메뉴 건너뛰기




Volumn 70, Issue 1, 2000, Pages 69-74

The tissue-specific, alternatively spliced single ATG exon of the type 3 voltage-dependent anion channel gene does not create a truncated protein isoform in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ANION CHANNEL; ANTIPORTER; ISOPROTEIN;

EID: 0034049927     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1006/mgme.2000.2987     Document Type: Article
Times cited : (28)

References (34)
  • 1
    • 0027238514 scopus 로고
    • Channels in mitochondrial membranes: Knowns, unknowns, and prospects for the future
    • Sorgato M, Moran O. Channels in mitochondrial membranes: Knowns, unknowns, and prospects for the future. Crit Rev Biochem Molec Biol. 28:1993;127-171.
    • (1993) Crit Rev Biochem Molec Biol , vol.28 , pp. 127-171
    • Sorgato, M.1    Moran, O.2
  • 2
    • 0026507895 scopus 로고
    • A soluble mitochondrial protein increases the voltage dependence of the mitochondrial channel, VDAC
    • Liu M Y, Colombini M. A soluble mitochondrial protein increases the voltage dependence of the mitochondrial channel, VDAC. J Bioenerg Biomembr. 24:1992;41-46.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 41-46
    • Liu, M.Y.1    Colombini, M.2
  • 3
    • 0029854155 scopus 로고    scopus 로고
    • ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane
    • Rostovtseva T, Colombini M. ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane. J Biol Chem. 271:1996;28006-28008.
    • (1996) J Biol Chem , vol.271 , pp. 28006-28008
    • Rostovtseva, T.1    Colombini, M.2
  • 4
    • 0028172237 scopus 로고
    • β-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6
    • Lee A C, Zizi M, Colombini M. β-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6. J Biol Chem. 269:1994;30974-30980.
    • (1994) J Biol Chem , vol.269 , pp. 30974-30980
    • Lee, A.C.1    Zizi, M.2    Colombini, M.3
  • 5
    • 0028158479 scopus 로고
    • NADH regulates the gating of VDAC, the mitochondrial outer membrane channel
    • Zizi M, Forte M, Blachly-Dyson E, Colombini M. NADH regulates the gating of VDAC, the mitochondrial outer membrane channel. J Biol Chem. 269:1994;1614-1616.
    • (1994) J Biol Chem , vol.269 , pp. 1614-1616
    • Zizi, M.1    Forte, M.2    Blachly-Dyson, E.3    Colombini, M.4
  • 6
    • 0025091803 scopus 로고
    • Interaction of mitochondrial porin with cytosolic proteins
    • Brdiczka D. Interaction of mitochondrial porin with cytosolic proteins. Experientia. 46:1990;161-167.
    • (1990) Experientia , vol.46 , pp. 161-167
    • Brdiczka, D.1
  • 7
    • 0031852596 scopus 로고    scopus 로고
    • Further studies on the coupling of mitochondrially bound hexokinase to intramitochondrially compartmented ATP, generated by oxidative phosphorylation
    • Cesar M de C, Wilson J E. Further studies on the coupling of mitochondrially bound hexokinase to intramitochondrially compartmented ATP, generated by oxidative phosphorylation. Arch Biochem Biophys. 350:1998;109-117.
    • (1998) Arch Biochem Biophys , vol.350 , pp. 109-117
    • Cesar, M.1    De, C.2    Wilson, J.E.3
  • 8
    • 0026494731 scopus 로고
    • Interaction of mitochondrially bound rat brain hexokinase with intramitochondrial compartments of ATP generated by oxidative phosphorylation and creatine kinase
    • BeltrandelRio H, Wilson J E. Interaction of mitochondrially bound rat brain hexokinase with intramitochondrial compartments of ATP generated by oxidative phosphorylation and creatine kinase. Arch Biochem Biophys. 299:1992;116-124.
    • (1992) Arch Biochem Biophys , vol.299 , pp. 116-124
    • Beltrandelrio, H.1    Wilson, J.E.2
  • 10
    • 0028034636 scopus 로고
    • In vitro complex formation between the octamer of mitochondrial creatine kinase and porin
    • Brdiczka D, Kaldis P, Wallimann T. In vitro complex formation between the octamer of mitochondrial creatine kinase and porin. J Biol Chem. 269:1994;27640-27644.
    • (1994) J Biol Chem , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 12
    • 0030050144 scopus 로고    scopus 로고
    • Identification of porin as a binding site for MAP2
    • Linden M, Karlsson G. Identification of porin as a binding site for MAP2. Biochem Biophys Res Commun. 218:1996;833-836.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 833-836
    • Linden, M.1    Karlsson, G.2
  • 13
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M, Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature. 399:1999;483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 15
    • 0032514888 scopus 로고    scopus 로고
    • A novel isoform of the mitochondrial outer membrane protein VDAC3 via alternative splicing of a 3-base exon
    • Sampson M J, Ross L, Decker W K, Craigen W J. A novel isoform of the mitochondrial outer membrane protein VDAC3 via alternative splicing of a 3-base exon. J Biol Chem. 273:1998;30482-30486.
    • (1998) J Biol Chem , vol.273 , pp. 30482-30486
    • Sampson, M.J.1    Ross, L.2    Decker, W.K.3    Craigen, W.J.4
  • 16
    • 0032581566 scopus 로고    scopus 로고
    • Characterization of rat porin isoforms: Cloning of a cardiac type-3 variant encoding an additional methionine at its putative N-terminal region
    • Anflous K, Blondel O, Bernard A, Khrestchatisky M, Ventura-Clapier R. Characterization of rat porin isoforms: Cloning of a cardiac type-3 variant encoding an additional methionine at its putative N-terminal region. Biochim Biophys Acta. 1399:1998;47-50.
    • (1998) Biochim Biophys Acta , vol.1399 , pp. 47-50
    • Anflous, K.1    Blondel, O.2    Bernard, A.3    Khrestchatisky, M.4    Ventura-Clapier, R.5
  • 17
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak M. The scanning model for translation: An update. J Cell Biol. 108:1989;229-241.
    • (1989) J Cell Biol , vol.108 , pp. 229-241
    • Kozak, M.1
  • 19
    • 0032852959 scopus 로고    scopus 로고
    • Each mammalian mitochondrial outer membrane porin is dispensible: Effects on cellular respiration
    • Wu S, Sampson M J, Decker W K, Craigen W J. Each mammalian mitochondrial outer membrane porin is dispensible: Effects on cellular respiration. Biochim Biophys Acta. 1452:1999;68-78.
    • (1999) Biochim Biophys Acta , vol.1452 , pp. 68-78
    • Wu, S.1    Sampson, M.J.2    Decker, W.K.3    Craigen, W.J.4
  • 21
    • 0032886205 scopus 로고    scopus 로고
    • Revised fine mapping of the human voltage-dependent anion channel loci by radiation hybrid analysis
    • Decker W K, Bowles K R, Schatte E C, Towbin J A, Craigen W J. Revised fine mapping of the human voltage-dependent anion channel loci by radiation hybrid analysis. Mamm Genome. 10:1999;1041-1042.
    • (1999) Mamm Genome , vol.10 , pp. 1041-1042
    • Decker, W.K.1    Bowles, K.R.2    Schatte, E.C.3    Towbin, J.A.4    Craigen, W.J.5
  • 22
    • 0030856487 scopus 로고    scopus 로고
    • The murine voltage-dependent anion channel gene family
    • Sampson M S, Lovell R S, Craigen W J. The murine voltage-dependent anion channel gene family. J Biol Chem. 272:1997;18966-18973.
    • (1997) J Biol Chem , vol.272 , pp. 18966-18973
    • Sampson, M.S.1    Lovell, R.S.2    Craigen, W.J.3
  • 25
    • 0024367080 scopus 로고
    • Differential exon usage involving an unusual splicing mechanism generates at least eight types of NCAM cDNA in mouse brain
    • Santoni M J, Barthels D, Vopper G, Boned A, Goridis C, Wille W. Differential exon usage involving an unusual splicing mechanism generates at least eight types of NCAM cDNA in mouse brain. EMBO J. 8:1989;385-392.
    • (1989) EMBO J , vol.8 , pp. 385-392
    • Santoni, M.J.1    Barthels, D.2    Vopper, G.3    Boned, A.4    Goridis, C.5    Wille, W.6
  • 26
    • 0032765963 scopus 로고    scopus 로고
    • Mouse VDAC isoforms expressed in yeast: Channel properties and their roles in mitochondrial outer membrane permeability
    • Xu X, Decker W, Sampson M J, Craigen W J, Colombini M. Mouse VDAC isoforms expressed in yeast: Channel properties and their roles in mitochondrial outer membrane permeability. J Membr Biol. 170:1999;89-102.
    • (1999) J Membr Biol , vol.170 , pp. 89-102
    • Xu, X.1    Decker, W.2    Sampson, M.J.3    Craigen, W.J.4    Colombini, M.5
  • 27
    • 0032981850 scopus 로고    scopus 로고
    • Identification of nuclear genes encoding mitochondrial proteins: Isolation of a collection of D. melanogaster cDNAs homologous to sequences in the Human Gene Index database
    • Caggese C, Ragone G, Perrini B, Moschetti R, De Pinto V, Caizzi R, Barsanti P. Identification of nuclear genes encoding mitochondrial proteins: Isolation of a collection of D. melanogaster cDNAs homologous to sequences in the Human Gene Index database. Mol Gen Genet. 261:1999;64-70.
    • (1999) Mol Gen Genet , vol.261 , pp. 64-70
    • Caggese, C.1    Ragone, G.2    Perrini, B.3    Moschetti, R.4    De Pinto, V.5    Caizzi, R.6    Barsanti, P.7
  • 29
    • 0023679092 scopus 로고
    • The carcinoembryonic antigen gene family: Structure, expression and evolution
    • Thompson J, Zimmermann W. The carcinoembryonic antigen gene family: Structure, expression and evolution. Tumour Biol. 9:1988;63-83.
    • (1988) Tumour Biol , vol.9 , pp. 63-83
    • Thompson, J.1    Zimmermann, W.2
  • 30
    • 0028343610 scopus 로고
    • Rates of transition and transversion in coding sequences since the human-rodent divergence
    • Collins D W, Jukes T H. Rates of transition and transversion in coding sequences since the human-rodent divergence. Genomics. 20:1994;386-396.
    • (1994) Genomics , vol.20 , pp. 386-396
    • Collins, D.W.1    Jukes, T.H.2
  • 31
    • 0026557719 scopus 로고
    • Mammalian phylogeny: Shaking the tree
    • Novacek M J. Mammalian phylogeny: Shaking the tree. Nature. 356:1992;121-125.
    • (1992) Nature , vol.356 , pp. 121-125
    • Novacek, M.J.1
  • 32
    • 0026039804 scopus 로고
    • Selection of splice sites in pre-mRNAs with short internal exons
    • Dominski Z, Kole R. Selection of splice sites in pre-mRNAs with short internal exons. Mol Cell Biol. 11:1991;6075-6083.
    • (1991) Mol Cell Biol , vol.11 , pp. 6075-6083
    • Dominski, Z.1    Kole, R.2
  • 33
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget S M. Exon recognition in vertebrate splicing. J Biol Chem. 270:1995;2411-2414.
    • (1995) J Biol Chem , vol.270 , pp. 2411-2414
    • Berget, S.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.