메뉴 건너뛰기




Volumn 295, Issue 4, 2008, Pages

Human H+ ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1

Author keywords

Acidosis; Glycolysis; Kidney; Proton pump; Yeast

Indexed keywords

6 PHOSPHOFRUCTOKINASE; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE A4; UNCLASSIFIED DRUG;

EID: 57049182517     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.90258.2008     Document Type: Article
Times cited : (50)

References (60)
  • 1
    • 0019818326 scopus 로고
    • Clinical and pathophysiologic spectrum of acquired distal renal tubular acidosis
    • Batlle DC, Sehy JT, Roseman MK, Arruda JA, Kurtzman NA. Clinical and pathophysiologic spectrum of acquired distal renal tubular acidosis. Kidney Int 20: 389-396, 1981.
    • (1981) Kidney Int , vol.20 , pp. 389-396
    • Batlle, D.C.1    Sehy, J.T.2    Roseman, M.K.3    Arruda, J.A.4    Kurtzman, N.A.5
  • 2
    • 0017106217 scopus 로고
    • + transport in the turtle urinary bladder. Coupling of transport to glucose oxidation
    • + transport in the turtle urinary bladder. Coupling of transport to glucose oxidation. J Gen Physiol 68: 421-439, 1976.
    • (1976) J Gen Physiol , vol.68 , pp. 421-439
    • Beauwens, R.1    Al-Awqati, Q.2
  • 3
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Bohm G, Muhr R, Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng 5: 191-195, 1992.
    • (1992) Protein Eng , vol.5 , pp. 191-195
    • Bohm, G.1    Muhr, R.2    Jaenicke, R.3
  • 4
    • 33846268425 scopus 로고    scopus 로고
    • New insights into the regulation of V-ATPase-dependent proton secretion
    • Breton S, Brown D. New insights into the regulation of V-ATPase-dependent proton secretion. Am J Physiol Renal Physiol 292: F1-F10, 2007.
    • (2007) Am J Physiol Renal Physiol , vol.292
    • Breton, S.1    Brown, D.2
  • 5
    • 0026795802 scopus 로고
    • A plasma membrane proton ATPase in specialized cells of rat epididymis
    • Brown D, Lui B, Gluck S, Sabolic I. A plasma membrane proton ATPase in specialized cells of rat epididymis. Am J Physiol Cell Physiol 263: C913-C916, 1992.
    • (1992) Am J Physiol Cell Physiol , vol.263
    • Brown, D.1    Lui, B.2    Gluck, S.3    Sabolic, I.4
  • 7
    • 0020964799 scopus 로고
    • Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme
    • Daldal F. Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme. J Mol Biol 168: 285-305, 1983.
    • (1983) J Mol Biol , vol.168 , pp. 285-305
    • Daldal, F.1
  • 8
    • 0020574746 scopus 로고
    • A review of animal phosphofructokinase isozymes with an emphasis on their physiological role
    • Dunaway GA. A review of animal phosphofructokinase isozymes with an emphasis on their physiological role. Mol Cell Biochem 52: 75-91, 1983.
    • (1983) Mol Cell Biochem , vol.52 , pp. 75-91
    • Dunaway, G.A.1
  • 9
    • 0036374134 scopus 로고    scopus 로고
    • Cterminal modification of 6-phosphofructo-1-kinase from Saccharomyces cerevisiae and its influence on enzyme structure and activity
    • Edelmann A, Kirchberger J, Heinisch JJ, Kopperschlager G. Cterminal modification of 6-phosphofructo-1-kinase from Saccharomyces cerevisiae and its influence on enzyme structure and activity. Biochem Biophys Res Commun 295: 992-999, 2002.
    • (2002) Biochem Biophys Res Commun , vol.295 , pp. 992-999
    • Edelmann, A.1    Kirchberger, J.2    Heinisch, J.J.3    Kopperschlager, G.4
  • 10
    • 0020479124 scopus 로고
    • Properties of phospho and dephospho forms of muscle phosphofructokinase
    • Foe LG, Kemp RG. Properties of phospho and dephospho forms of muscle phosphofructokinase. J Biol Chem 257: 6368-6372, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 6368-6372
    • Foe, L.G.1    Kemp, R.G.2
  • 11
    • 0033967198 scopus 로고    scopus 로고
    • +-ATPases
    • +-ATPases. J Exp Biol 203: 71-80, 2000.
    • (2000) J Exp Biol , vol.203 , pp. 71-80
    • Forgac, M.1
  • 13
    • 15944371520 scopus 로고    scopus 로고
    • Inhibition sites in F1-ATPase from bovine heart mitochondria
    • Gledhill JR, Walker JE. Inhibition sites in F1-ATPase from bovine heart mitochondria. Biochem J 386: 591-598, 2005.
    • (2005) Biochem J , vol.386 , pp. 591-598
    • Gledhill, J.R.1    Walker, J.E.2
  • 14
    • 0026801517 scopus 로고
    • + ATPase in proximal and distal urinary acidification
    • + ATPase in proximal and distal urinary acidification. J Bioenerg Biomembr 24: 351-359, 1992.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 351-359
    • Gluck, S.L.1
  • 15
    • 0032514213 scopus 로고    scopus 로고
    • +-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex
    • +-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex. J Biol Chem 142: 39-49, 1998.
    • (1998) J Biol Chem , vol.142 , pp. 39-49
    • Graham, L.A.1    Hill, K.J.2    Stevens, T.H.3
  • 17
    • 0022911240 scopus 로고
    • Construction and physiological characterization of mutants disrupted in the phosphofructokinase genes of Saccharomyces cerevisiae
    • Heinisch J. Construction and physiological characterization of mutants disrupted in the phosphofructokinase genes of Saccharomyces cerevisiae. Curr Genet 11: 227-234, 1986.
    • (1986) Curr Genet , vol.11 , pp. 227-234
    • Heinisch, J.1
  • 23
    • 0035861664 scopus 로고    scopus 로고
    • The amino-terminal domain of the vacuolar proton-translocating 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 TH. The amino-terminal domain of the vacuolar proton-translocating 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
  • 24
    • 0035940474 scopus 로고    scopus 로고
    • Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
    • Kawasaki-Nishi S, Nishi T, Forgac M. Arg-735 of the 100-kDa subunit a 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
  • 25
    • 0023657724 scopus 로고
    • Amino acid sequence at the citrate allosteric site of rabbit muscle phosphofructokinase
    • Kemp RG, Fox RW, Latshaw SP. Amino acid sequence at the citrate allosteric site of rabbit muscle phosphofructokinase. Biochemistry 26: 3443-3446, 1987.
    • (1987) Biochemistry , vol.26 , pp. 3443-3446
    • Kemp, R.G.1    Fox, R.W.2    Latshaw, S.P.3
  • 26
    • 0037199468 scopus 로고    scopus 로고
    • Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase
    • Kemp RG, Gunasekera D. Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase. Biochemistry 41: 9426-9430, 2002.
    • (2002) Biochemistry , vol.41 , pp. 9426-9430
    • Kemp, R.G.1    Gunasekera, D.2
  • 29
    • 0032549629 scopus 로고    scopus 로고
    • Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase
    • Leng XH, Manolson MF, Forgac M. Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase. J Biol Chem 273: 6717-6723, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 6717-6723
    • Leng, X.H.1    Manolson, M.F.2    Forgac, M.3
  • 30
    • 0033591450 scopus 로고    scopus 로고
    • Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase
    • Leng XH, Nishi T, Forgac M. Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase. J Biol Chem 274: 14655-14661, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 14655-14661
    • Leng, X.H.1    Nishi, T.2    Forgac, M.3
  • 31
    • 0027363656 scopus 로고
    • Site-directed mutagenesis of rabbit muscle phosphofructokinase cDNA. Mutations at glutamine 200 affect the allosteric properties of the enzyme
    • Li J, Zhu X, Byrnes M, Nelson JW, Chang SH. Site-directed mutagenesis of rabbit muscle phosphofructokinase cDNA. Mutations at glutamine 200 affect the allosteric properties of the enzyme. J Biol Chem 268: 24599-24606, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 24599-24606
    • Li, J.1    Zhu, X.2    Byrnes, M.3    Nelson, J.W.4    Chang, S.H.5
  • 32
    • 0033534164 scopus 로고    scopus 로고
    • Identification of allosteric sites in rabbit phosphofructo-1-kinase
    • Li Y, Rivera D, Ru W, Gunasekera D, Kemp RG. Identification of allosteric sites in rabbit phosphofructo-1-kinase. Biochemistry 38: 16407-16412, 1999.
    • (1999) Biochemistry , vol.38 , pp. 16407-16412
    • Li, Y.1    Rivera, D.2    Ru, W.3    Gunasekera, D.4    Kemp, R.G.5
  • 33
    • 0029782419 scopus 로고    scopus 로고
    • Mutational analysis of the catalytic subunit of the yeast vacuolar proton-translocating ATPase
    • Liu J, Kane PM. Mutational analysis of the catalytic subunit of the yeast vacuolar proton-translocating ATPase. Biochemistry 35: 10938-10948, 1996.
    • (1996) Biochemistry , vol.35 , pp. 10938-10948
    • Liu, J.1    Kane, P.M.2
  • 34
    • 34548300007 scopus 로고    scopus 로고
    • +-ATPase is essential for the assembly and activity of the proton pump
    • +-ATPase is essential for the assembly and activity of the proton pump. J Biol Chem 282: 24495-24503, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 24495-24503
    • Lu, M.1    Ammar, D.2    Ives, H.3    Albrecht, F.4    Gluck, S.L.5
  • 35
    • 0035839499 scopus 로고    scopus 로고
    • +-ATPase: Evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump
    • +-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J Biol Chem 276: 30407-30413, 2001.
    • (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
  • 37
    • 0031961872 scopus 로고    scopus 로고
    • Mutational analysis of the nucleotide binding sites of the yeast vacuolar proton-translocating ATPase
    • MacLeod KJ, Vasilyeva E, Baleja JD, Forgac M. Mutational analysis of the nucleotide binding sites of the yeast vacuolar proton-translocating ATPase. J Biol Chem 273: 150-156, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 150-156
    • MacLeod, K.J.1    Vasilyeva, E.2    Baleja, J.D.3    Forgac, M.4
  • 42
    • 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
  • 44
    • 33748742279 scopus 로고    scopus 로고
    • Effects of human a3 and a4 mutations that result in osteopetrosis and distal renal tubular acidosis on yeast V-ATPase expression and activity
    • Ochotny N, Van Vliet A, Chan N, Yao Y, Morel M, Kartner N, von Schroeder HP, Heersche JN, Manolson MF. Effects of human a3 and a4 mutations that result in osteopetrosis and distal renal tubular acidosis on yeast V-ATPase expression and activity. J Biol Chem 281: 26102-26111, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 26102-26111
    • Ochotny, N.1    Van Vliet, A.2    Chan, N.3    Yao, Y.4    Morel, M.5    Kartner, N.6    von Schroeder, H.P.7    Heersche, J.N.8    Manolson, M.F.9
  • 46
    • 0031597366 scopus 로고    scopus 로고
    • +-ATPase is an unconventional glucose-induced effect
    • +-ATPase is an unconventional glucose-induced effect. Mol Cell Biol 18: 7064-7074, 1998.
    • (1998) Mol Cell Biol , vol.18 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 47
    • 0025907484 scopus 로고
    • Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump
    • Perin MS, Fried VA, Stone DK, Xie XS, Sudhof TC. Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump. J Biol Chem 266: 3877-3881, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 3877-3881
    • Perin, M.S.1    Fried, V.A.2    Stone, D.K.3    Xie, X.S.4    Sudhof, T.C.5
  • 49
    • 2342435823 scopus 로고    scopus 로고
    • The yeast V-ATPase contains a subunit homologous to the M. sexta and bovine e subunits that is essential for function
    • Sambade M, Kane PM. The yeast V-ATPase contains a subunit homologous to the M. 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
  • 50
    • 0037630395 scopus 로고    scopus 로고
    • Mutational analysis of the nonhomologous region of subunit A of the yeast V-ATPase
    • Shao E, Nishi T, Kawasaki-Nishi S, Forgac M. Mutational analysis of the nonhomologous 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
  • 56
    • 18744379726 scopus 로고    scopus 로고
    • Stover EH, Borthwick KJ, Bavalia C, Eady N, Fritz DM, Rungroj N, Giersch AB, Morton CC, Axon PR, Akil I, Al-Sabban EA, Baguley DM, Bianca S, Bakkaloglu A, Bircan Z, Chauveau D, Clermont MJ, Guala A, Hulton SA, Kroes H, Li Volti G, Mir S, Mocan H, Nayir A, Ozen S, Rodriguez Soriano J, Sanjad SA, Tasic V, Taylor CM, Topaloglu R, Smith AN, Karet FE. Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss. J Med Genet 39: 796-803, 2002.
    • Stover EH, Borthwick KJ, Bavalia C, Eady N, Fritz DM, Rungroj N, Giersch AB, Morton CC, Axon PR, Akil I, Al-Sabban EA, Baguley DM, Bianca S, Bakkaloglu A, Bircan Z, Chauveau D, Clermont MJ, Guala A, Hulton SA, Kroes H, Li Volti G, Mir S, Mocan H, Nayir A, Ozen S, Rodriguez Soriano J, Sanjad SA, Tasic V, Taylor CM, Topaloglu R, Smith AN, Karet FE. Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss. J Med Genet 39: 796-803, 2002.
  • 58
    • 33646372973 scopus 로고    scopus 로고
    • Vargas-Poussou R, Houillier P, Le Pottier N, Strompf L, Loirat C, Baudouin V, Macher MA, Dechaux M, Ulinski T, Nobili F, Eckart P, Novo R, Cailliez M, Salomon R, Nivet H, Cochat P, Tack I, Fargeot A, Bouissou F, Kesler GR, Lorotte S, Godefroid N, Layet V, Morin G, Jeunemaitre X, Blanchard A. Genetic investigation of autosomal recessive distal renal tubular acidosis: evidence for early sensorineural hearing loss associated with mutations in the ATP6V0A4 gene. J Am Soc Nephrol 17: 1437-1443, 2006.
    • Vargas-Poussou R, Houillier P, Le Pottier N, Strompf L, Loirat C, Baudouin V, Macher MA, Dechaux M, Ulinski T, Nobili F, Eckart P, Novo R, Cailliez M, Salomon R, Nivet H, Cochat P, Tack I, Fargeot A, Bouissou F, Kesler GR, Lorotte S, Godefroid N, Layet V, Morin G, Jeunemaitre X, Blanchard A. Genetic investigation of autosomal recessive distal renal tubular acidosis: evidence for early sensorineural hearing loss associated with mutations in the ATP6V0A4 gene. J Am Soc Nephrol 17: 1437-1443, 2006.
  • 60
    • 0028358811 scopus 로고
    • Identification of interactions that stabilize the transition state in Escherichia coli phosphofructo-1-kinase
    • Zheng RL, Kemp RG. Identification of interactions that stabilize the transition state in Escherichia coli phosphofructo-1-kinase. J Biol Chem 269: 18475-18479, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 18475-18479
    • Zheng, R.L.1    Kemp, R.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.