메뉴 건너뛰기




Volumn 4, Issue 1, 2011, Pages 120-125

pH-dependent localization of Btn1p in the yeast model for Batten disease

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; PROTEIN BTN1P; UNCLASSIFIED DRUG;

EID: 78650912761     PISSN: 17548403     EISSN: 17548411     Source Type: Journal    
DOI: 10.1242/dmm.006114     Document Type: Article
Times cited : (10)

References (37)
  • 1
    • 0024510036 scopus 로고
    • Interaction of anions and ATP with the coated vesicle proton pump
    • Arai, H., Pink, S. and Forgac, M. (1989). Interaction of anions and ATP with the coated vesicle proton pump. Biochemistry 28, 3075-3082.
    • (1989) Biochemistry , vol.28 , pp. 3075-3082
    • Arai, H.1    Pink, S.2    Forgac, M.3
  • 2
    • 0041706233 scopus 로고    scopus 로고
    • Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase
    • Chung, J. H., Lester, R. L. and Dickson, R. C. (2003). Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J. Biol. Chem. 278, 28872-28881.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28872-28881
    • Chung, J.H.1    Lester, R.L.2    Dickson, R.C.3
  • 3
    • 54449098487 scopus 로고    scopus 로고
    • Gene symbol: CLN6. Disease: Neuronal ceroid lipofuscinosis, late Infantile
    • Cismondi, I. A., Kohan, R., Ghio, A., Ramirez, A. M. and Halac, I. N. (2008). Gene symbol: CLN6. Disease: Neuronal ceroid lipofuscinosis, late Infantile. Hum. Genet. 124, 324.
    • (2008) Hum. Genet. , vol.124 , pp. 324
    • Cismondi, I.A.1    Kohan, R.2    Ghio, A.3    Ramirez, A.M.4    Halac, I.N.5
  • 4
    • 66849138215 scopus 로고    scopus 로고
    • S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p
    • Codlin, S. and Mole, S. E. (2009). S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p. J. Cell Sci. 122, 1163-1173.
    • (2009) J. Cell Sci. , vol.122 , pp. 1163-1173
    • Codlin, S.1    Mole, S.E.2
  • 5
    • 0032544574 scopus 로고    scopus 로고
    • The subcellular location of the yeast Saccharomyces cerevisiae homologue of the protein defective in the juvenile form of Batten disease
    • Croopnick, J. B., Choi, H. C. and Mueller, D. M. (1998). The subcellular location of the yeast Saccharomyces cerevisiae homologue of the protein defective in the juvenile form of Batten disease. Biochem. Biophys. Res. Commun. 250, 335-341.
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 335-341
    • Croopnick, J.B.1    Choi, H.C.2    Mueller, D.M.3
  • 6
    • 0343471377 scopus 로고    scopus 로고
    • Modification of a PCR-based site-directed mutagenesis method
    • 574
    • Fisher, C. L. and Pei, G. K. (1997). Modification of a PCR-based site-directed mutagenesis method. Biotechniques 23, 570-571, 574.
    • (1997) Biotechniques , vol.23 , pp. 570-571
    • Fisher, C.L.1    Pei, G.K.2
  • 7
    • 0033531950 scopus 로고    scopus 로고
    • Structure and properties of the vacuolar (H+)-ATPases
    • Forgac, M. (1999). Structure and properties of the vacuolar (H+)-ATPases. J. Biol. Chem. 274, 12951-12954.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12951-12954
    • Forgac, M.1
  • 8
    • 30544437316 scopus 로고    scopus 로고
    • Btn1, the Schizosaccharomyces pombe homologue of the human Batten disease gene CLN3, regulates vacuole homeostasis
    • Gachet, Y., Codlin, S., Hyams, J. S. and Mole, S. E. (2005). btn1, the Schizosaccharomyces pombe homologue of the human Batten disease gene CLN3, regulates vacuole homeostasis. J. Cell Sci. 118, 5525-5536.
    • (2005) J. Cell Sci. , vol.118 , pp. 5525-5536
    • Gachet, Y.1    Codlin, S.2    Hyams, J.S.3    Mole, S.E.4
  • 9
    • 0033973341 scopus 로고    scopus 로고
    • Composition and assembly of the yeast vacuolar H(+)-ATPase complex
    • Graham, L. A., Powell, B. and Stevens, T. H. (2000). Composition and assembly of the yeast vacuolar H(+)-ATPase complex. J. Exp. Biol. 203, 61-70.
    • (2000) J. Exp. Biol. , vol.203 , pp. 61-70
    • Graham, L.A.1    Powell, B.2    Stevens, T.H.3
  • 10
    • 0029994841 scopus 로고    scopus 로고
    • A new efficient gene disruption cassette for repeated use in budding yeast
    • Guldener, U., Heck, S., Fielder, T., Beinhauer, J. and Hegemann, J. H. (1996). A new efficient gene disruption cassette for repeated use in budding yeast. Nucleic Acids Res. 24, 2519-2524.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2519-2524
    • Guldener, U.1    Heck, S.2    Fielder, T.3    Beinhauer, J.4    Hegemann, J.H.5
  • 12
    • 27744480250 scopus 로고    scopus 로고
    • Deletion of the glucosidase II gene in Trypanosoma brucei reveals novel N-glycosylation mechanisms in the biosynthesis of variant surface glycoprotein
    • Jones, D. C., Mehlert, A., Guther, M. L. and Ferguson, M. A. (2005). Deletion of the glucosidase II gene in Trypanosoma brucei reveals novel N-glycosylation mechanisms in the biosynthesis of variant surface glycoprotein. J. Biol. Chem. 280, 35929-35942.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35929-35942
    • Jones, D.C.1    Mehlert, A.2    Guther, M.L.3    Ferguson, M.A.4
  • 13
    • 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
  • 14
    • 0033974290 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H(+)-ATPase
    • Kane, P. M. and Parra, K. J. (2000). Assembly and regulation of the yeast vacuolar H(+)-ATPase. J. Exp. Biol. 203, 81-87.
    • (2000) J. Exp. Biol. , vol.203 , pp. 81-87
    • Kane, P.M.1    Parra, K.J.2
  • 15
    • 0347364649 scopus 로고    scopus 로고
    • A role in vacuolar arginine transport for yeast Btn1p and for human CLN3, the protein defective in Batten disease
    • Kim, Y., Ramirez-Montealegre, D. and Pearce, D. A. (2003). A role in vacuolar arginine transport for yeast Btn1p and for human CLN3, the protein defective in Batten disease. Proc. Natl. Acad. Sci. USA 100, 15458-15462.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15458-15462
    • Kim, Y.1    Ramirez-Montealegre, D.2    Pearce, D.A.3
  • 16
    • 1542313968 scopus 로고    scopus 로고
    • Two Motifs Target Batten Disease Protein CLN3 to Lysosomes in Transfected Nonneuronal and Neuronal Cells
    • DOI 10.1091/mbc.E03-02-0120
    • Kyttala, A., Ihrke, G., Vesa, J., Schell, M. J. and Luzio, J. P. (2004). Two motifs target Batten disease protein CLN3 to lysosomes in transfected nonneuronal and neuronal cells. Mol. Biol. Cell 15, 1313-1323. (Pubitemid 38316237)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1313-1323
    • Kyttala, A.1    Ihrke, G.2    Vesa, J.3    Schell, M.J.4    Luzio, J.P.5
  • 20
    • 0019411588 scopus 로고
    • Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
    • Ohsumi, Y. and Anraku, Y. (1981). Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J. Biol. Chem. 256, 2079-2082.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2079-2082
    • Ohsumi, Y.1    Anraku, Y.2
  • 21
    • 0030834977 scopus 로고    scopus 로고
    • Mutations in the CYS4 gene provide evidence for regulation of the yeast vacuolar H+-ATPase by oxidation and reduction in vivo
    • Oluwatosin, Y. E. and Kane, P. M. (1997). Mutations in the CYS4 gene provide evidence for regulation of the yeast vacuolar H+-ATPase by oxidation and reduction in vivo. J Biol. Chem. 272, 28149-28157.
    • (1997) J Biol. Chem. , vol.272 , pp. 28149-28157
    • Oluwatosin, Y.E.1    Kane, P.M.2
  • 22
    • 33744530432 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae lacking Btn1p modulate vacuolar ATPase activity to regulate pH imbalance in the vacuole
    • Padilla-Lopez, S. and Pearce, D. A. (2006). Saccharomyces cerevisiae lacking Btn1p modulate vacuolar ATPase activity to regulate pH imbalance in the vacuole. J. Biol. Chem. 281, 10273-10280.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10273-10280
    • Padilla-Lopez, S.1    Pearce, D.A.2
  • 23
    • 0030855171 scopus 로고    scopus 로고
    • BTN1, a yeast gene corresponding to the human gene responsible for Batten's disease, is not essential for viability, mitochondrial function, or degradation of mitochondrial ATP synthase
    • Pearce, D. A. and Sherman, F. (1997). BTN1, a yeast gene corresponding to the human gene responsible for Batten's disease, is not essential for viability, mitochondrial function, or degradation of mitochondrial ATP synthase. Yeast 13, 691-697.
    • (1997) Yeast , vol.13 , pp. 691-697
    • Pearce, D.A.1    Sherman, F.2
  • 24
    • 0032499745 scopus 로고    scopus 로고
    • A yeast model for the study of Batten disease
    • Pearce, D. A. and Sherman, F. (1998). A yeast model for the study of Batten disease. Proc. Natl. Acad. Sci. USA 95, 6915-6918.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6915-6918
    • Pearce, D.A.1    Sherman, F.2
  • 25
    • 0032905252 scopus 로고    scopus 로고
    • Action of BTN1, the yeast orthologue of the gene mutated in Batten disease
    • Pearce, D. A., Ferea, T., Nosel, S. A., Das, B. and Sherman, F. (1999). Action of BTN1, the yeast orthologue of the gene mutated in Batten disease. Nat. Genet. 22, 55-58.
    • (1999) Nat. Genet. , vol.22 , pp. 55-58
    • Pearce, D.A.1    Ferea, T.2    Nosel, S.A.3    Das, B.4    Sherman, F.5
  • 26
    • 0242317675 scopus 로고    scopus 로고
    • Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis
    • Peirson, S. N., Butler, J. N. and Foster, R. G. (2003). Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis. Nucleic Acids Res. 31, e73.
    • (2003) Nucleic Acids Res. , vol.31
    • Peirson, S.N.1    Butler, J.N.2    Foster, R.G.3
  • 27
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl, M. W., Horgan, G. W. and Dempfle, L. (2002). Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res. 30, e36.
    • (2002) Nucleic Acids Res. , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 28
    • 16444366586 scopus 로고    scopus 로고
    • CLN3, the protein associated with batten disease: Structure, function and localization
    • Phillips, S. N., Benedict, J. W., Weimer, J. M. and Pearce, D. A. (2005). CLN3, the protein associated with batten disease: structure, function and localization. J. Neurosci. Res. 79, 573-583.
    • (2005) J. Neurosci. Res. , vol.79 , pp. 573-583
    • Phillips, S.N.1    Benedict, J.W.2    Weimer, J.M.3    Pearce, D.A.4
  • 29
    • 34548319580 scopus 로고    scopus 로고
    • Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity
    • DOI 10.1074/jbc.M700663200
    • Qi, J. and Forgac, M. (2007). Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity. J. Biol. Chem. 282, 24743-24751. (Pubitemid 47347540)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24743-24751
    • Qi, J.1    Forgac, M.2
  • 30
    • 0035968245 scopus 로고    scopus 로고
    • A family of yeast proteins mediating bidirectional vacuolar amino acid transport
    • Russnak, R., Konczal, D. and McIntire, S. L. (2001). A family of yeast proteins mediating bidirectional vacuolar amino acid transport. J. Biol. Chem. 276, 23849-23857.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23849-23857
    • Russnak, R.1    Konczal, D.2    McIntire, S.L.3
  • 31
    • 3042722112 scopus 로고    scopus 로고
    • Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae
    • Sheff, M. A. and Thorn, K. S. (2004). Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae. Yeast 21, 661-670.
    • (2004) Yeast , vol.21 , pp. 661-670
    • Sheff, M.A.1    Thorn, K.S.2
  • 32
    • 14244258606 scopus 로고    scopus 로고
    • A family of basic amino acid transporters of the vacuolar membrane from Saccharomyces cerevisiae
    • Shimazu, M., Sekito, T., Akiyama, K., Ohsumi, Y. and Kakinuma, Y. (2005). A family of basic amino acid transporters of the vacuolar membrane from Saccharomyces cerevisiae. J. Biol. Chem. 280, 4851-4857.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4851-4857
    • Shimazu, M.1    Sekito, T.2    Akiyama, K.3    Ohsumi, Y.4    Kakinuma, Y.5
  • 33
    • 11144231239 scopus 로고    scopus 로고
    • A dileucine motif and a cluster of acidic amino acids in the second cytoplasmic domain of the batten disease-related CLN3 protein are required for efficient lysosomal targeting
    • Storch, S., Pohl, S. and Braulke, T. (2004). A dileucine motif and a cluster of acidic amino acids in the second cytoplasmic domain of the batten disease-related CLN3 protein are required for efficient lysosomal targeting. J. Biol. Chem. 279, 53625-53634.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53625-53634
    • Storch, S.1    Pohl, S.2    Braulke, T.3
  • 34
    • 33947245588 scopus 로고    scopus 로고
    • C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes
    • Storch, S., Pohl, S., Quitsch, A., Falley, K. and Braulke, T. (2007). C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes. Traffic 8, 431-444.
    • (2007) Traffic , vol.8 , pp. 431-444
    • Storch, S.1    Pohl, S.2    Quitsch, A.3    Falley, K.4    Braulke, T.5
  • 35
    • 0029147298 scopus 로고
    • Solation of a novel gene underlying Batten disease, CLN3
    • The International Batten Disease Consortium
    • The International Batten Disease Consortium (1995). Isolation of a novel gene underlying Batten disease, CLN3. Cell 82, 949-957.
    • (1995) Cell , vol.82 , pp. 949-957
  • 36
    • 34347369690 scopus 로고    scopus 로고
    • Absence of Btn1p in the yeast model for juvenile Batten disease may cause arginine to become toxic to yeast cells
    • Vitiello, S. P., Wolfe, D. M. and Pearce, D. A. (2007). Absence of Btn1p in the yeast model for juvenile Batten disease may cause arginine to become toxic to yeast cells. Hum. Mol. Genet. 16, 1007-1016.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1007-1016
    • Vitiello, S.P.1    Wolfe, D.M.2    Pearce, D.A.3
  • 37
    • 77950536687 scopus 로고    scopus 로고
    • Interaction between Sdo1p and Btn1p in the Saccharomyces cerevisiae model for Batten disease
    • Vitiello, S. P., Benedict, J. W., Padilla-Lopez, S. and Pearce, D. A. (2010). Interaction between Sdo1p and Btn1p in the Saccharomyces cerevisiae model for Batten disease. Hum. Mol. Genet. 19, 931-942.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 931-942
    • Vitiello, S.P.1    Benedict, J.W.2    Padilla-Lopez, S.3    Pearce, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.