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Volumn 6, Issue , 2016, Pages

Translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ABCD4 PROTEIN, HUMAN; LMBRD1 PROTEIN, HUMAN; NUCLEOCYTOPLASMIC TRANSPORT PROTEIN;

EID: 84979516867     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep30183     Document Type: Article
Times cited : (42)

References (35)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8, 67-113 (1992).
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCs: A phylogenetic and functional classification of ABC systems in living organisms
    • Dassa, E. & Bouige, P. The ABC of ABCs: a phylogenetic and functional classification of ABC systems in living organisms. Res Microbiol 152, 211-229 (2001).
    • (2001) Res Microbiol , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, P.2
  • 3
    • 65549121495 scopus 로고    scopus 로고
    • Human ATP-binding cassette (ABC) transporter family
    • Vasiliou, V., Vasiliou, K. & Nebert, D. W. Human ATP-binding cassette (ABC) transporter family. Hum Genomics 3, 281-290 (2009).
    • (2009) Hum Genomics , vol.3 , pp. 281-290
    • Vasiliou, V.1    Vasiliou, K.2    Nebert, D.W.3
  • 4
    • 0025255475 scopus 로고
    • The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily
    • Kamijo, K., Taketani, S., Yokota, S., Osumi, T. & Hashimoto, T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily. J Biol Chem 265, 4534-4540 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 4534-4540
    • Kamijo, K.1    Taketani, S.2    Yokota, S.3    Osumi, T.4    Hashimoto, T.5
  • 5
    • 0027532282 scopus 로고
    • Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters
    • Mosser, J. et al. Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters. Nature 361, 726-730 (1993).
    • (1993) Nature , vol.361 , pp. 726-730
    • Mosser, J.1
  • 6
    • 0030034602 scopus 로고    scopus 로고
    • A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern
    • Lombard-Platet, G., Savary, S., Sarde, C. O., Mandel, J. L. & Chimini, G. A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern. Proc Natl Acad Sci USA 93, 1265-1269 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1265-1269
    • Lombard-Platet, G.1    Savary, S.2    Sarde, C.O.3    Mandel, J.L.4    Chimini, G.5
  • 7
    • 0030776037 scopus 로고    scopus 로고
    • Identification of a fourth half ABC transporter in the human peroxisomal membrane
    • Shani, N., Jimenez-Sanchez, G., Steel, G., Dean, M. & Valle, D. Identification of a fourth half ABC transporter in the human peroxisomal membrane. Hum Mol Genet 6, 1925-1931 (1997).
    • (1997) Hum Mol Genet , vol.6 , pp. 1925-1931
    • Shani, N.1    Jimenez-Sanchez, G.2    Steel, G.3    Dean, M.4    Valle, D.5
  • 8
    • 84864052256 scopus 로고    scopus 로고
    • Peroxisomal ABC transporters: Structure, function and role in disease
    • Morita, M. & Imanaka, T. Peroxisomal ABC transporters: structure, function and role in disease. Biochim Biophys Acta 1822, 1387-1396 (2012).
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 1387-1396
    • Morita, M.1    Imanaka, T.2
  • 9
    • 79953142344 scopus 로고    scopus 로고
    • Substrate specificity overlap and interaction between adrenoleukodystrophy protein (ALDP/ABCD1) and adrenoleukodystrophy-related protein (ALDRP/ABCD2)
    • Genin, E. C. et al. Substrate specificity overlap and interaction between adrenoleukodystrophy protein (ALDP/ABCD1) and adrenoleukodystrophy-related protein (ALDRP/ABCD2). J Biol Chem 286, 8075-8084 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 8075-8084
    • Genin, E.C.1
  • 10
    • 78651253382 scopus 로고    scopus 로고
    • Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid beta-oxidation
    • van Roermund, C. W., Visser, W. F., Ijlst, L., Waterham, H. R. & Wanders, R. J. Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid beta-oxidation. Biochim Biophys Acta 1811, 148-152 (2011).
    • (2011) Biochim Biophys Acta , vol.1811 , pp. 148-152
    • Van Roermund, C.W.1    Visser, W.F.2    Ijlst, L.3    Waterham, H.R.4    Wanders, R.J.5
  • 11
    • 84896882251 scopus 로고    scopus 로고
    • A role for the human peroxisomal half-transporter ABCD3 in the oxidation of dicarboxylic acids
    • van Roermund, C. W., Ijlst, L., Wagemans, T., Wanders, R. J. & Waterham, H. R. A role for the human peroxisomal half-transporter ABCD3 in the oxidation of dicarboxylic acids. Biochim Biophys Acta 1841, 563-568 (2014).
    • (2014) Biochim Biophys Acta , vol.1841 , pp. 563-568
    • Van Roermund, C.W.1    Ijlst, L.2    Wagemans, T.3    Wanders, R.J.4    Waterham, H.R.5
  • 12
    • 57749175975 scopus 로고    scopus 로고
    • 70-kDa peroxisomal membrane protein related protein (P70R/ABCD4) localizes to endoplasmic reticulum not peroxisomes, and NH2-terminal hydrophobic property determines the subcellular localization of ABC subfamily D proteins
    • Kashiwayama, Y. et al. 70-kDa peroxisomal membrane protein related protein (P70R/ABCD4) localizes to endoplasmic reticulum not peroxisomes, and NH2-terminal hydrophobic property determines the subcellular localization of ABC subfamily D proteins. Exp Cell Res 315, 190-205 (2009).
    • (2009) Exp Cell Res , vol.315 , pp. 190-205
    • Kashiwayama, Y.1
  • 13
    • 84866937421 scopus 로고    scopus 로고
    • Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism
    • Coelho, D. et al. Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism. Nat Genet 44, 1152-1155 (2012).
    • (2012) Nat Genet , vol.44 , pp. 1152-1155
    • Coelho, D.1
  • 14
    • 41649092991 scopus 로고    scopus 로고
    • Gene identification for the cblD defect of vitamin B12 metabolism
    • Coelho, D. et al. Gene identification for the cblD defect of vitamin B12 metabolism. N Engl J Med 358, 1454-1464 (2008).
    • (2008) N Engl J Med , vol.358 , pp. 1454-1464
    • Coelho, D.1
  • 15
    • 59149091781 scopus 로고    scopus 로고
    • Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism
    • Rutsch, F. et al. Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism. Nat Genet 41, 234-239 (2009).
    • (2009) Nat Genet , vol.41 , pp. 234-239
    • Rutsch, F.1
  • 16
    • 0034234383 scopus 로고    scopus 로고
    • A novel candidate gene for mouse and human preaxial polydactyly with altered expression in limbs of Hemimelic extra-toes mutant mice
    • Clark, R. M., Marker, P. C. & Kingsley, D. M. A novel candidate gene for mouse and human preaxial polydactyly with altered expression in limbs of Hemimelic extra-toes mutant mice. Genomics 67, 19-27 (2000).
    • (2000) Genomics , vol.67 , pp. 19-27
    • Clark, R.M.1    Marker, P.C.2    Kingsley, D.M.3
  • 17
    • 0035827544 scopus 로고    scopus 로고
    • Molecular cloning of a novel lipocalin-1 interacting human cell membrane receptor using phage display
    • Wojnar, P., Lechner, M., Merschak, P. & Redl, B. Molecular cloning of a novel lipocalin-1 interacting human cell membrane receptor using phage display. J Biol Chem 276, 20206-20212 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 20206-20212
    • Wojnar, P.1    Lechner, M.2    Merschak, P.3    Redl, B.4
  • 18
    • 38349061551 scopus 로고    scopus 로고
    • Lipocalin-interacting-membrane-receptor (LIMR) mediates cellular internalization of beta-lactoglobulin
    • Fluckinger, M., Merschak, P., Hermann, M., Haertle, T. & Redl, B. Lipocalin-interacting-membrane-receptor (LIMR) mediates cellular internalization of beta-lactoglobulin. Biochim Biophys Acta 1778, 342-347 (2008).
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 342-347
    • Fluckinger, M.1    Merschak, P.2    Hermann, M.3    Haertle, T.4    Redl, B.5
  • 19
    • 84887500079 scopus 로고    scopus 로고
    • LMBD1 protein serves as a specific adaptor for insulin receptor internalization
    • Tseng, L. T., Lin, C. L., Tzen, K. Y., Chang, S. C. & Chang, M. F. LMBD1 protein serves as a specific adaptor for insulin receptor internalization. J Biol Chem 288, 32424-32432 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 32424-32432
    • Tseng, L.T.1    Lin, C.L.2    Tzen, K.Y.3    Chang, S.C.4    Chang, M.F.5
  • 20
    • 84919791507 scopus 로고    scopus 로고
    • Purification and interaction analyses of two human lysosomal vitamin B12 transporters: LMBD1 and ABCD4
    • Deme, J. C. et al. Purification and interaction analyses of two human lysosomal vitamin B12 transporters: LMBD1 and ABCD4. Mol Membr Biol 31, 250-261 (2014).
    • (2014) Mol Membr Biol , vol.31 , pp. 250-261
    • Deme, J.C.1
  • 21
    • 84896512558 scopus 로고    scopus 로고
    • Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog
    • Kodan, A. et al. Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Proc Natl Acad Sci USA 111, 4049-4054 (2014).
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 4049-4054
    • Kodan, A.1
  • 22
    • 77954565111 scopus 로고    scopus 로고
    • Insights into lysosomal cobalamin trafficking: Lessons learned from cblF disease
    • Gailus, S. et al. Insights into lysosomal cobalamin trafficking: lessons learned from cblF disease. J Mol Med (Berl) 88, 459-466 (2010).
    • (2010) J Mol Med (Berl) , vol.88 , pp. 459-466
    • Gailus, S.1
  • 23
    • 84876567971 scopus 로고    scopus 로고
    • RNA-programmed genome editing in human cells
    • Jinek, M. et al. RNA-programmed genome editing in human cells. eLife 2, e00471 (2013).
    • (2013) ELife , vol.2
    • Jinek, M.1
  • 24
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S. & Eliceiri, K. W. NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9, 671-675 (2012).
    • (2012) Nat Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 25
    • 84876315023 scopus 로고    scopus 로고
    • Hepatitis C virus replication is modulated by the interaction of nonstructural protein NS5B and fatty acid synthase
    • Huang, J. T. et al. Hepatitis C virus replication is modulated by the interaction of nonstructural protein NS5B and fatty acid synthase. J Virol 87, 4994-5004 (2013).
    • (2013) J Virol , vol.87 , pp. 4994-5004
    • Huang, J.T.1
  • 26
    • 0034725705 scopus 로고    scopus 로고
    • Characterization of ABCB9, an ATP binding cassette protein associated with lysosomes
    • Zhang, F. et al. Characterization of ABCB9, an ATP binding cassette protein associated with lysosomes. J Biol Chem 275, 23287-23294 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 23287-23294
    • Zhang, F.1
  • 27
    • 14944385370 scopus 로고    scopus 로고
    • A proteomic analysis of lysosomal integral membrane proteins reveals the diverse composition of the organelle
    • Bagshaw, R. D., Mahuran, D. J. & Callahan, J. W. A proteomic analysis of lysosomal integral membrane proteins reveals the diverse composition of the organelle. Mol Cell Proteomics 4, 133-143 (2005).
    • (2005) Mol Cell Proteomics , vol.4 , pp. 133-143
    • Bagshaw, R.D.1    Mahuran, D.J.2    Callahan, J.W.3
  • 28
    • 39349100294 scopus 로고    scopus 로고
    • Vesicular localization of the rat ATP-binding cassette half-transporter rAbcb6
    • Jalil, Y. A. et al. Vesicular localization of the rat ATP-binding cassette half-transporter rAbcb6. Am J Physiol Cell Physiol 294, C579-590 (2008).
    • (2008) Am J Physiol Cell Physiol , vol.294 , pp. C579-C590
    • Jalil, Y.A.1
  • 29
    • 77949521198 scopus 로고    scopus 로고
    • Tuning the cellular trafficking of the lysosomal peptide transporter TAPL by its N-terminal domain
    • Demirel, O., Bangert, I., Tampe, R. & Abele, R. Tuning the cellular trafficking of the lysosomal peptide transporter TAPL by its N-terminal domain. Traffic 11, 383-393 (2010).
    • (2010) Traffic , vol.11 , pp. 383-393
    • Demirel, O.1    Bangert, I.2    Tampe, R.3    Abele, R.4
  • 30
    • 84935897756 scopus 로고    scopus 로고
    • Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein
    • Kiss, K. et al. Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein. Biochem J 467, 127-139 (2015).
    • (2015) Biochem J , vol.467 , pp. 127-139
    • Kiss, K.1
  • 31
    • 28944442871 scopus 로고    scopus 로고
    • In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake
    • Borths, E. L., Poolman, B., Hvorup, R. N., Locher, K. P. & Rees, D. C. In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake. Biochemistry 44, 16301-16309 (2005).
    • (2005) Biochemistry , vol.44 , pp. 16301-16309
    • Borths, E.L.1    Poolman, B.2    Hvorup, R.N.3    Locher, K.P.4    Rees, D.C.5
  • 32
    • 77949904065 scopus 로고    scopus 로고
    • Identification of multidrug resistance protein 1 (MRP1/ABCC1) as a molecular gate for cellular export of cobalamin
    • Beedholm-Ebsen, R. et al. Identification of multidrug resistance protein 1 (MRP1/ABCC1) as a molecular gate for cellular export of cobalamin. Blood 115, 1632-1639 (2010).
    • (2010) Blood , vol.115 , pp. 1632-1639
    • Beedholm-Ebsen, R.1
  • 33
    • 84863304501 scopus 로고    scopus 로고
    • ABCA4 is an N-retinylidene-phosphatidylethanolamine and phosphatidylethanolamine importer
    • Quazi, F., Lenevich, S. & Molday, R. S. ABCA4 is an N-retinylidene-phosphatidylethanolamine and phosphatidylethanolamine importer. Nat Commun 3, 925 (2012).
    • (2012) Nat Commun , vol.3 , pp. 925
    • Quazi, F.1    Lenevich, S.2    Molday, R.S.3
  • 34
    • 84936952731 scopus 로고    scopus 로고
    • A Novel Double Mutation in the ABCD1 Gene in a Patient with X-linked Adrenoleukodystrophy: Analysis of the Stability and Function of the Mutant ABCD1 Protein
    • Morita, M. et al. A Novel Double Mutation in the ABCD1 Gene in a Patient with X-linked Adrenoleukodystrophy: Analysis of the Stability and Function of the Mutant ABCD1 Protein. JIMD Rep 10, 95-102 (2013).
    • (2013) JIMD Rep , vol.10 , pp. 95-102
    • Morita, M.1
  • 35
    • 84887010498 scopus 로고    scopus 로고
    • Genome engineering using the CRISPR-Cas9 system
    • Ran, F. A. et al. Genome engineering using the CRISPR-Cas9 system. Nat Protoc 8, 2281-2308 (2013).
    • (2013) Nat Protoc , vol.8 , pp. 2281-2308
    • Ran, F.A.1


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