메뉴 건너뛰기




Volumn 13, Issue 2, 2012, Pages 124-133

Novel insights into V-ATPase functioning: Distinct roles for its accessory subunits ATP6AP1/AC45 and ATP6AP2/(pro) renin receptor

Author keywords

Acidification; Membrane fusion; Neurodevelopment; Osteoporosis; Renin angiotensin system; Secretory pathway

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ATP6AP1 PROTEIN; ATP6AP2 PROTEIN; PROTEIN; SNARE PROTEIN; UNCLASSIFIED DRUG; VACUOLAR ADENOSINE TRIPHOSPHATASE;

EID: 84860820531     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312800493160     Document Type: Article
Times cited : (36)

References (103)
  • 1
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases-nature's most versatile proton pumps
    • T. Nishi; M. Forgac. The vacuolar (H+)-ATPases-nature's most versatile proton pumps, Nat. Rev. Mol. Cell Biol., 2002, 3, 94-103.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 2
    • 0035024033 scopus 로고    scopus 로고
    • Regulation of organelle acidity
    • M. Grabe; G. Oster. Regulation of organelle acidity. J. Gen. Physiol., 2001, 117, 329-344.
    • (2001) J. Gen. Physiol , vol.117 , pp. 329-344
    • Grabe, M.1    Oster, G.2
  • 3
    • 0028008329 scopus 로고
    • Acidification of three types of liver endocytic vesicles: Similarities and differences
    • R.W. Van Dyke; J.D. Belcher. Acidification of three types of liver endocytic vesicles: similarities and differences. Am. J. Physiol., 1994, 266, C81-C94.
    • (1994) Am. J. Physiol , vol.266
    • van Dyke, R.W.1    Belcher, J.D.2
  • 4
    • 0032946360 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton- adenosinetriphosphatases
    • N. Nelson; W.R. Harvey. Vacuolar and plasma membrane proton- adenosinetriphosphatases. Physiol. Rev., 1999, 79, 361-385.
    • (1999) Physiol. Rev , vol.79 , pp. 361-385
    • Nelson, N.1    Harvey, W.R.2
  • 5
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • T.J. Jentsch; V. Stein, F. Weinreich, AA. Zdebik. Molecular structure and physiological function of chloride channels. Physiol. Rev., 2002, 82, 503-568.
    • (2002) Physiol. Rev , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.A.4
  • 6
    • 62149142874 scopus 로고    scopus 로고
    • V-ATPase functions in normal and disease processes
    • A. Hinton; S. Bond; M. Forgac. V-ATPase functions in normal and disease processes, Pflugers Arch., 2009, 457, 589-598.
    • (2009) Pflugers Arch , vol.457 , pp. 589-598
    • Hinton, A.1    Bond, S.2    Forgac, M.3
  • 7
    • 39649119621 scopus 로고    scopus 로고
    • The pH of the secretory pathway: Measurement, determinants, and regulation
    • P. Paroutis; N. Touret; S. Grinstein. The pH of the secretory pathway: measurement, determinants, and regulation. Physiology (Bethesda), 2004, 19, 207-215.
    • (2004) Physiology (Bethesda) , vol.19 , pp. 207-215
    • Paroutis, P.1    Touret, N.2    Grinstein, S.3
  • 8
    • 33947513226 scopus 로고    scopus 로고
    • Structure and function of V-ATPases in osteoclasts: Potential therapeutic targets for the treatment of osteolysis
    • J. Xu; T. Cheng; H.T. Feng; N.J. Pavlos; M.H. Zheng. Structure and function of V-ATPases in osteoclasts: potential therapeutic targets for the treatment of osteolysis. Histol. Histopathol., 2007, 22, 443-454.
    • (2007) Histol. Histopathol , vol.22 , pp. 443-454
    • Xu, J.1    Cheng, T.2    Feng, H.T.3    Pavlos, N.J.4    Zheng, M.H.5
  • 9
    • 33744506178 scopus 로고    scopus 로고
    • Early, H+-V-ATPase-dependent proton flux is necessary for consistent left-right patterning of non-mammalian vertebrates
    • D.S. Adams; K.R. Robinson; T. Fukumoto; S. Yuan; R.C. Albertson; P. Yelick; L. Kuo; M. McSweeney; M. Levin. Early, H+-V-ATPase-dependent proton flux is necessary for consistent left-right patterning of non-mammalian vertebrates. Development, 2006, 133, 1657-1671.
    • (2006) Development , vol.133 , pp. 1657-1671
    • Adams, D.S.1    Robinson, K.R.2    Fukumoto, T.3    Yuan, S.4    Albertson, R.C.5    Yelick, P.6    Kuo, L.7    McSweeney, M.8    Levin, M.9
  • 10
    • 0035425020 scopus 로고    scopus 로고
    • Proton pumping in the secretory pathway
    • V.T. Schoonderwoert; G.J. Martens. Proton pumping in the secretory pathway. J. Membr. Biol., 2001, 182, 159-169.
    • (2001) J. Membr. Biol , vol.182 , pp. 159-169
    • Schoonderwoert, V.T.1    Martens, G.J.2
  • 11
    • 0026950284 scopus 로고
    • The role of V-ATPase in neuronal and endocrine systems
    • Y. Moriyama; M. Maeda; M. Futai. The role of V-ATPase in neuronal and endocrine systems. J. Exp. Biol., 1992, 172, 171-178.
    • (1992) J. Exp. Biol , vol.172 , pp. 171-178
    • Moriyama, Y.1    Maeda, M.2    Futai, M.3
  • 12
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • M. Forgac. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology, Nat. Rev. Mol. Cell Biol., 2007, 8, 917-929.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 917-929
    • Forgac, M.1
  • 13
    • 0037056038 scopus 로고    scopus 로고
    • Structure, subunit function and regulation of the coated vesicle and yeast vacuolar (H(+))-ATPases
    • Y. Arata; T. Nishi; S. Kawasaki-Nishi; E. Shao; S. Wilkens; M. Forgac. Structure, subunit function and regulation of the coated vesicle and yeast vacuolar (H(+))-ATPases, Biochim. Biophys. Acta., 2002, 1555, 71-74.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 71-74
    • Arata, Y.1    Nishi, T.2    Kawasaki-Nishi, S.3    Shao, E.4    Wilkens, S.5    Forgac, M.6
  • 15
    • 4544289322 scopus 로고    scopus 로고
    • Topological characterization of the c, c', and c subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae
    • A.R. Flannery; L.A. Graham; T.H. Stevens. Topological characterization of the c, c', and c subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae. J. Biol. Chem., 2004, 279, 39856-39862.
    • (2004) J. Biol. Chem , vol.279 , pp. 39856-39862
    • Flannery, A.R.1    Graham, L.A.2    Stevens, T.H.3
  • 16
    • 41249097135 scopus 로고    scopus 로고
    • Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry
    • N. Kitagawa; H. Mazon; A.J. Heck; S. Wilkens. Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry. J. Biol. Chem., 2008, 283, 3329-3337.
    • (2008) J. Biol. Chem , vol.283 , pp. 3329-3337
    • Kitagawa, N.1    Mazon, H.2    Heck, A.J.3    Wilkens, S.4
  • 17
    • 60149087436 scopus 로고    scopus 로고
    • Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity
    • S.P. Muench; M. Huss; C.F. Song; C. Phillips; H. Wieczorek; J. Trinick; M.A. Harrison. Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity. J. Mol. Biol., 2009, 386, 989-999.
    • (2009) J. Mol. Biol , vol.386 , pp. 989-999
    • Muench, S.P.1    Huss, M.2    Song, C.F.3    Phillips, C.4    Wieczorek, H.5    Trinick, J.6    Harrison, M.A.7
  • 18
    • 0030589058 scopus 로고    scopus 로고
    • Chromaffin granule membrane glycoprotein IV is identical with Ac45, a membrane-integral subunit of the granule's H(+)-ATPase
    • F. Getlawi; A. Laslop; H. Schagger; J. Ludwig; J. Haywood; D. Apps. Chromaffin granule membrane glycoprotein IV is identical with Ac45, a membrane-integral subunit of the granule's H(+)-ATPase. Neurosci. Lett., 1996, 219, 13-16.
    • (1996) Neurosci. Lett , vol.219 , pp. 13-16
    • Getlawi, F.1    Laslop, A.2    Schagger, H.3    Ludwig, J.4    Haywood, J.5    Apps, D.6
  • 19
    • 0028067756 scopus 로고
    • A novel accessory subunit for vacuolar H(+)-ATPase from chromaffin granules
    • F. Supek; L. Supekova; S. Mandiyan; Y.C. Pan; H. Nelson; N. Nelson. A novel accessory subunit for vacuolar H(+)-ATPase from chromaffin granules. J. Biol. Chem., 1994, 269, 24102-24106.
    • (1994) J. Biol. Chem , vol.269 , pp. 24102-24106
    • Supek, F.1    Supekova, L.2    Mandiyan, S.3    Pan, Y.C.4    Nelson, H.5    Nelson, N.6
  • 20
    • 0032079560 scopus 로고    scopus 로고
    • Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules
    • J. Ludwig; S. Kerscher; U. Brandt; K. Pfeiffer; F. Getlawi; D.K. Apps; H. Schagger. Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules. J. Biol. Chem., 1998, 273, 10939-10947.
    • (1998) J. Biol. Chem , vol.273 , pp. 10939-10947
    • Ludwig, J.1    Kerscher, S.2    Brandt, U.3    Pfeiffer, K.4    Getlawi, F.5    Apps, D.K.6    Schagger, H.7
  • 22
    • 0032514213 scopus 로고    scopus 로고
    • Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex
    • L.A. Graham; K.J. Hill; T.H. Stevens. Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex. J. Cell Biol., 1998, 142, 39-49.
    • (1998) J. Cell Biol , vol.142 , pp. 39-49
    • Graham, L.A.1    Hill, K.J.2    Stevens, T.H.3
  • 23
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • J.P. Sumner; J.A. Dow; F.G. Earley; U. Klein; D. Jager; H. Wieczorek. Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem., 1995, 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    Jager, D.5    Wieczorek, H.6
  • 24
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo
    • P.M. Kane. Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo. J. Biol. Chem., 1995, 270, 17025-17032.
    • (1995) J. Biol. Chem , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 25
    • 50549104079 scopus 로고    scopus 로고
    • Regulation of the V-ATPase along the endocytic pathway occurs through reversible subunit association and membrane localization
    • C. Lafourcade; K. Sobo; S. Kieffer-Jaquinod; J. Garin; F.G. van der Goot. Regulation of the V-ATPase along the endocytic pathway occurs through reversible subunit association and membrane localization. PLoS ONE, 2008, 3, e2758.
    • (2008) PLoS ONE , vol.3
    • Lafourcade, C.1    Sobo, K.2    Kieffer-Jaquinod, S.3    Garin, J.4    van der Goot, F.G.5
  • 26
    • 0035067367 scopus 로고    scopus 로고
    • Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly
    • J.H. Seol; A. Shevchenko; R.J. Deshaies. Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly. Nat. Cell Biol., 2001, 3, 384-391.
    • (2001) Nat. Cell Biol , vol.3 , pp. 384-391
    • Seol, J.H.1    Shevchenko, A.2    Deshaies, R.J.3
  • 27
    • 0037134525 scopus 로고    scopus 로고
    • The RAVE complex is essential for stable assembly of the yeast V-ATPase
    • A.M. Smardon; M. Tarsio; P.M. Kane. The RAVE complex is essential for stable assembly of the yeast V-ATPase. J. Biol. Chem., 2002, 277, 13831-13839.
    • (2002) J. Biol. Chem , vol.277 , pp. 13831-13839
    • Smardon, A.M.1    Tarsio, M.2    Kane, P.M.3
  • 28
    • 33644935227 scopus 로고    scopus 로고
    • The V-type H+ ATPase: Molecular structure and function, physiological roles and regulation
    • K.W. Beyenbach; H. Wieczorek. The V-type H+ ATPase: molecular structure and function, physiological roles and regulation. J. Exp. Biol., 2006, 209, 577-589.
    • (2006) J. Exp. Biol , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 29
    • 34548300007 scopus 로고    scopus 로고
    • Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump
    • M. Lu; D. Ammar; H. Ives; F. Albrecht; S.L. Gluck. Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump. J. Biol. Chem., 2007.
    • (2007) J. Biol. Chem
    • Lu, M.1    Ammar, D.2    Ives, H.3    Albrecht, F.4    Gluck, S.L.5
  • 30
    • 0035839499 scopus 로고    scopus 로고
    • Interaction between aldolase and vacuolar H+-ATPase: Evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump
    • M. Lu; L.S. Holliday; L. Zhang; W.A. Dunn; Jr. S.L. Gluck. Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J. Biol. Chem., 276, 2001, 30407-30413.
    • (2001) J. Biol. Chem , vol.276 , pp. 30407-30413
    • Lu, M.1    Holliday, L.S.2    Zhang, L.3    Dunn, W.A.4    Gluck, S.L.5
  • 31
    • 1542365368 scopus 로고    scopus 로고
    • The glycolytic enzyme aldolase mediates assembly, expression, and activity of vacuolar H+-ATPase
    • M. Lu; Y.Y. Sautin; L.S. Holliday; S.L. Gluck. The glycolytic enzyme aldolase mediates assembly, expression, and activity of vacuolar H+-ATPase. J. Biol. Chem., 2004, 279, 8732-8739.
    • (2004) J. Biol. Chem , vol.279 , pp. 8732-8739
    • Lu, M.1    Sautin, Y.Y.2    Holliday, L.S.3    Gluck, S.L.4
  • 32
    • 15544385722 scopus 로고    scopus 로고
    • Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding
    • A. Armbruster; C. Hohn; A. Hermesdorf; K. Schumacher; M. Borsch; G. Gruber. Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding. FEBS Lett., 2005, 579, 1961-1967.
    • (2005) FEBS Lett , vol.579 , pp. 1961-1967
    • Armbruster, A.1    Hohn, C.2    Hermesdorf, A.3    Schumacher, K.4    Borsch, M.5    Gruber, G.6
  • 33
    • 0033974290 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H(+)-ATPase
    • P.M. Kane; K.J. Parra. Assembly and regulation of the yeast vacuolar H(+)-ATPase. J. Exp. Biol., 2000, 203, 81-87.
    • (2000) J. Exp. Biol , vol.203 , pp. 81-87
    • Kane, P.M.1    Parra, K.J.2
  • 34
    • 0033981348 scopus 로고    scopus 로고
    • H(+)V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: Vesicle recycling and transcytotic pathways
    • D. Brown; S. Breton. H(+)V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: vesicle recycling and transcytotic pathways. J. Exp. Biol., 2000, 203, 137-145.
    • (2000) J. Exp. Biol , vol.203 , pp. 137-145
    • Brown, D.1    Breton, S.2
  • 35
    • 0023571839 scopus 로고
    • Structure of the novel membrane-coating material in proton-secreting epithelial cells and identification as an H+ATPase
    • D. Brown; S. Gluck; J. Hartwig. Structure of the novel membrane-coating material in proton-secreting epithelial cells and identification as an H+ATPase. J. Cell Biol., 1987, 1637-1648.
    • (1987) J. Cell Biol , pp. 1637-1648
    • Brown, D.1    Gluck, S.2    Hartwig, J.3
  • 36
    • 59849095753 scopus 로고    scopus 로고
    • Sensing, signaling and sorting events in kidney epithelial cell physiology
    • D. Brown; S. Breton; D.A. Ausiello; V. Marshansky. Sensing, signaling and sorting events in kidney epithelial cell physiology. Traffic, 2009, 275-284.
    • (2009) Traffic , pp. 275-284
    • Brown, D.1    Breton, S.2    Ausiello, D.A.3    Marshansky, V.4
  • 37
    • 12544249243 scopus 로고    scopus 로고
    • The V-ATPase subunit C binds to polymeric F-actin as well as to monomeric G-actin and induces cross-linking of actin filaments
    • O. Vitavska; H. Merzendorfer; H. Wieczorek. The V-ATPase subunit C binds to polymeric F-actin as well as to monomeric G-actin and induces cross-linking of actin filaments. J. Biol. Chem., 2005, 280, 1070-1076.
    • (2005) J. Biol. Chem , vol.280 , pp. 1070-1076
    • Vitavska, O.1    Merzendorfer, H.2    Wieczorek, H.3
  • 38
    • 0038043266 scopus 로고    scopus 로고
    • A novel role for subunit C in mediating binding of the H+-V-ATPase to the actin cytoskeleton
    • O. Vitavska; H. Wieczorek; H. Merzendorfer. A novel role for subunit C in mediating binding of the H+-V-ATPase to the actin cytoskeleton. J. Biol. Chem., 2003, 278, 18499-18505.
    • (2003) J. Biol. Chem , vol.278 , pp. 18499-18505
    • Vitavska, O.1    Wieczorek, H.2    Merzendorfer, H.3
  • 39
    • 0034644703 scopus 로고    scopus 로고
    • The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site
    • L.S. Holliday; M. Lu; B.S. Lee; R.D. Nelson; S. Solivan; L. Zhang; S.L. Gluck. The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site. J. Biol. Chem., 2000, 275, 32331-32337.
    • (2000) J. Biol. Chem , vol.275 , pp. 32331-32337
    • Holliday, L.S.1    Lu, M.2    Lee, B.S.3    Nelson, R.D.4    Solivan, S.5    Zhang, L.6    Gluck, S.L.7
  • 41
    • 77649102858 scopus 로고    scopus 로고
    • Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging
    • M. Clarke; L. Maddera; U. Engel; G. Gerisch. Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging. PLoS One, 2010, 5, e8585.
    • (2010) PLoS One , vol.5
    • Clarke, M.1    Maddera, L.2    Engel, U.3    Gerisch, G.4
  • 42
    • 0022872029 scopus 로고
    • Purification of a presynaptic membrane protein that mediates a calcium-dependent translocation of acetylcholine
    • M. Israel; N. Morel; B. Lesbats; S. Birman; R. Manaranche. Purification of a presynaptic membrane protein that mediates a calcium-dependent translocation of acetylcholine. Proc. Natl. Acad. Sci. USA, 83 (1986) 9226-9230.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9226-9230
    • Israel, M.1    Morel, N.2    Lesbats, B.3    Birman, S.4    Manaranche, R.5
  • 43
    • 0025057463 scopus 로고
    • A 15 kDa proteolipid found in mediatophore preparations from Torpedo electric organ presents high sequence homology with the bovine chromaffin granule protonophore
    • S. Birman; F.M. Meunier; B. Lesbats; J.P. Le Caer; J. Rossier; M. Israel. A 15 kDa proteolipid found in mediatophore preparations from Torpedo electric organ presents high sequence homology with the bovine chromaffin granule protonophore. FEBS Lett., 1990, 261, 303-306.
    • (1990) FEBS Lett , vol.261 , pp. 303-306
    • Birman, S.1    Meunier, F.M.2    Lesbats, B.3    Le Caer, J.P.4    Rossier, J.5    Israel, M.6
  • 44
    • 0043174011 scopus 로고    scopus 로고
    • Vacuole membrane fusion: V0 functions after trans-SNARE pairing and is coupled to the Ca2+-releasing channel
    • M.J. Bayer; C. Reese; S. Buhler; C. Peters; A. Mayer. Vacuole membrane fusion: V0 functions after trans-SNARE pairing and is coupled to the Ca2+-releasing channel. J. Cell Biol., 2003, 162, 211-222.
    • (2003) J. Cell Biol , vol.162 , pp. 211-222
    • Bayer, M.J.1    Reese, C.2    Buhler, S.3    Peters, C.4    Mayer, A.5
  • 45
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • C. Peters; M.J. Bayer; S. Buhler; J.S. Andersen; M. Mann; A. Mayer. Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature, 2001, 409, 581-588.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Buhler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 47
    • 33751511196 scopus 로고    scopus 로고
    • The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta-cells
    • G.H. Sun-Wada; T. Toyomura; Y. Murata; A. Yamamoto; M. Futai; Y. Wada. The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta-cells. J. Cell Sci., 2006, 119, 4531-4540.
    • (2006) J. Cell Sci , vol.119 , pp. 4531-4540
    • Sun-Wada, G.H.1    Toyomura, T.2    Murata, Y.3    Yamamoto, A.4    Futai, M.5    Wada, Y.6
  • 48
    • 43949088191 scopus 로고    scopus 로고
    • Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo
    • F. Peri; C. Nusslein-Volhard. Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo. Cell, 2008, 133, 916-927.
    • (2008) Cell , vol.133 , pp. 916-927
    • Peri, F.1    Nusslein-Volhard, C.2
  • 50
    • 0029664522 scopus 로고    scopus 로고
    • The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex
    • T. Galli; P.S. McPherson; P. De Camilli. The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex. J. Biol. Chem., 1996, 271, 2193-2198.
    • (1996) J. Biol. Chem , vol.271 , pp. 2193-2198
    • Galli, T.1    McPherson, P.S.2    de Camilli, P.3
  • 52
    • 0347382415 scopus 로고    scopus 로고
    • Specific sorting of the a1 isoform of the V-H+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane
    • N. Morel; J.C. Dedieu; J.M. Philippe. Specific sorting of the a1 isoform of the V-H+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane. J. Cell Sci., 2003, 116, 4751-4762.
    • (2003) J. Cell Sci , vol.116 , pp. 4751-4762
    • Morel, N.1    Dedieu, J.C.2    Philippe, J.M.3
  • 54
    • 0033578614 scopus 로고    scopus 로고
    • A novel family of yeast chaperons involved in the distribution of V-ATPase and other membrane proteins
    • A. Cohen; N. Perzov; H. Nelson; N. Nelson. A novel family of yeast chaperons involved in the distribution of V-ATPase and other membrane proteins. J. Biol. Chem., 1999, 274, 26885-26893.
    • (1999) J. Biol. Chem , vol.274 , pp. 26885-26893
    • Cohen, A.1    Perzov, N.2    Nelson, H.3    Nelson, N.4
  • 55
  • 56
    • 0036470112 scopus 로고    scopus 로고
    • The Vtc proteins in vacuole fusion: Coupling NSF activity to V(0) trans-complex formation
    • O. Muller; M.J. Bayer; C. Peters; J.S. Andersen; M. Mann; A. Mayer. The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation. Embo. J., 2002, 21, 259-269.
    • (2002) Embo. J , vol.21 , pp. 259-269
    • Muller, O.1    Bayer, M.J.2    Peters, C.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 57
    • 0037444478 scopus 로고    scopus 로고
    • Role of the Vtc proteins in V-ATPase stability and membrane trafficking
    • O. Muller; H. Neumann; M.J. Bayer; A. Mayer. Role of the Vtc proteins in V-ATPase stability and membrane trafficking. J. Cell Sci., 2003, 116, 1107-1115.
    • (2003) J. Cell Sci , vol.116 , pp. 1107-1115
    • Muller, O.1    Neumann, H.2    Bayer, M.J.3    Mayer, A.4
  • 59
    • 0033637520 scopus 로고    scopus 로고
    • New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis
    • N. Ogawa; J. DeRisi; P.O. Brown. New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis. Mol. Biol. Cell, 2000, 11, 4309-4321.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4309-4321
    • Ogawa, N.1    Derisi, J.2    Brown, P.O.3
  • 60
    • 33846116102 scopus 로고    scopus 로고
    • The vacuolar transporter chaperone (VTC) complex is required for microautophagy
    • A. Uttenweiler; H. Schwarz; H. Neumann; A. Mayer. The vacuolar transporter chaperone (VTC) complex is required for microautophagy. Mol. Biol. Cell, 2007, 18, 166-175.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 166-175
    • Uttenweiler, A.1    Schwarz, H.2    Neumann, H.3    Mayer, A.4
  • 61
    • 0035793636 scopus 로고    scopus 로고
    • The Cdc42p GTPase and its regulators Nrf1p and Scd1p are involved in endocytic trafficking in the fission yeast Schizosaccharomyces pombe
    • J.M. Murray; D.I. Johnson. The Cdc42p GTPase and its regulators Nrf1p and Scd1p are involved in endocytic trafficking in the fission yeast Schizosaccharomyces pombe. J. Biol. Chem., 2001, 276, 3004-3009.
    • (2001) J. Biol. Chem , vol.276 , pp. 3004-3009
    • Murray, J.M.1    Johnson, D.I.2
  • 63
    • 0036266596 scopus 로고    scopus 로고
    • Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin
    • G. Nguyen; F. Delarue; C. Burckle; L. Bouzhir; T. Giller; J.D. Sraer. Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin. J. Clin. Invest., 2002, 109, 1417-1427.
    • (2002) J. Clin. Invest , vol.109 , pp. 1417-1427
    • Nguyen, G.1    Delarue, F.2    Burckle, C.3    Bouzhir, L.4    Giller, T.5    Sraer, J.D.6
  • 64
    • 38649119156 scopus 로고    scopus 로고
    • The second life of the (pro)renin receptor
    • M. Bader. The second life of the (pro)renin receptor. J. Renin. Angiotensin Aldosterone Syst., 2007, 8, 205-208.
    • (2007) J. Renin. Angiotensin Aldosterone Syst , vol.8 , pp. 205-208
    • Bader, M.1
  • 66
    • 67049144916 scopus 로고    scopus 로고
    • Soluble form of the (pro)renin receptor generated by intracellular cleavage by furin is secreted in plasma
    • C. Cousin; D. Bracquart; A. Contrepas; P. Corvol; L. Muller; G. Nguyen. Soluble form of the (pro)renin receptor generated by intracellular cleavage by furin is secreted in plasma, Hypertension, 2009, 53, 1077-1082.
    • (2009) Hypertension , vol.53 , pp. 1077-1082
    • Cousin, C.1    Bracquart, D.2    Contrepas, A.3    Corvol, P.4    Muller, L.5    Nguyen, G.6
  • 69
    • 34447262612 scopus 로고    scopus 로고
    • Angiotensin II stimulates vacuolar H+ -ATPase activity in renal acid-secretory intercalated cells from the outer medullary collecting duct
    • F. Rothenberger; A. Velic; P.A. Stehberger; J. Kovacikova; C.A. Wagner. Angiotensin II stimulates vacuolar H+ -ATPase activity in renal acid-secretory intercalated cells from the outer medullary collecting duct. J. Am. Soc. Nephrol., 2007, 18, 2085-2093.
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 2085-2093
    • Rothenberger, F.1    Velic, A.2    Stehberger, P.A.3    Kovacikova, J.4    Wagner, C.A.5
  • 70
    • 33845608395 scopus 로고    scopus 로고
    • A novel signal transduction cascade involving direct physical interaction of the renin/prorenin receptor with the transcription factor promyelocytic zinc finger protein
    • J.H. Schefe; M. Menk; J. Reinemund; K. Effertz; R.M. Hobbs; P.P. Pandolfi; P. Ruiz; T. Unger; H. Funke-Kaiser. A novel signal transduction cascade involving direct physical interaction of the renin/prorenin receptor with the transcription factor promyelocytic zinc finger protein. Circ. Res., 2006, 99, 1355-1366.
    • (2006) Circ. Res , vol.99 , pp. 1355-1366
    • Schefe, J.H.1    Menk, M.2    Reinemund, J.3    Effertz, K.4    Hobbs, R.M.5    Pandolfi, P.P.6    Ruiz, P.7    Unger, T.8    Funke-Kaiser, H.9
  • 72
    • 0036122004 scopus 로고    scopus 로고
    • Targeted disruption of the mouse gene encoding the V-ATPase accessory subunit Ac45
    • V.T. Schoonderwoert; G.J. Martens. Targeted disruption of the mouse gene encoding the V-ATPase accessory subunit Ac45. Mol. Membr. Biol., 2002, 19, 67-71.
    • (2002) Mol. Membr. Biol , vol.19 , pp. 67-71
    • Schoonderwoert, V.T.1    Martens, G.J.2
  • 73
    • 0347157164 scopus 로고    scopus 로고
    • Identification, genomic structure, and screening of the vacuolar proton-ATPase membrane sector-associated protein M8-9 gene within the COD1 critical region (Xp11.4)
    • F.Y. Demirci; N.J. White; B.W. Rigatti; K.F. Lewis; M.B. Gorin. Identification, genomic structure, and screening of the vacuolar proton-ATPase membrane sector-associated protein M8-9 gene within the COD1 critical region (Xp11.4). Mol. Vis., 2001, 7, 234-239.
    • (2001) Mol. Vis , vol.7 , pp. 234-239
    • Demirci, F.Y.1    White, N.J.2    Rigatti, B.W.3    Lewis, K.F.4    Gorin, M.B.5
  • 75
    • 45149125392 scopus 로고    scopus 로고
    • Cytoplasmic terminus of vacuolar type proton pump accessory subunit Ac45 is required for proper interaction with V(0) domain subunits and efficient osteoclastic bone resorption
    • H. Feng; T. Cheng; N.J. Pavlos; K.H. Yip; A. Carrello; R. Seeber; K. Eidne; M.H. Zheng; J. Xu. Cytoplasmic terminus of vacuolar type proton pump accessory subunit Ac45 is required for proper interaction with V(0) domain subunits and efficient osteoclastic bone resorption. J. Biol. Chem., 2008, 283, 13194-13204.
    • (2008) J. Biol. Chem , vol.283 , pp. 13194-13204
    • Feng, H.1    Cheng, T.2    Pavlos, N.J.3    Yip, K.H.4    Carrello, A.5    Seeber, R.6    Eidne, K.7    Zheng, M.H.8    Xu, J.9
  • 76
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • M. Toei; R. Saum; M. Forgac. Regulation and isoform function of the V-ATPases. Biochemistry, 2010, 49, 4715-4723.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 78
    • 0029157139 scopus 로고
    • Molecular probing of the secretory pathway in peptide hormone-producing cells
    • J.C. Holthuis; E.J. Jansen; M.C. van Riel; G.J. Martens. Molecular probing of the secretory pathway in peptide hormone-producing cells. J. Cell Sci., 1995, 108(10) 3295-3305.
    • (1995) J. Cell Sci , vol.108 , Issue.10 , pp. 3295-3305
    • Holthuis, J.C.1    Jansen, E.J.2    van Riel, M.C.3    Martens, G.J.4
  • 80
    • 85047696284 scopus 로고    scopus 로고
    • The fate of newly synthesized V-ATPase accessory subunit Ac45 in the secretory pathway
    • V.T. Schoonderwoert; E.J. Jansen; G.J. Martens. The fate of newly synthesized V-ATPase accessory subunit Ac45 in the secretory pathway. Eur. J. Biochem., 2002, 269, 1844-1853.
    • (2002) Eur. J. Biochem , vol.269 , pp. 1844-1853
    • Schoonderwoert, V.T.1    Jansen, E.J.2    Martens, G.J.3
  • 81
    • 0034710889 scopus 로고    scopus 로고
    • Furin-mediated processing in the early secretory pathway: Sequential cleavage and degradation of misfolded insulin receptors
    • J. Bass; C. Turck; M. Rouard; D.F. Steiner. Furin-mediated processing in the early secretory pathway: sequential cleavage and degradation of misfolded insulin receptors. Proc. Natl. Acad. Sci. USA, 2000, 97, 11905-11909.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11905-11909
    • Bass, J.1    Turck, C.2    Rouard, M.3    Steiner, D.F.4
  • 82
    • 55249083292 scopus 로고    scopus 로고
    • Accessory subunit Ac45 controls the V-ATPase in the regulated secretory pathway
    • E.J. Jansen; W.J. Scheenen; T.G. Hafmans; G.J. Martens. Accessory subunit Ac45 controls the V-ATPase in the regulated secretory pathway. Biochim. Biophys. Acta., 2008, 1783, 2301-2310.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2301-2310
    • Jansen, E.J.1    Scheenen, W.J.2    Hafmans, T.G.3    Martens, G.J.4
  • 83
    • 77958070738 scopus 로고    scopus 로고
    • V-ATPase-mediated granular acidification is regulated by the V-ATPase accessory subunit Ac45 in POMC-producing cells
    • E.J. Jansen; T.G. Hafmans; G.J. Martens. V-ATPase-mediated granular acidification is regulated by the V-ATPase accessory subunit Ac45 in POMC-producing cells. Mol. Biol. Cell, 2010.
    • (2010) Mol. Biol. Cell
    • Jansen, E.J.1    Hafmans, T.G.2    Martens, G.J.3
  • 85
    • 0031771006 scopus 로고    scopus 로고
    • Intracellular trafficking of the vacuolar H+-ATPase accessory subunit Ac45
    • E.J. Jansen; J.C. Holthuis; C. McGrouther; J.P. Burbach; G.J. Martens. Intracellular trafficking of the vacuolar H+-ATPase accessory subunit Ac45. J. Cell Sci., 1998, 111 (20), 2999-3006.
    • (1998) J. Cell Sci , vol.111 , Issue.20 , pp. 2999-3006
    • Jansen, E.J.1    Holthuis, J.C.2    McGrouther, C.3    Burbach, J.P.4    Martens, G.J.5
  • 86
    • 78549293945 scopus 로고    scopus 로고
    • Inhibition of osteoclast bone resorption by disrupting vacuolar H+-ATPase a3-B2 subunit interaction
    • N. Kartner; Y. Yao; K. Li; G.J. Crasto; A. Datti; M.F. Manolson. Inhibition of osteoclast bone resorption by disrupting vacuolar H+-ATPase a3-B2 subunit interaction. J. Biol. Chem., 2010, 285, 37476-37490.
    • (2010) J. Biol. Chem , vol.285 , pp. 37476-37490
    • Kartner, N.1    Yao, Y.2    Li, K.3    Crasto, G.J.4    Datti, A.5    Manolson, M.F.6
  • 87
    • 0032726897 scopus 로고    scopus 로고
    • Targeted disruption of the gene encoding the proteolipid subunit of mouse vacuolar H(+)-ATPase leads to early embryonic lethality
    • H. Inoue; T. Noumi; M. Nagata; H. Murakami; H. Kanazawa. Targeted disruption of the gene encoding the proteolipid subunit of mouse vacuolar H(+)-ATPase leads to early embryonic lethality. Biochim. Biophys. Acta., 1999, 1413, 130-138.
    • (1999) Biochim. Biophys. Acta , vol.1413 , pp. 130-138
    • Inoue, H.1    Noumi, T.2    Nagata, M.3    Murakami, H.4    Kanazawa, H.5
  • 88
    • 0034671585 scopus 로고    scopus 로고
    • Acidic endomembrane organelles are required for mouse postimplantation development
    • G. Sun-Wada; Y. Murata; A. Yamamoto; H. Kanazawa; Y. Wada; M. Futai. Acidic endomembrane organelles are required for mouse postimplantation development. Dev. Biol., 2000, 228, 315-325.
    • (2000) Dev. Biol , vol.228 , pp. 315-325
    • Sun-Wada, G.1    Murata, Y.2    Yamamoto, A.3    Kanazawa, H.4    Wada, Y.5    Futai, M.6
  • 89
    • 25144514858 scopus 로고    scopus 로고
    • Genome-wide survey of V-ATPase genes in Drosophila reveals a conserved renal phenotype for lethal alleles
    • A.K. Allan; J. Du; S.A. Davies; J.A. Dow. Genome-wide survey of V-ATPase genes in Drosophila reveals a conserved renal phenotype for lethal alleles. Physiol. Genomics, 2005, 22, 128-138.
    • (2005) Physiol. Genomics , vol.22 , pp. 128-138
    • Allan, A.K.1    Du, J.2    Davies, S.A.3    Dow, J.A.4
  • 90
    • 0035980087 scopus 로고    scopus 로고
    • Four subunit a isoforms of Caenorhabditis elegans vacuolar H+-ATPase. Cell-specific expression during development
    • T. Oka; T. Toyomura; K. Honjo; Y. Wada; M. Futai. Four subunit a isoforms of Caenorhabditis elegans vacuolar H+-ATPase. Cell-specific expression during development. J. Biol. Chem., 2001, 276, 33079-33085.
    • (2001) J. Biol. Chem , vol.276 , pp. 33079-33085
    • Oka, T.1    Toyomura, T.2    Honjo, K.3    Wada, Y.4    Futai, M.5
  • 91
    • 0034703050 scopus 로고    scopus 로고
    • Requirement of V-ATPase for ovulation and embryogenesis in Caenorhabditis elegans
    • T. Oka; M. Futai. Requirement of V-ATPase for ovulation and embryogenesis in Caenorhabditis elegans. J Biol Chem, 2000, 275, 29556-29561.
    • (2000) J Biol Chem , vol.275 , pp. 29556-29561
    • Oka, T.1    Futai, M.2
  • 92
    • 59449087945 scopus 로고    scopus 로고
    • The vacuolar-ATPase complex regulates retinoblast proliferation and survival, photoreceptor morphogenesis, and pigmentation in the zebrafish eye
    • R.J. Nuckels; A. Ng; T. Darland; J.M. Gross. The vacuolar-ATPase complex regulates retinoblast proliferation and survival, photoreceptor morphogenesis, and pigmentation in the zebrafish eye. Invest. Ophthalmol. Vis. Sci., 2009, 50, 893-905.
    • (2009) Invest. Ophthalmol. Vis. Sci , vol.50 , pp. 893-905
    • Nuckels, R.J.1    Ng, A.2    Darland, T.3    Gross, J.M.4
  • 98
    • 0032748995 scopus 로고    scopus 로고
    • Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification
    • Y.P. Li; W. Chen; Y. Liang; E. Li; P. Stashenko. Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification. Nat. Genet., 1999, 23, 447-451.
    • (1999) Nat. Genet , vol.23 , pp. 447-451
    • Li, Y.P.1    Chen, W.2    Liang, Y.3    Li, E.4    Stashenko, P.5
  • 100
    • 0028288256 scopus 로고
    • Isolation of expressed sequences encoded by the human Xq terminal portion using microclone probes generated by laser microdissection
    • H. Yokoi; S. Hadano; M. Kogi; X. Kang; K. Wakasa; J.E. Ikeda. Isolation of expressed sequences encoded by the human Xq terminal portion using microclone probes generated by laser microdissection. Genomics, 1994, 20, 404-411.
    • (1994) Genomics , vol.20 , pp. 404-411
    • Yokoi, H.1    Hadano, S.2    Kogi, M.3    Kang, X.4    Wakasa, K.5    Ikeda, J.E.6
  • 102
    • 0034177681 scopus 로고    scopus 로고
    • Determination of X-chromosome inactivation status using X-linked expressed polymorphisms identified by database searching
    • R. Kutsche; C.J. Brown. Determination of X-chromosome inactivation status using X-linked expressed polymorphisms identified by database searching. Genomics, 2000, 65, 9-15.
    • (2000) Genomics , vol.65 , pp. 9-15
    • Kutsche, R.1    Brown, C.J.2
  • 103
    • 0033961647 scopus 로고    scopus 로고
    • Age-dependent increase in C7-1 gene expression in rat frontal cortex
    • H. Hung; M.J. Tsai; H.C. Wu; E.H. Lee. Age-dependent increase in C7-1 gene expression in rat frontal cortex. Brain Res. Mol. Brain Res., 2000, 75, 330-336.
    • (2000) Brain Res. Mol. Brain Res , vol.75 , pp. 330-336
    • Hung, H.1    Tsai, M.J.2    Wu, H.C.3    Lee, E.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.