scopus 로고    scopus 로고
    • Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1
    • Bar-Peled, L., Schweitzer, L. D., Zoncu, R., and Sabatini, D. M. (2012) Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell 150, 1196-1208.
    • (2012) Cell , vol.150 , pp. 1196-1208
    • Bar-Peled, L.1    Schweitzer, L.D.2    Zoncu, R.3    Sabatini, D.M.4
  • 14
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., and Sabatini, D. M. (2010) Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141, 290-303.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 18
    • 0031597366 scopus 로고    scopus 로고
    • Reversible association between the V1 and V0 domains of yeast vacuolar H+-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.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 19
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol- 3, 4-bisphosphate
    • Franke, T. F., Kaplan, D. R., Cantley, L. C., and Toker, A. (1997) Direct regulation of the Akt proto-oncogene product by phosphatidylinositol- 3, 4-bisphosphate. Science 275, 665-668.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 20
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation
    • Shao, E., and Forgac, M. (2004) Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation. J. Biol. Chem. 279, 48663-48670.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 22
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases
    • Chung, J., Kuo, C. J., Crabtree, G. R., and Blenis, J. (1992) Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases. Cell 69, 1227-1236.
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3    Blenis, J.4
  • 23
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • Hara, K., Yonezawa, K., Weng, Q.-P., Kozlowski, M. T., Belham, C., and Avruch, J. (1998) Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J. Biol. Chem. 273, 14484-14494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.-P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 24
    • 0027470686 scopus 로고
    • Effects of intracellular amino acid concentrations, cyclic AMP, and dexamethasone on lysosomal proteolysis in primary cultures of perinatal rat hepatocytes
    • Blommaart, P. J., Zonneveld, D., Meijer, A. J., and Lamers, W. H. (1993) Effects of intracellular amino acid concentrations, cyclic AMP, and dexamethasone on lysosomal proteolysis in primary cultures of perinatal rat hepatocytes. J. Biol. Chem. 268, 1610-1617.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1610-1617
    • Blommaart, P.J.1    Zonneveld, D.2    Meijer, A.J.3    Lamers, W.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.