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Volumn 274, Issue 20, 2007, Pages 5298-5310

Switching of the homooligomeric ATP-binding cassette transport complex MDL1 from post-translational mitochondrial import to endoplasmic reticulum insertion

Author keywords

ABC transporter; ER targeting; Membrane protein trafficking transport ATPase; Mitochondrial import; Mitochondrial targeting sequence

Indexed keywords

ABC TRANSPORTER A1; ADENOSINE TRIPHOSPHATE; IMIDAZOLE;

EID: 34848855513     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06052.x     Document Type: Article
Times cited : (14)

References (54)
  • 2
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson AL Chen J (2004) ATP-binding cassette transporters in bacteria. Annu Rev Biochem 73, 241 268.
    • (2004) Annu Rev Biochem , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 3
    • 0036909285 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Schmitt L Tampé R (2002) Structure and mechanism of ABC transporters. Curr Opin Struct Biol 12, 754 760.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 754-760
    • Schmitt, L.1    Tampé, R.2
  • 4
    • 0035896360 scopus 로고    scopus 로고
    • Role of the ABC transporter Mdl1 in peptide export from mitochondria
    • Young L, Leonhard K, Tatsuta T, Trowsdale J Langer T (2001) Role of the ABC transporter Mdl1 in peptide export from mitochondria. Science 291, 2135 2138.
    • (2001) Science , vol.291 , pp. 2135-2138
    • Young, L.1    Leonhard, K.2    Tatsuta, T.3    Trowsdale, J.4    Langer, T.5
  • 5
    • 0038161214 scopus 로고    scopus 로고
    • MDL1 is a high copy suppressor of ATM1: Evidence for a role in resistance to oxidative stress
    • Chloupkova M, LeBard LS Koeller DM (2003) MDL1 is a high copy suppressor of ATM1: evidence for a role in resistance to oxidative stress. J Mol Biol 331, 155 165.
    • (2003) J Mol Biol , vol.331 , pp. 155-165
    • Chloupkova, M.1    Lebard, L.S.2    Koeller, D.M.3
  • 6
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill R Kispal G (2000) Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem Sci 25, 352 356.
    • (2000) Trends Biochem Sci , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 10
    • 0037009105 scopus 로고    scopus 로고
    • Protein import into and across the mitochondrial inner membrane: Role of the TIM23 and TIM22 translocons
    • Jensen RE Dunn CD (2002) Protein import into and across the mitochondrial inner membrane: role of the TIM23 and TIM22 translocons. Biochim Biophys Acta 1592, 25 34.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 25-34
    • Jensen, R.E.1    Dunn, C.D.2
  • 11
    • 0042386354 scopus 로고    scopus 로고
    • Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles
    • Endo T, Yamamoto H Esaki M (2003) Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. J Cell Sci 116, 3259 3267.
    • (2003) J Cell Sci , vol.116 , pp. 3259-3267
    • Endo, T.1    Yamamoto, H.2    Esaki, M.3
  • 12
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • Koehler CM (2004) New developments in mitochondrial assembly. Annu Rev Cell Dev Biol 20, 309 335.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 13
    • 2442555970 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria
    • Wiedemann N, Frazier AE Pfanner N (2004) The protein import machinery of mitochondria. J Biol Chem 279, 14473 14476.
    • (2004) J Biol Chem , vol.279 , pp. 14473-14476
    • Wiedemann, N.1    Frazier, A.E.2    Pfanner, N.3
  • 15
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W (1997) Protein import into mitochondria. Annu Rev Biochem 66, 863 917.
    • (1997) Annu Rev Biochem , vol.66 , pp. 863-917
    • Neupert, W.1
  • 16
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G Dobberstein B (1996) Common principles of protein translocation across membranes. Science 271, 1519 1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 17
    • 0025053384 scopus 로고
    • Cleavage-site motifs in mitochondrial targeting peptides
    • Gavel Y von Heijne G (1990) Cleavage-site motifs in mitochondrial targeting peptides. Protein Eng 4, 33 37.
    • (1990) Protein Eng , vol.4 , pp. 33-37
    • Gavel, Y.1    Von Heijne, G.2
  • 18
    • 0024688488 scopus 로고
    • Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: Leader peptides cleaved by two matrix proteases share a three-amino acid motif
    • Hendrick JP, Hodges PE Rosenberg LE (1989) Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc Natl Acad Sci USA 86, 4056 4060.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4056-4060
    • Hendrick, J.P.1    Hodges, P.E.2    Rosenberg, L.E.3
  • 19
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • Glick BS, Brandt A, Cunningham K, Muller S, Hallberg RL Schatz G (1992) Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell 69, 809 822.
    • (1992) Cell , vol.69 , pp. 809-822
    • Glick, B.S.1    Brandt, A.2    Cunningham, K.3    Muller, S.4    Hallberg, R.L.5    Schatz, G.6
  • 20
    • 0037009132 scopus 로고    scopus 로고
    • Insertion of proteins into the inner membrane of mitochondria: The role of the Oxa1 complex
    • Stuart R (2002) Insertion of proteins into the inner membrane of mitochondria: the role of the Oxa1 complex. Biochim Biophys Acta 1592, 79 87.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 79-87
    • Stuart, R.1
  • 22
    • 0030941531 scopus 로고    scopus 로고
    • Intracellular location, complex formation, and function of the transporter associated with antigen processing in yeast
    • Urlinger S, Kuchler K, Meyer TH, Uebel S Tampé R (1997) Intracellular location, complex formation, and function of the transporter associated with antigen processing in yeast. Eur J Biochem 245, 266 272.
    • (1997) Eur J Biochem , vol.245 , pp. 266-272
    • Urlinger, S.1    Kuchler, K.2    Meyer, T.H.3    Uebel, S.4    Tampé, R.5
  • 23
    • 21244454544 scopus 로고    scopus 로고
    • Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)
    • Wolters JC, Abele R Tampé R (2005) Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9). J Biol Chem 280, 23631 23636.
    • (2005) J Biol Chem , vol.280 , pp. 23631-23636
    • Wolters, J.C.1    Abele, R.2    Tampé, R.3
  • 24
    • 0029016564 scopus 로고
    • Yeast N-terminal amidase. a new enzyme and component of the N-end rule pathway
    • Baker RT Varshavsky A (1995) Yeast N-terminal amidase. A new enzyme and component of the N-end rule pathway. J Biol Chem 270, 12065 12074.
    • (1995) J Biol Chem , vol.270 , pp. 12065-12074
    • Baker, R.T.1    Varshavsky, A.2
  • 25
    • 0021731775 scopus 로고
    • Subunit IV of yeast cytochrome c oxidase: Cloning and nucleotide sequencing of the gene and partial amino acid sequencing of the mature protein
    • Maarse AC, Van Loon AP, Riezman H, Gregor I, Schatz G Grivell LA (1984) Subunit IV of yeast cytochrome c oxidase: cloning and nucleotide sequencing of the gene and partial amino acid sequencing of the mature protein. EMBO J 3, 2831 2837.
    • (1984) EMBO J , vol.3 , pp. 2831-2837
    • Maarse, A.C.1    Van Loon, A.P.2    Riezman, H.3    Gregor, I.4    Schatz, G.5    Grivell, L.A.6
  • 27
    • 0036291180 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes of PMP70, an ATP binding cassette transporter on rat liver peroxisomal membranes
    • Kashiwayama Y, Morita M, Kamijo K Imanaka T (2002) Nucleotide-induced conformational changes of PMP70, an ATP binding cassette transporter on rat liver peroxisomal membranes. Biochem Biophys Res Commun 291, 1245 1251.
    • (2002) Biochem Biophys Res Commun , vol.291 , pp. 1245-1251
    • Kashiwayama, Y.1    Morita, M.2    Kamijo, K.3    Imanaka, T.4
  • 28
    • 33947496630 scopus 로고    scopus 로고
    • Structural and functional fingerprint of the mitochondrial ATP-binding cassette transporter Mdl1 from Saccharomyces cerevisiae
    • Hofacker M, Gompf S, Zutz A, Presenti C, Haase W, van der Does C, Model K Tampé R (2007) Structural and functional fingerprint of the mitochondrial ATP-binding cassette transporter Mdl1 from Saccharomyces cerevisiae. J Biol Chem 282, 3951 3961.
    • (2007) J Biol Chem , vol.282 , pp. 3951-3961
    • Hofacker, M.1    Gompf, S.2    Zutz, A.3    Presenti, C.4    Haase, W.5    Van Der Does, C.6    Model, K.7    Tampé, R.8
  • 29
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch IL, Sankaran B, Bhagat S Senior AE (1995) Both P-glycoprotein nucleotide-binding sites are catalytically active. J Biol Chem 270, 26956 26961.
    • (1995) J Biol Chem , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 30
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch IL, Sankaran B, Weber J Senior AE (1995) P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J Biol Chem 270, 19383 19390.
    • (1995) J Biol Chem , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 31
    • 0035957431 scopus 로고    scopus 로고
    • Allosteric crosstalk between peptide-binding, transport, and ATP hydrolysis of the ABC transporter TAP
    • Gorbulev S, Abele R Tampé R (2001) Allosteric crosstalk between peptide-binding, transport, and ATP hydrolysis of the ABC transporter TAP. Proc Natl Acad Sci USA 98, 3732 3737.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3732-3737
    • Gorbulev, S.1    Abele, R.2    Tampé, R.3
  • 32
    • 0033740174 scopus 로고    scopus 로고
    • Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis
    • Detmers FJ, Lanfermeijer FC, Abele R, Jack RW, Tampé R, Konings WN Poolman B (2000) Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis. Proc Natl Acad Sci USA 97, 12487 12492.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12487-12492
    • Detmers, F.J.1    Lanfermeijer, F.C.2    Abele, R.3    Jack, R.W.4    Tampé, R.5    Konings, W.N.6    Poolman, B.7
  • 33
    • 3542996250 scopus 로고    scopus 로고
    • The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter
    • Doeven MK, Abele R, Tampé R Poolman B (2004) The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter. J Biol Chem 279, 32301 32307.
    • (2004) J Biol Chem , vol.279 , pp. 32301-32307
    • Doeven, M.K.1    Abele, R.2    Tampé, R.3    Poolman, B.4
  • 35
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith PC, Karpowich N, Millen L, Moody JE, Rosen J, Thomas PJ Hunt JF (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10, 139 149.
    • (2002) Mol Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 36
    • 0038711772 scopus 로고    scopus 로고
    • The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
    • Janas E, Hofacker M, Chen M, Gompf S, van der Does C Tampé R (2003) The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J Biol Chem 278, 26862 26869.
    • (2003) J Biol Chem , vol.278 , pp. 26862-26869
    • Janas, E.1    Hofacker, M.2    Chen, M.3    Gompf, S.4    Van Der Does, C.5    Tampé, R.6
  • 37
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J, Jenewein S, Jumpertz T, Holland IB Schmitt L (2005) H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J 24, 1901 1910.
    • (2005) EMBO J , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 38
    • 33646876880 scopus 로고    scopus 로고
    • Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds
    • Kuhnke G, Neumann K, Mühlenhoff U Lill R (2006) Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds. Mol Membr Biol 23, 173 184.
    • (2006) Mol Membr Biol , vol.23 , pp. 173-184
    • Kuhnke, G.1    Neumann, K.2    Mühlenhoff, U.3    Lill, R.4
  • 39
    • 16344387139 scopus 로고    scopus 로고
    • Switching the sorting mode of membrane proteins from cotranslational endoplasmic reticulum targeting to posttranslational mitochondrial import
    • Miyazaki E, Kida Y, Mihara K Sakaguchi M (2005) Switching the sorting mode of membrane proteins from cotranslational endoplasmic reticulum targeting to posttranslational mitochondrial import. Mol Biol Cell 16, 1788 1799.
    • (2005) Mol Biol Cell , vol.16 , pp. 1788-1799
    • Miyazaki, E.1    Kida, Y.2    Mihara, K.3    Sakaguchi, M.4
  • 40
    • 5644288507 scopus 로고    scopus 로고
    • Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)
    • Graf SA, Haigh SE, Corson ED Shirihai OS (2004) Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me). J Biol Chem 279, 42954 42963.
    • (2004) J Biol Chem , vol.279 , pp. 42954-42963
    • Graf, S.A.1    Haigh, S.E.2    Corson, E.D.3    Shirihai, O.S.4
  • 41
    • 0029148985 scopus 로고
    • Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries
    • Uebel S, Meyer TH, Kraas W, Kienle S, Jung G, Wiesmüller KH Tampé R (1995) Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries. J Biol Chem 270, 18512 18516.
    • (1995) J Biol Chem , vol.270 , pp. 18512-18516
    • Uebel, S.1    Meyer, T.H.2    Kraas, W.3    Kienle, S.4    Jung, G.5    Wiesmüller, K.H.6    Tampé, R.7
  • 43
    • 33846700429 scopus 로고    scopus 로고
    • Intracellular peptide transporters in human - Compartmentalization of the 'peptidome'
    • Herget M Tampé R (2007) Intracellular peptide transporters in human - compartmentalization of the 'peptidome'. Pflugers Arch 453, 591 600.
    • (2007) Pflugers Arch , vol.453 , pp. 591-600
    • Herget, M.1    Tampé, R.2
  • 44
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann CB, Davies A, Cost GJ, Caputo E, Li J, Hieter P Boeke JD (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115 132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 45
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman F (1991) Getting started with yeast. Methods Enzymol 194, 3 21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 46
    • 0042390981 scopus 로고    scopus 로고
    • Purification of cytochrome bc1 complex from yeast
    • In. Hunte, C., von Jagow, G. Schägger, H., eds), pp. Academic Press, San Diego, CA.
    • Palsdottir H Hunte C (2003) Purification of cytochrome bc1 complex from yeast. In Membrane Protein Purification and Crystallization: A Practical Guide (Hunte C, von Jagow G Schägger H, eds), pp. 191 203. Academic Press, San Diego, CA.
    • (2003) Membrane Protein Purification and Crystallization: A Practical Guide , pp. 191-203
    • Palsdottir, H.1    Hunte, C.2
  • 47
    • 0034672334 scopus 로고    scopus 로고
    • Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations
    • Meisinger C, Sommer T Pfanner N (2000) Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations. Anal Biochem 287, 339 342.
    • (2000) Anal Biochem , vol.287 , pp. 339-342
    • Meisinger, C.1    Sommer, T.2    Pfanner, N.3
  • 48
    • 0035911154 scopus 로고    scopus 로고
    • Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion
    • Fritz S, Rapaport D, Klanner E, Neupert W Westermann B (2001) Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion. J Cell Biol 152, 683 692.
    • (2001) J Cell Biol , vol.152 , pp. 683-692
    • Fritz, S.1    Rapaport, D.2    Klanner, E.3    Neupert, W.4    Westermann, B.5
  • 49
    • 0025984393 scopus 로고
    • Import of precursor proteins into yeast submitochondrial particles
    • Jascur T (1991) Import of precursor proteins into yeast submitochondrial particles. Methods Cell Biol 34, 359 368.
    • (1991) Methods Cell Biol , vol.34 , pp. 359-368
    • Jascur, T.1
  • 50
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolate protein complexes from mitochondria
    • Schägger H (2001) Blue-native gels to isolate protein complexes from mitochondria. Methods Cell Biol 65, 231 244.
    • (2001) Methods Cell Biol , vol.65 , pp. 231-244
    • Schägger, H.1
  • 51
    • 0029837129 scopus 로고    scopus 로고
    • SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm
    • van der Does C, den Blaauwen T, de Wit JG, Manting EH, Groot NA, Fekkes P Driessen AJ (1996) SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm. Mol Microbiol 22, 619 629.
    • (1996) Mol Microbiol , vol.22 , pp. 619-629
    • Van Der Does, C.1    Den Blaauwen, T.2    De Wit, J.G.3    Manting, E.H.4    Groot, N.A.5    Fekkes, P.6    Driessen, A.J.7
  • 52
    • 0037177811 scopus 로고    scopus 로고
    • Biochemical characterization of the human RAD51 protein. I. ATP hydrolysis
    • Tombline G Fishel R (2002) Biochemical characterization of the human RAD51 protein. I. ATP hydrolysis. J Biol Chem 277, 14417 14425.
    • (2002) J Biol Chem , vol.277 , pp. 14417-14425
    • Tombline, G.1    Fishel, R.2
  • 53
    • 0043032667 scopus 로고    scopus 로고
    • Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
    • Chen M, Abele R Tampé R (2003) Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing. J Biol Chem 278, 29686 29692.
    • (2003) J Biol Chem , vol.278 , pp. 29686-29692
    • Chen, M.1    Abele, R.2    Tampé, R.3
  • 54
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke JD, Trueheart J, Natsoulis G Fink GR (1987) 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol 154, 164 175.
    • (1987) Methods Enzymol , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4


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