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Volumn 8, Issue 11, 2007, Pages 917-929

Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTON PUMP;

EID: 35448946098     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2272     Document Type: Review
Times cited : (1239)

References (105)
  • 1
    • 0036481562 scopus 로고    scopus 로고
    • +)-ATPases: Nature's most versatile proton pumps
    • +)-ATPases: Nature's most versatile proton pumps. Nature Rev. Mol. Cell Biol. 3, 94-103 (2002).
    • (2002) Nature Rev. Mol. Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 7
    • 17844369968 scopus 로고    scopus 로고
    • Murata, T., Yamamoto, I., Kakinuma, Y., Leslie, A. G. & Walker, J. E. Structure of the rotor of the V-type Na-ATPase from Enterococcus hirae. Science 308, 654-659 (2005). The first high-resolution structure of an A-ATPase subcomplex (namely the proteolipid ring from E. hirae).
    • Murata, T., Yamamoto, I., Kakinuma, Y., Leslie, A. G. & Walker, J. E. Structure of the rotor of the V-type Na-ATPase from Enterococcus hirae. Science 308, 654-659 (2005). The first high-resolution structure of an A-ATPase subcomplex (namely the proteolipid ring from E. hirae).
  • 8
    • 0037418211 scopus 로고    scopus 로고
    • 1-ATPase. Proc. Natl Acad. Sci. USA 100, 2312-2315 (2003). The first evidence that an A-ATPase (closely related to the V-ATPases) is operated by a rotary mechanism.
    • 1-ATPase. Proc. Natl Acad. Sci. USA 100, 2312-2315 (2003). The first evidence that an A-ATPase (closely related to the V-ATPases) is operated by a rotary mechanism.
  • 9
    • 33747371955 scopus 로고    scopus 로고
    • 1 complex
    • 1 complex. J. Biol. Chem. 281, 22752-22760 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 22752-22760
    • Ohira, M.1
  • 10
    • 2342435823 scopus 로고    scopus 로고
    • The yeast vacuolar proton-translocating ATPase contains a subunit homologous to the Manduca sexta and bovine e subunits that is essential for function
    • Sambade, M. & Kane, P. M. The yeast vacuolar proton-translocating ATPase contains a subunit homologous to the Manduca sexta and bovine e subunits that is essential for function. J. Biol. Chem. 279, 17361-17365 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 17361-17365
    • Sambade, M.1    Kane, P.M.2
  • 11
    • 0028067756 scopus 로고
    • +-ATPase from chromaffin granules
    • +-ATPase from chromaffin granules. J. Biol. Chem. 269, 24102-24106 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 24102-24106
    • Supek, F.1
  • 13
    • 0035941232 scopus 로고    scopus 로고
    • Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy
    • Wilkens, S. & Forgac, M. Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy. J. Biol. Chem. 276, 44064-44068 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 44064-44068
    • Wilkens, S.1    Forgac, M.2
  • 15
    • 0035940474 scopus 로고    scopus 로고
    • Arg735 of the 100 kDa a subunit of the yeast V-ATPase is essential for proton translocation
    • Kawasaki-Nishi, S., Nishi, T. & Forgac, M. Arg735 of the 100 kDa a subunit of the yeast V-ATPase is essential for proton translocation. Proc. Natl Acad. Sci. USA. 98, 12397-12402 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12397-12402
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 16
    • 9144222170 scopus 로고    scopus 로고
    • Crystal structure of a central stalk subunit C and reversible dissociation of V-ATPase
    • Iwata, M. et al. Crystal structure of a central stalk subunit C and reversible dissociation of V-ATPase. Proc. Natl Acad. Sci. USA 101, 59-64 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 59-64
    • Iwata, M.1
  • 17
    • 4544289322 scopus 로고    scopus 로고
    • Topological characterization of the c, c′ and c″ subunits of the V-ATPase from the yeast S. cerevisae
    • Flannery, A. R., Graham, L. A. & Stevens, T. H. Topological characterization of the c, c′ and c″ subunits of the V-ATPase from the yeast S. cerevisae. J. Biol. Chem. 279, 39856-39862 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 39856-39862
    • Flannery, A.R.1    Graham, L.A.2    Stevens, T.H.3
  • 18
    • 34248585138 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of bovine brain V-ATPase by cryo-electron microscopy and single particle analysis
    • Gregorini, M., Wang, J., Xie, X. S., Milligan, R. A. & Engel, A. Three-dimensional reconstruction of bovine brain V-ATPase by cryo-electron microscopy and single particle analysis. J. Struct. Biol. 158, 445-454 (2007).
    • (2007) J. Struct. Biol , vol.158 , pp. 445-454
    • Gregorini, M.1    Wang, J.2    Xie, X.S.3    Milligan, R.A.4    Engel, A.5
  • 19
    • 33745867962 scopus 로고    scopus 로고
    • An expanded and flexible form of the vacuolar ATPase membrane sector
    • Clare, D. K. et al. An expanded and flexible form of the vacuolar ATPase membrane sector. Structure 14, 1149-1156 (2006).
    • (2006) Structure , vol.14 , pp. 1149-1156
    • Clare, D.K.1
  • 20
    • 0142149158 scopus 로고    scopus 로고
    • Interacting helical surfaces of the transmembrane segments of subunits a and c′ of the yeast V-ATPase defined by disilfide-mediated cross-linking
    • Kawasaki-Nishi, S., Nishi, T. & Forgac, M. Interacting helical surfaces of the transmembrane segments of subunits a and c′ of the yeast V-ATPase defined by disilfide-mediated cross-linking. J. Biol. Chem. 278, 41908-41913 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 41908-41913
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 21
    • 7244248726 scopus 로고    scopus 로고
    • Wang, Y., Inoue, T. & Forgac, M. TM2 but not TM4 of subunit c″ interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking. J. Biol. Chem. 279, 44628-44638 (2004).
    • Wang, Y., Inoue, T. & Forgac, M. TM2 but not TM4 of subunit c″ interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking. J. Biol. Chem. 279, 44628-44638 (2004).
  • 22
    • 0037125922 scopus 로고    scopus 로고
    • Localization of subunits D, E and G in the yeast V-ATPase complex using cysteine-mediated crosslinking to subunit B
    • Arata, Y., Baleja, J. D. & Forgac, M. Localization of subunits D, E and G in the yeast V-ATPase complex using cysteine-mediated crosslinking to subunit B. Biochemistry 41, 11301-11307 (2002).
    • (2002) Biochemistry , vol.41 , pp. 11301-11307
    • Arata, Y.1    Baleja, J.D.2    Forgac, M.3
  • 23
    • 4744375526 scopus 로고    scopus 로고
    • Wilkens, S., Inoue, T. & Forgac, M. Three-dimensional structure of the vacuolar ATPase - localization of subunit H by difference imaging and chemical cross-linking. J. Biol. Chem. 279, 41942-41949 (2004). Describes the first use of a combination of EM image analysis and photoactivated cross-linking to localize a subunit in the V-ATPase.
    • Wilkens, S., Inoue, T. & Forgac, M. Three-dimensional structure of the vacuolar ATPase - localization of subunit H by difference imaging and chemical cross-linking. J. Biol. Chem. 279, 41942-41949 (2004). Describes the first use of a combination of EM image analysis and photoactivated cross-linking to localize a subunit in the V-ATPase.
  • 25
    • 27844508579 scopus 로고    scopus 로고
    • Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus
    • Makyio, H. et al. Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus. EMBO J. 24, 3974-3983 (2005).
    • (2005) EMBO J , vol.24 , pp. 3974-3983
    • Makyio, H.1
  • 26
    • 0344875467 scopus 로고    scopus 로고
    • Yeast V1-ATPase: Affinity purification and structural features by electron microscopy
    • Zhang, Z., Charsky, C., Kane, P. M. & Wilkens, S. Yeast V1-ATPase: affinity purification and structural features by electron microscopy. J. Biol. Chem. 278, 47299-47306 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 47299-47306
    • Zhang, Z.1    Charsky, C.2    Kane, P.M.3    Wilkens, S.4
  • 27
    • 33645241290 scopus 로고    scopus 로고
    • Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immunoelectron microscopy
    • Zhang, Z., Inoue, T., Forgac, M. & Wilkens, S. Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immunoelectron microscopy. FEBS Lett. 580, 2006-2010 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 2006-2010
    • Zhang, Z.1    Inoue, T.2    Forgac, M.3    Wilkens, S.4
  • 28
    • 19444381126 scopus 로고    scopus 로고
    • Elucidation of the stator organization in the V-ATPase of Neurospora crassa
    • Venzke, D. et al. Elucidation of the stator organization in the V-ATPase of Neurospora crassa. J. Mol. Biol. 349, 659-669 (2005).
    • (2005) J. Mol. Biol , vol.349 , pp. 659-669
    • Venzke, D.1
  • 29
    • 0142120592 scopus 로고    scopus 로고
    • Subunit composition, structure, and distribution of bacterial V-type ATPases
    • Lolkema, J. S., Chaban, Y. & Boekema, E. J. Subunit composition, structure, and distribution of bacterial V-type ATPases. J. Bioenerg. Biomembr. 35, 323-335 (2003).
    • (2003) J. Bioenerg. Biomembr , vol.35 , pp. 323-335
    • Lolkema, J.S.1    Chaban, Y.2    Boekema, E.J.3
  • 31
    • 12144279605 scopus 로고    scopus 로고
    • Crystal structure of yeast V-ATPase C subunit reveals its stator function
    • 1148-1152
    • Drory, O., Frolow, F. & Nelson, N. Crystal structure of yeast V-ATPase C subunit reveals its stator function. EMBO Rep. 5, 1148-1152 (2004).
    • (2004) EMBO Rep , vol.5
    • Drory, O.1    Frolow, F.2    Nelson, N.3
  • 32
    • 0037169510 scopus 로고    scopus 로고
    • Novel V-ATPase complexes resulting from overproduction of Vma5p and Vma13p
    • This study provided important insight into the function of two regulatory subunits
    • Curtis, K. K. & Kane, P. M. Novel V-ATPase complexes resulting from overproduction of Vma5p and Vma13p. J. Biol. Chem. 277, 2716-2724 (2002). This study provided important insight into the function of two regulatory subunits.
    • (2002) J. Biol. Chem , vol.277 , pp. 2716-2724
    • Curtis, K.K.1    Kane, P.M.2
  • 33
    • 27744447197 scopus 로고    scopus 로고
    • Structural and functional separation of the N- and C-terminal domains of the yeast V-ATPase subunit H
    • Liu, M., Tarsio, M., Charsky, C. M. & Kane, P. M. Structural and functional separation of the N- and C-terminal domains of the yeast V-ATPase subunit H. J. Biol. Chem. 280, 36978-36985 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 36978-36985
    • Liu, M.1    Tarsio, M.2    Charsky, C.M.3    Kane, P.M.4
  • 34
    • 28544445574 scopus 로고    scopus 로고
    • Peripheral stator of the yeast V-ATPase: Stoichiometry and specificity of interaction between the EG complex and subunits C and H
    • Fethiere, J., Venzke, D., Madden, D. R. & Bottcher, B. Peripheral stator of the yeast V-ATPase: stoichiometry and specificity of interaction between the EG complex and subunits C and H. Biochemistry 44, 15906-15914 (2005).
    • (2005) Biochemistry , vol.44 , pp. 15906-15914
    • Fethiere, J.1    Venzke, D.2    Madden, D.R.3    Bottcher, B.4
  • 35
    • 0037064113 scopus 로고    scopus 로고
    • +-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function
    • +-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function. J. Biol. Chem. 277, 38409-38415 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 38409-38415
    • Lu, M.1
  • 37
    • 0038606551 scopus 로고    scopus 로고
    • Subunit rotation of vacuolar-type proton pumping ATPase: Relative rotation of the G as to c subunit
    • Hirata, T. et al. Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G as to c subunit. J. Biol. Chem. 278, 23714-23719 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 23714-23719
    • Hirata, T.1
  • 38
    • 0034737966 scopus 로고    scopus 로고
    • A model for the structure of subunit a of the E. coli ATP synthase and its role in proton translocation
    • Vik, S. B., Long, J. C., Wada, T. & Zhang, D. A model for the structure of subunit a of the E. coli ATP synthase and its role in proton translocation. Biochim. Biophys. Acta 1458, 457-466 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 457-466
    • Vik, S.B.1    Long, J.C.2    Wada, T.3    Zhang, D.4
  • 40
    • 0035979760 scopus 로고    scopus 로고
    • 1-ATPase
    • 1-ATPase. FEBS Lett. 504, 152-160 (2001).
    • (2001) FEBS Lett , vol.504 , pp. 152-160
    • Junge, W.1
  • 41
    • 0344982110 scopus 로고    scopus 로고
    • Electrophysiological analysis of the yeast V-type proton pump: Variable coupling ratio and proton shunt
    • Kettner, C., Bertl, A., Obermeyer, G., Slayman, C. & Bihler, H. Electrophysiological analysis of the yeast V-type proton pump: variable coupling ratio and proton shunt. Biophys. J. 85, 3730-3738 (2003).
    • (2003) Biophys. J , vol.85 , pp. 3730-3738
    • Kettner, C.1    Bertl, A.2    Obermeyer, G.3    Slayman, C.4    Bihler, H.5
  • 43
    • 6344272891 scopus 로고    scopus 로고
    • Role of Vma21p in assembly and transport of the yeast vacuolar ATPase
    • Malkus, P., Graham, L. A., Stevens, T. H. & Schekman, R. Role of Vma21p in assembly and transport of the yeast vacuolar ATPase. Mol. Biol. Cell 15, 5075-5091 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5075-5091
    • Malkus, P.1    Graham, L.A.2    Stevens, T.H.3    Schekman, R.4
  • 44
    • 33846002764 scopus 로고    scopus 로고
    • PKR1 encodes an assembly factor for the yeast V-type ATPase
    • Davis-Kaplan, S. R. et al. PKR1 encodes an assembly factor for the yeast V-type ATPase. J. Biol. Chem. 281, 32025-32035 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 32025-32035
    • Davis-Kaplan, S.R.1
  • 45
    • 0035861664 scopus 로고    scopus 로고
    • The amino-terminal domain of the V-ATPase a subunit controls targeting and in vivo dissociation and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis
    • Kawasaki-Nishi, S., Bowers, K., Nishi, T., Forgac, M. & Stevens, T. H The amino-terminal domain of the V-ATPase a subunit controls targeting and in vivo dissociation and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J. Biol. Chem. 276, 47411-47420 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 47411-47420
    • Kawasaki-Nishi, S.1    Bowers, K.2    Nishi, T.3    Forgac, M.4    Stevens, T.H.5
  • 46
    • 0035947711 scopus 로고    scopus 로고
    • Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation
    • This study provided an important insight into the functional differences between isoforms of subunit a
    • Kawasaki-Nishi, S., Nishi, T. & Forgac, M. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J. Biol. Chem. 276, 17941-17948 (2001). This study provided an important insight into the functional differences between isoforms of subunit a.
    • (2001) J. Biol. Chem , vol.276 , pp. 17941-17948
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 47
    • 0028224791 scopus 로고
    • +-ATPase subunit Vph1p
    • +-ATPase subunit Vph1p. J. Biol. Chem. 269, 14064-14074 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 14064-14074
    • Manolson, M.F.1
  • 48
    • 0037936890 scopus 로고    scopus 로고
    • +-ATPase with the a3 isoform during osteoclast differentiation. J. Biol. Chem. 278, 22023-22030 (2003). This study indicated that V-ATPase localization that is directed by isoforms of subunit a is not necessarily static.
    • +-ATPase with the a3 isoform during osteoclast differentiation. J. Biol. Chem. 278, 22023-22030 (2003). This study indicated that V-ATPase localization that is directed by isoforms of subunit a is not necessarily static.
  • 49
    • 30344445397 scopus 로고    scopus 로고
    • Distinct expression patterns of different subunit isoforms of the V-ATPase in the rat epididymis
    • Pietrement, C. et al. Distinct expression patterns of different subunit isoforms of the V-ATPase in the rat epididymis. Biol. Reprod. 74, 185-194 (2006).
    • (2006) Biol. Reprod , vol.74 , pp. 185-194
    • Pietrement, C.1
  • 50
    • 0347382415 scopus 로고    scopus 로고
    • +ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane
    • +ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane. J. Cell Sci. 116, 4751-4762 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 4751-4762
    • Morel, N.1    Dedieu, J.C.2    Philippe, J.M.3
  • 51
    • 33645152194 scopus 로고    scopus 로고
    • Hurtado-Lorenzo, A. et al. V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway. Nature Cell Biol. 8, 124-136 (2006). This finding suggests that V-ATPase subunits interact with other parts of the trafficking machinery in a pH-dependent manner.
    • Hurtado-Lorenzo, A. et al. V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway. Nature Cell Biol. 8, 124-136 (2006). This finding suggests that V-ATPase subunits interact with other parts of the trafficking machinery in a pH-dependent manner.
  • 52
    • 0344443771 scopus 로고    scopus 로고
    • Expression and function of the mouse V-ATPase d subunit isoforms
    • Nishi, T., Kawasaki-Nishi, S. & Forgac, M. Expression and function of the mouse V-ATPase d subunit isoforms. J. Biol. Chem. 278, 46396-46402 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 46396-46402
    • Nishi, T.1    Kawasaki-Nishi, S.2    Forgac, M.3
  • 53
    • 0037019817 scopus 로고    scopus 로고
    • +-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis
    • +-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis. Gene 297, 169-177 (2002).
    • (2002) Gene , vol.297 , pp. 169-177
    • Smith, A.N.1    Borthwick, K.J.2    Karet, F.E.3
  • 54
    • 0037124047 scopus 로고    scopus 로고
    • A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification
    • Sun-Wada, G. H. et al. A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification. J. Biol. Chem. 277, 18098-18105 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 18098-18105
    • Sun-Wada, G.H.1
  • 55
    • 0037413670 scopus 로고    scopus 로고
    • Diversity of mouse proton-translocating ATPase: Presence of multiple isoforms of the C, d and G subunits
    • Sun-Wada, G. H., Yoshimizu, T., Imai-Senga, Y., Wada, Y. & Futai, M. Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits. Gene 302, 147-153 (2003).
    • (2003) Gene , vol.302 , pp. 147-153
    • Sun-Wada, G.H.1    Yoshimizu, T.2    Imai-Senga, Y.3    Wada, Y.4    Futai, M.5
  • 56
    • 2942638407 scopus 로고    scopus 로고
    • +-ATPase in proton-secreting cells of the kidney and epididymis
    • +-ATPase in proton-secreting cells of the kidney and epididymis. Am. J. Physiol. Cell Physiol. 287, C149-C162 (2004).
    • (2004) Am. J. Physiol. Cell Physiol , vol.287
    • Paunescu, T.G.1
  • 57
    • 0037184028 scopus 로고    scopus 로고
    • + pump with G subunit isoforms (G1 and G2) in mouse neurons
    • + pump with G subunit isoforms (G1 and G2) in mouse neurons. J. Biol. Chem. 277, 36296-36303 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 36296-36303
    • Murata, Y.1
  • 58
    • 23944509836 scopus 로고    scopus 로고
    • +-ATPase d2 subunit: Molecular characterization, developmental regulation, and localization to specialized proton pumps in kidney and bone
    • +-ATPase d2 subunit: molecular characterization, developmental regulation, and localization to specialized proton pumps in kidney and bone. J. Am. Soc. Nephrol. 16, 1245-1256 (2005).
    • (2005) J. Am. Soc. Nephrol , vol.16 , pp. 1245-1256
    • Smith, A.N.1
  • 59
    • 34347238974 scopus 로고    scopus 로고
    • +-ATPase are linked by an interaction between the G and a subunits. J. Biol. Chem. 282, 14421-14427 (2007).
    • +-ATPase are linked by an interaction between the G and a subunits. J. Biol. Chem. 282, 14421-14427 (2007).
  • 60
    • 33644935227 scopus 로고    scopus 로고
    • + ATPase: Molecular structure and function, physiological roles and regulation
    • + ATPase: molecular structure and function, physiological roles and regulation. J. Exp. Biol. 209, 577-589 (2006).
    • (2006) J. Exp. Biol , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 61
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta, E. S., Ebersold, M., Garrett, W., Pypaert, M. & Mellman, I. Activation of lysosomal function during dendritic cell maturation. Science 299, 1400-1403 (2003).
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 62
    • 11844260070 scopus 로고    scopus 로고
    • +-ATPase assembly, translocation and acidification of intracellular compartments in renal epithelial cells
    • +-ATPase assembly, translocation and acidification of intracellular compartments in renal epithelial cells. Mol. Cell. Biol. 25, 575-589 (2005).
    • (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
  • 63
    • 0035816719 scopus 로고    scopus 로고
    • Microtubules are involved in glucose-dependent dissociation of the yeast V-ATPase in vivo
    • Xu, T. & Forgac, M. Microtubules are involved in glucose-dependent dissociation of the yeast V-ATPase in vivo. J. Biol. Chem. 276, 24855-24861 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 24855-24861
    • Xu, T.1    Forgac, M.2
  • 64
    • 0035067367 scopus 로고    scopus 로고
    • Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly
    • Seol, J. H., Shevchenko, A., Shevchenko, A. & Deshaies, R. J. Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly. Nature Cell Biol. 3, 384-391 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 384-391
    • Seol, J.H.1    Shevchenko, A.2    Shevchenko, A.3    Deshaies, R.J.4
  • 65
    • 0037134525 scopus 로고    scopus 로고
    • The RAVE complex is essential for stable assembly of the yeast V-ATPase
    • Smardon, A. M., Tarsio, M. & Kane, P. M. The RAVE complex is essential for stable assembly of the yeast V-ATPase. J. Biol. Chem. 277, 13831-13839 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 13831-13839
    • Smardon, A.M.1    Tarsio, M.2    Kane, P.M.3
  • 67
  • 68
    • 0037630395 scopus 로고    scopus 로고
    • Mutational analysis of the non-homologous region of subunit A of the yeast V-ATPase
    • Shao, E., Nishi, T., Kawasaki-Nishi, S. & Forgac, M. Mutational analysis of the non-homologous region of subunit A of the yeast V-ATPase. J. Biol. Chem. 278, 12985-12991 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 12985-12991
    • Shao, E.1    Nishi, T.2    Kawasaki-Nishi, S.3    Forgac, M.4
  • 69
    • 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. & Forgac, M. 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).
    • (2004) J. Biol. Chem , vol.279 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 70
    • 34548319580 scopus 로고    scopus 로고
    • Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity
    • Qi, J. & Forgac, M. Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity. J. Biol. Chem. 282, 24743-24751 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 24743-24751
    • Qi, J.1    Forgac, M.2
  • 71
    • 1242291596 scopus 로고    scopus 로고
    • Bicarbonate-regulated adenylyl cyclase (sAC) is a sensor that regulates pH-dependent V-ATPase recycling
    • Pastor-Soler, N. et al. Bicarbonate-regulated adenylyl cyclase (sAC) is a sensor that regulates pH-dependent V-ATPase recycling. J. Biol. Chem. 278, 49523-49529 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 49523-49529
    • Pastor-Soler, N.1
  • 72
    • 14844318508 scopus 로고    scopus 로고
    • +-ATPase recycling
    • +-ATPase recycling. J. Biol. Chem. 280, 8452-8463 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 8452-8463
    • Beaulieu, V.1
  • 73
    • 0034644703 scopus 로고    scopus 로고
    • +-ATPase contains a filamentous actin binding site
    • +-ATPase contains a filamentous actin binding site. J. Biol. Chem. 275, 32331-32337 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 32331-32337
    • Holliday, L.S.1
  • 75
    • 10744233422 scopus 로고    scopus 로고
    • +-ATPase binding to microfilaments: regulation in response to phosphatidylinositol 3-kinase activity and detailed characterization of the actin-binding site in subunit B. J. Biol. Chem. 279, 7988-7998 (2004).
    • +-ATPase binding to microfilaments: regulation in response to phosphatidylinositol 3-kinase activity and detailed characterization of the actin-binding site in subunit B. J. Biol. Chem. 279, 7988-7998 (2004).
  • 76
    • 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 to actin filaments
    • Vitavska, O., Merzendorfer, H. & Wieczorek, H. The V-ATPase subunit C binds to polymeric F-actin as well as to monomeric G-actin and induces cross-linking to actin filaments. J. Biol. Chem. 280, 1070-1076 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 1070-1076
    • Vitavska, O.1    Merzendorfer, H.2    Wieczorek, H.3
  • 77
    • 33749580695 scopus 로고    scopus 로고
    • 0 subunit d that is critical for coupling of the yeast vacuolar proton-translocating ATPase
    • 0 subunit d that is critical for coupling of the yeast vacuolar proton-translocating ATPase. J. Biol. Chem. 281, 30001-30014 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 30001-30014
    • Owegi, M.A.1
  • 78
    • 33745859044 scopus 로고    scopus 로고
    • Mechanisms of pathogen entry through the endosomal compartments
    • Gruenberg, J. & van der Goot, F. G. Mechanisms of pathogen entry through the endosomal compartments. Nature Rev. Mol. Cell Biol. 7, 495-504 (2006).
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 495-504
    • Gruenberg, J.1    van der Goot, F.G.2
  • 79
    • 4444224022 scopus 로고    scopus 로고
    • Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway
    • Abrami, L., Lindsay, M., Parton, R. G., Leppla, S. H. & van der Goot, F. G. Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway. J. Cell Biol. 166, 645-651 (2004).
    • (2004) J. Cell Biol , vol.166 , pp. 645-651
    • Abrami, L.1    Lindsay, M.2    Parton, R.G.3    Leppla, S.H.4    van der Goot, F.G.5
  • 80
    • 0037047282 scopus 로고    scopus 로고
    • Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery
    • Geyer, M. et al. Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery. J. Biol. Chem. 277, 28521-2859 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 28521-32859
    • Geyer, M.1
  • 81
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters, C. et al. Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409, 581-588 (2001).
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1
  • 83
    • 20544470501 scopus 로고    scopus 로고
    • 0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila
    • 0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila. Cell 121, 607-620 (2005).
    • (2005) Cell , vol.121 , pp. 607-620
    • Hiesinger, P.R.1
  • 84
    • 33745280126 scopus 로고    scopus 로고
    • 0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans
    • 0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans. J. Cell Biol. 173, 949-961 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 949-961
    • Liegeois, S.1    Benedetto, A.2    Garnier, J.M.3    Schwab, Y.4    Labouesse, M.5
  • 85
    • 33751511196 scopus 로고    scopus 로고
    • The a3 isoform of V-ATPase regulates insulin secretion from pancreatic β-cells
    • Sun-Wada, G. H. et al. The a3 isoform of V-ATPase regulates insulin secretion from pancreatic β-cells. J. Cell Sci. 119, 4531-4540 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 4531-4540
    • Sun-Wada, G.H.1
  • 87
    • 2442560191 scopus 로고    scopus 로고
    • +-ATPase in human breast cancer cells with distinct metastatic potential: Distribution and functional activity
    • This study provided the first compelling evidence for a role of plasma membrane V-ATPases in tumour-cell invasion
    • +-ATPase in human breast cancer cells with distinct metastatic potential: distribution and functional activity. Am. J. Physiol. Cell Physiol. 286, C1443-C1452 (2004). This study provided the first compelling evidence for a role of plasma membrane V-ATPases in tumour-cell invasion.
    • (2004) Am. J. Physiol. Cell Physiol , vol.286
    • Sennoune, S.R.1
  • 88
    • 4644256731 scopus 로고    scopus 로고
    • +-ATPases at the plasma membrane regulate pH and cell migration in microvascular endothelial cells
    • +-ATPases at the plasma membrane regulate pH and cell migration in microvascular endothelial cells. J. Cell. Physiol. 201, 190-200 (2004).
    • (2004) J. Cell. Physiol , vol.201 , pp. 190-200
    • Rojas, J.D.1
  • 89
    • 33744506178 scopus 로고    scopus 로고
    • +-V-ATPase-dependent proton flux is necessary for consistent left-right patterning of non-mammalian vertebrates
    • +-V-ATPase-dependent proton flux is necessary for consistent left-right patterning of non-mammalian vertebrates. Development 133, 1657-1671 (2006).
    • (2006) Development , vol.133 , pp. 1657-1671
    • Adams, D.S.1
  • 90
    • 33646537184 scopus 로고    scopus 로고
    • Bowman, E. J. & Bowman, B. J. V-ATPases as drug targets. J. Bioenerg. Biomembr. 37, 431-435 (2005).
    • Bowman, E. J. & Bowman, B. J. V-ATPases as drug targets. J. Bioenerg. Biomembr. 37, 431-435 (2005).
  • 91
    • 0037040244 scopus 로고    scopus 로고
    • Mutations in subunit c of the V-ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site
    • Bowman, B. J. & Bowman, E. J. Mutations in subunit c of the V-ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site. J. Biol. Chem. 277, 3965-3972 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 3965-3972
    • Bowman, B.J.1    Bowman, E.J.2
  • 92
    • 0037175008 scopus 로고    scopus 로고
    • 0 subunit c
    • 0 subunit c. J. Biol. Chem. 277, 40544-40548 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 40544-40548
    • Huss, M.1
  • 93
    • 33751085062 scopus 로고    scopus 로고
    • Bowman, B. J., McCall, M. E., Baertsch, R. & Bowman, E. J. A model for the proteolipid ring and Bafilomycin/Concanamycin binding site in the vacuolar ATPase of Neurospora crassa. J. Biol. Chem. 281, 31885-31893 (2006). This paper provides the first molecular model for the binding site of the highly specific V-ATPase inhibitors bafilomycin and concanamycin.
    • Bowman, B. J., McCall, M. E., Baertsch, R. & Bowman, E. J. A model for the proteolipid ring and Bafilomycin/Concanamycin binding site in the vacuolar ATPase of Neurospora crassa. J. Biol. Chem. 281, 31885-31893 (2006). This paper provides the first molecular model for the binding site of the highly specific V-ATPase inhibitors bafilomycin and concanamycin.
  • 95
    • 17744370342 scopus 로고    scopus 로고
    • Synthesis of photoactivatable acyclic analogues of the lobatamides
    • Shen, R., Inoue, T., Forgac, M. & Porco, J. A. Synthesis of photoactivatable acyclic analogues of the lobatamides. J. Org. Chem. 70, 3686-3692 (2004).
    • (2004) J. Org. Chem , vol.70 , pp. 3686-3692
    • Shen, R.1    Inoue, T.2    Forgac, M.3    Porco, J.A.4
  • 96
    • 2442522365 scopus 로고    scopus 로고
    • 0 sector of the V-ATPase through a mechanism distinct from bafilomycin A1
    • 0 sector of the V-ATPase through a mechanism distinct from bafilomycin A1. J. Biol. Chem. 279, 19755-19763 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 19755-19763
    • Xie, X.S.1
  • 97
    • 3042784841 scopus 로고    scopus 로고
    • A novel inhibitor of vacuolar ATPase, FR167356, which can discriminate between osteoclast vacuolar ATPase and lysosomal vacuolar ATPase
    • Niikura, K., Takano, M. & Sawada, M. A novel inhibitor of vacuolar ATPase, FR167356, which can discriminate between osteoclast vacuolar ATPase and lysosomal vacuolar ATPase. Br. J. Pharmacol. 142, 558-566 (2004).
    • (2004) Br. J. Pharmacol , vol.142 , pp. 558-566
    • Niikura, K.1    Takano, M.2    Sawada, M.3
  • 98
    • 0032943534 scopus 로고    scopus 로고
    • +-ATPase cause renal tubular acidosis with sensorineural deafness
    • +-ATPase cause renal tubular acidosis with sensorineural deafness. Nature Genet. 21, 84-90 (1999).
    • (1999) Nature Genet , vol.21 , pp. 84-90
    • Karet, F.E.1
  • 99
    • 0033812944 scopus 로고    scopus 로고
    • Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116 kDa subunit, cause recessive distal renal tubular acidosis with preserved hearing
    • Smith, A. N. et al. Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116 kDa subunit, cause recessive distal renal tubular acidosis with preserved hearing. Nature Genet. 26, 71-75 (2000).
    • (2000) Nature Genet , vol.26 , pp. 71-75
    • Smith, A.N.1
  • 100
    • 34447272956 scopus 로고    scopus 로고
    • Relocalization of the V-ATPase B2 subunit to the apical membraneof epididymal clear cells of mice deficient in the B1 subunit
    • Da Silva, N. et al. Relocalization of the V-ATPase B2 subunit to the apical membraneof epididymal clear cells of mice deficient in the B1 subunit. Am. J. Physiol. Cell Physiol. 293, 199-210 (2007).
    • (2007) Am. J. Physiol. Cell Physiol , vol.293 , pp. 199-210
    • Da Silva, N.1
  • 101
    • 0033946477 scopus 로고    scopus 로고
    • Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis
    • Frattini, A. et al. Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis. Nature Genet. 25, 343-346 (2000).
    • (2000) Nature Genet , vol.25 , pp. 343-346
    • Frattini, A.1
  • 105
    • 0034678130 scopus 로고    scopus 로고
    • ARF1 regulates pH-dependent COP functions in the early endocytic pathway
    • Gu, F. & Gruenberg, J. ARF1 regulates pH-dependent COP functions in the early endocytic pathway. J. Biol. Chem. 275, 8154-8160 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 8154-8160
    • Gu, F.1    Gruenberg, J.2


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