메뉴 건너뛰기




Volumn 48, Issue 11, 2007, Pages 2354-2364

Topology of the yeast fatty acid transport protein Fat1p: Mechanistic implications for functional domains on the cytosolic surface of the plasma membrane

Author keywords

Fatty acid transport protein; Functional domains; Topology

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID; EPITOPE; FATTY ACID TRANSPORTER; FATTY ACID TRANSPORTER PROTEIN 1P; HEMAGGLUTININ; LONG CHAIN FATTY ACID COENZYME A LIGASE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 35848935833     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M700300-JLR200     Document Type: Article
Times cited : (25)

References (48)
  • 1
    • 0032854610 scopus 로고    scopus 로고
    • Membrane proteins implicated in long-chain fatty acid uptake by mammalian cells: CD36, FATP and FABPm
    • Abumrad, N., C. Coburn, and A. Ibrahimi. 1999. Membrane proteins implicated in long-chain fatty acid uptake by mammalian cells: CD36, FATP and FABPm. Biochim. Biophys. Acta. 1441: 4-13.
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 4-13
    • Abumrad, N.1    Coburn, C.2    Ibrahimi, A.3
  • 2
    • 0141566277 scopus 로고    scopus 로고
    • Transmembrane movement of exogenous long-chain fatty acids: Proteins, enzymes, and vectorial esterification
    • Black, P. N., and C. C. DiRusso. 2003. Transmembrane movement of exogenous long-chain fatty acids: proteins, enzymes, and vectorial esterification. Microbiol. Mol. Biol. Rev. 67: 454-472.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 454-472
    • Black, P.N.1    DiRusso, C.C.2
  • 3
    • 0033256884 scopus 로고    scopus 로고
    • Fatty acid transporters (FABPpm, FAT, FATP) in human muscle
    • Bonen, A., D. Miskovic, and B. Kiens. 1999. Fatty acid transporters (FABPpm, FAT, FATP) in human muscle. Can. J. Appl. Physiol. 24: 515-523.
    • (1999) Can. J. Appl. Physiol , vol.24 , pp. 515-523
    • Bonen, A.1    Miskovic, D.2    Kiens, B.3
  • 4
    • 0033769759 scopus 로고    scopus 로고
    • Cellular uptake of long-chain fatty acids: Role of membrane-associated fatty-acid-binding/transport proteins
    • Dutta-Roy, A. K. 2000. Cellular uptake of long-chain fatty acids: role of membrane-associated fatty-acid-binding/transport proteins. Cell. Mol. Life Sci. 57: 1360-1372.
    • (2000) Cell. Mol. Life Sci , vol.57 , pp. 1360-1372
    • Dutta-Roy, A.K.1
  • 5
    • 1242317654 scopus 로고    scopus 로고
    • A current review of fatty acid transport proteins (SLC27)
    • Stahl, A. 2004. A current review of fatty acid transport proteins (SLC27). Pflugers Arch. 447: 722-727.
    • (2004) Pflugers Arch , vol.447 , pp. 722-727
    • Stahl, A.1
  • 7
    • 17144370240 scopus 로고    scopus 로고
    • Fatty acid transport proteins and insulin resistance
    • Fisher, R. M., and K. Gertow. 2005. Fatty acid transport proteins and insulin resistance. Curr. Opin. Lipidol. 16: 173-178.
    • (2005) Curr. Opin. Lipidol , vol.16 , pp. 173-178
    • Fisher, R.M.1    Gertow, K.2
  • 11
    • 0037971325 scopus 로고    scopus 로고
    • Long-chain fatty acid uptake by skeletal muscle is impaired in homozygous, but not heterozygous, heart-type-FABP null mice
    • Luiken, J. J., D. P. Koonen, W. A. Coumans, M. M. Pelsers, B. Binas, A. Bonen, and J. F. Glatz. 2003. Long-chain fatty acid uptake by skeletal muscle is impaired in homozygous, but not heterozygous, heart-type-FABP null mice. Lipids. 38: 491-496.
    • (2003) Lipids , vol.38 , pp. 491-496
    • Luiken, J.J.1    Koonen, D.P.2    Coumans, W.A.3    Pelsers, M.M.4    Binas, B.5    Bonen, A.6    Glatz, J.F.7
  • 12
    • 0037627582 scopus 로고    scopus 로고
    • Cloning of wrinkle-free, a previously uncharacterized mouse mutation, reveals crucial roles for fatty acid transport protein 4 in skin and hair development
    • Moulson, C. L., D. R. Martin, J. J. Lugus, J. E. Schaffer, A. C. Lind, and J. H. Miner. 2003. Cloning of wrinkle-free, a previously uncharacterized mouse mutation, reveals crucial roles for fatty acid transport protein 4 in skin and hair development. Proc. Natl. Acad. Sci. USA. 100: 5274-5279.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5274-5279
    • Moulson, C.L.1    Martin, D.R.2    Lugus, J.J.3    Schaffer, J.E.4    Lind, A.C.5    Miner, J.H.6
  • 13
    • 34547117903 scopus 로고    scopus 로고
    • FATP4 is the principal very long-chain fatty acyl-CoA synthetase in skin fibroblasts
    • Jia, Z., C. L. Moulson, Z. Pei, J. H. Miner, and P. A. Watkins. 2007. FATP4 is the principal very long-chain fatty acyl-CoA synthetase in skin fibroblasts. J. Biol. Chem. 282: 20573-20583.
    • (2007) J. Biol. Chem , vol.282 , pp. 20573-20583
    • Jia, Z.1    Moulson, C.L.2    Pei, Z.3    Miner, J.H.4    Watkins, P.A.5
  • 15
    • 0032543378 scopus 로고    scopus 로고
    • A novel relative of the very-long-chain acyl-CoA synthetase and fatty acid transporter protein genes with a distinct expression pattern
    • Berger, J., C. Truppe, H. Neumann, and S. Forss-Petter. 1998. A novel relative of the very-long-chain acyl-CoA synthetase and fatty acid transporter protein genes with a distinct expression pattern. Biochem. Biophys. Res. Commun. 247: 255-260.
    • (1998) Biochem. Biophys. Res. Commun , vol.247 , pp. 255-260
    • Berger, J.1    Truppe, C.2    Neumann, H.3    Forss-Petter, S.4
  • 17
    • 0035168901 scopus 로고    scopus 로고
    • A new concept of cellular uptake and intracellular trafficking of long-chain fatty acids
    • Stremmel, W., L. Pohl, A. Ring, and T. Herrmann. 2001. A new concept of cellular uptake and intracellular trafficking of long-chain fatty acids. Lipids. 36: 981-989.
    • (2001) Lipids , vol.36 , pp. 981-989
    • Stremmel, W.1    Pohl, L.2    Ring, A.3    Herrmann, T.4
  • 18
    • 0032788926 scopus 로고    scopus 로고
    • Human very long-chain acyl-CoA synthetase and two human homologs: Initial characterization and relationship to fatty acid transport protein
    • Watkins, P. A., J. Pevsner, and S. J. Steinberg. 1999. Human very long-chain acyl-CoA synthetase and two human homologs: initial characterization and relationship to fatty acid transport protein. Prostaglandins Leukot. Essent. Fatty Acids. 60: 323-328.
    • (1999) Prostaglandins Leukot. Essent. Fatty Acids , vol.60 , pp. 323-328
    • Watkins, P.A.1    Pevsner, J.2    Steinberg, S.J.3
  • 19
    • 0242384922 scopus 로고    scopus 로고
    • Characterization of the acyl-CoA synthetase activity of purified murine fatty acid transport protein 1
    • Hall, A. M., A. J. Smith, and D. A. Bernlohr. 2003. Characterization of the acyl-CoA synthetase activity of purified murine fatty acid transport protein 1. J. Biol. Chem. 278: 43008-43013.
    • (2003) J. Biol. Chem , vol.278 , pp. 43008-43013
    • Hall, A.M.1    Smith, A.J.2    Bernlohr, D.A.3
  • 20
    • 15744364393 scopus 로고    scopus 로고
    • Enzymatic properties of purified murine fatty acid transport protein 4 and analysis of acyl-CoA synthetase activities in tissues from FATP4 null mice
    • Hall, A. M., B. M. Wiczer, T. Herrmann, W. Stremmel, and D. A. Bernlohr. 2005. Enzymatic properties of purified murine fatty acid transport protein 4 and analysis of acyl-CoA synthetase activities in tissues from FATP4 null mice. J. Biol. Chem. 280: 11948-11954.
    • (2005) J. Biol. Chem , vol.280 , pp. 11948-11954
    • Hall, A.M.1    Wiczer, B.M.2    Herrmann, T.3    Stremmel, W.4    Bernlohr, D.A.5
  • 21
    • 0033960276 scopus 로고    scopus 로고
    • Long-chain acyl-CoA-dependent regulation of gene expression in bacteria, yeast and mammals
    • Black, P. N., N. J. Faergeman, and C. C. DiRusso. 2000. Long-chain acyl-CoA-dependent regulation of gene expression in bacteria, yeast and mammals. J. Nutr. 130 (Suppl.): 305-309.
    • (2000) J. Nutr , vol.130 , Issue.SUPPL. , pp. 305-309
    • Black, P.N.1    Faergeman, N.J.2    DiRusso, C.C.3
  • 22
    • 0032911908 scopus 로고    scopus 로고
    • Long-chain fatty acid transport in bacteria and yeast. Paradigms for defining the mechanism underlying this protein-mediated process
    • DiRusso, C. C., and P. N. Black. 1999. Long-chain fatty acid transport in bacteria and yeast. Paradigms for defining the mechanism underlying this protein-mediated process. Mol. Cell. Biochem. 192: 41-52.
    • (1999) Mol. Cell. Biochem , vol.192 , pp. 41-52
    • DiRusso, C.C.1    Black, P.N.2
  • 23
    • 20444484799 scopus 로고    scopus 로고
    • Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast
    • DiRusso, C. C., H. Li, D. Darwis, P. A. Watkins, J. Berger, and P. N. Black. 2005. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J. Biol. Chem. 280: 16829-16837.
    • (2005) J. Biol. Chem , vol.280 , pp. 16829-16837
    • DiRusso, C.C.1    Li, H.2    Darwis, D.3    Watkins, P.A.4    Berger, J.5    Black, P.N.6
  • 24
    • 0035813196 scopus 로고    scopus 로고
    • The acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular utilization
    • Faergeman, N. J., P. N. Black, X. D. Zhao, J. Knudsen, and C. C. DiRusso. 2001. The acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular utilization. J. Biol. Chem. 276: 37051-37059.
    • (2001) J. Biol. Chem , vol.276 , pp. 37051-37059
    • Faergeman, N.J.1    Black, P.N.2    Zhao, X.D.3    Knudsen, J.4    DiRusso, C.C.5
  • 25
    • 0030889638 scopus 로고    scopus 로고
    • Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids
    • Faergeman, N. J., C. C. DiRusso, A. Elberger, J. Knudsen, and P. N. Black. 1997. Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids. J. Biol. Chem. 272: 8531-8538.
    • (1997) J. Biol. Chem , vol.272 , pp. 8531-8538
    • Faergeman, N.J.1    DiRusso, C.C.2    Elberger, A.3    Knudsen, J.4    Black, P.N.5
  • 26
    • 0037163035 scopus 로고    scopus 로고
    • Fatty acid transport in Saccharomyces cerevisiae. Directed mutagenesis of FAT1 distinguishes the biochemical activities associated with Fat1p
    • Zou, Z., C. C. DiRusso, V. Ctrnacta, and P. N. Black. 2002. Fatty acid transport in Saccharomyces cerevisiae. Directed mutagenesis of FAT1 distinguishes the biochemical activities associated with Fat1p. J. Biol. Chem. 277: 31062-31071.
    • (2002) J. Biol. Chem , vol.277 , pp. 31062-31071
    • Zou, Z.1    DiRusso, C.C.2    Ctrnacta, V.3    Black, P.N.4
  • 27
    • 0037507257 scopus 로고    scopus 로고
    • Vectorial acylation in Saccharomyces cerevisiae. Fat1p and fatty acyl-CoA synthetase are interacting components of a fatty acid import complex
    • Zou, Z., F. Tong, N. J. Faergeman, C. Borsting, P. N. Black, and C. C. DiRusso. 2003. Vectorial acylation in Saccharomyces cerevisiae. Fat1p and fatty acyl-CoA synthetase are interacting components of a fatty acid import complex. J. Biol. Chem. 278: 16414-16422.
    • (2003) J. Biol. Chem , vol.278 , pp. 16414-16422
    • Zou, Z.1    Tong, F.2    Faergeman, N.J.3    Borsting, C.4    Black, P.N.5    DiRusso, C.C.6
  • 28
    • 33644746164 scopus 로고    scopus 로고
    • Fatty acid transport protein 1 and long-chain acyl coenzyme A synthetase 1 interact in adipocytes
    • Richards, M. R., J. D. Harp, D. S. Ory, and J. E. Schaffer. 2006. Fatty acid transport protein 1 and long-chain acyl coenzyme A synthetase 1 interact in adipocytes. J. Lipid Res. 47: 665-672.
    • (2006) J. Lipid Res , vol.47 , pp. 665-672
    • Richards, M.R.1    Harp, J.D.2    Ory, D.S.3    Schaffer, J.E.4
  • 29
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SSDNA/PEG procedure
    • Gietz, R. D., R. H. Schiestl, A. R. Willems, and R. A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SSDNA/PEG procedure. Yeast. 11: 355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 30
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 31
    • 0000207681 scopus 로고
    • TMbase - a database of membrane spanning protein segments
    • Hofmann, K., and W. Stoffel. 1993. TMbase - a database of membrane spanning protein segments. Biol. Chem. Hoppe Seyler. 374: 166.
    • (1993) Biol. Chem. Hoppe Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 32
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., K. Bryson, and D. T. Jones. 2000. The PSIPRED protein structure prediction server. Bioinformatics. 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 33
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., J. Kopp, N. Guex, and M. C. Peitsch. 2003. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31: 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 34
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., N. P. Franks, and P. Brick. 1996. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure. 4: 287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 35
    • 1042276711 scopus 로고    scopus 로고
    • Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP
    • Jogl, G., and L. Tong. 2004. Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP. Biochemistry. 43: 1425-1431.
    • (2004) Biochemistry , vol.43 , pp. 1425-1431
    • Jogl, G.1    Tong, L.2
  • 37
    • 0029009125 scopus 로고
    • Isolation and biochemical characterization of organelles from the yeast
    • Zinser, E., and G. Daum. 1995. Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae. Yeast. 11: 493-536.
    • (1995) Saccharomyces cerevisiae. Yeast , vol.11 , pp. 493-536
    • Zinser, E.1    Daum, G.2
  • 38
    • 9944241271 scopus 로고    scopus 로고
    • A live-cell high-throughput screening assay for identification of fatty acid uptake inhibitors
    • Li, H., P. N. Black, and C. C. DiRusso. 2005. A live-cell high-throughput screening assay for identification of fatty acid uptake inhibitors. Anal. Biochem. 336: 11-19.
    • (2005) Anal. Biochem , vol.336 , pp. 11-19
    • Li, H.1    Black, P.N.2    DiRusso, C.C.3
  • 40
    • 0038801311 scopus 로고    scopus 로고
    • A common polymorphism in the fatty acid transport protein-1 gene associated with elevated post-prandial lipaemia and alterations in LDL particle size distribution
    • Gertow, K., C. Skoglund-Andersson, P. Eriksson, S. Boquist, K. Orth-Gomer, K. Schenck-Gustafsson, A. Hamsten, and R. M. Fisher. 2003. A common polymorphism in the fatty acid transport protein-1 gene associated with elevated post-prandial lipaemia and alterations in LDL particle size distribution. Atherosclerosis. 167: 265-273.
    • (2003) Atherosclerosis , vol.167 , pp. 265-273
    • Gertow, K.1    Skoglund-Andersson, C.2    Eriksson, P.3    Boquist, S.4    Orth-Gomer, K.5    Schenck-Gustafsson, K.6    Hamsten, A.7    Fisher, R.M.8
  • 41
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley, L. A., R. M. MacCallum, and M. J. Sternberg. 2000. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299: 499-520.
    • (2000) J. Mol. Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 42
    • 0034624015 scopus 로고    scopus 로고
    • Affinity labeling fatty acyl-CoA synthetase with 9-p-azidophenoxy nonanoic acid and the identification of the fatty acid-binding site
    • Black, P. N., C. C. DiRusso, D. Sherin, R. MacColl, J. Knudsen, and J. D. Weimar. 2000. Affinity labeling fatty acyl-CoA synthetase with 9-p-azidophenoxy nonanoic acid and the identification of the fatty acid-binding site. J. Biol. Chem. 275: 38547-38553.
    • (2000) J. Biol. Chem , vol.275 , pp. 38547-38553
    • Black, P.N.1    DiRusso, C.C.2    Sherin, D.3    MacColl, R.4    Knudsen, J.5    Weimar, J.D.6
  • 43
    • 0032693609 scopus 로고    scopus 로고
    • Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae
    • Athenstaedt, K., D. Zweytick, A. Jandrositz, S. D. Kohlwein, and G. Daum. 1999. Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J. Bacteriol. 181: 6441-6448.
    • (1999) J. Bacteriol , vol.181 , pp. 6441-6448
    • Athenstaedt, K.1    Zweytick, D.2    Jandrositz, A.3    Kohlwein, S.D.4    Daum, G.5
  • 44
    • 0014466104 scopus 로고
    • Fatty acid degradation in Escherichia coli. An inducible acyl-CoA synthetase, the mapping of old-mutations, and the isolation of regulatory mutants
    • Overath, P., G. Pauli, and H. U. Schairer. 1969. Fatty acid degradation in Escherichia coli. An inducible acyl-CoA synthetase, the mapping of old-mutations, and the isolation of regulatory mutants. Eur. J. Biochem. 7: 559-574.
    • (1969) Eur. J. Biochem , vol.7 , pp. 559-574
    • Overath, P.1    Pauli, G.2    Schairer, H.U.3
  • 45
    • 9644302482 scopus 로고    scopus 로고
    • Bacterial long chain fatty acid transport: Gateway to a fatty acid-responsive signaling system
    • DiRusso, C. C., and P. N. Black. 2004. Bacterial long chain fatty acid transport: gateway to a fatty acid-responsive signaling system. J. Biol. Chem. 279: 49563-49566.
    • (2004) J. Biol. Chem , vol.279 , pp. 49563-49566
    • DiRusso, C.C.1    Black, P.N.2
  • 46
    • 33947316606 scopus 로고    scopus 로고
    • Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation
    • Black, P. N., and C. C. DiRusso. 2007. Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation. Biochim. Biophys. Acta. 1771: 286-298.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 286-298
    • Black, P.N.1    DiRusso, C.C.2
  • 47
    • 33746625148 scopus 로고    scopus 로고
    • Protein-mediated fatty acid uptake: Novel insights from in vivo models
    • Doege, H., and A. Stahl. 2006. Protein-mediated fatty acid uptake: novel insights from in vivo models. Physiology (Bethesda). 21: 259-268.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 259-268
    • Doege, H.1    Stahl, A.2
  • 48
    • 0035813201 scopus 로고    scopus 로고
    • Membrane topology of the murine fatty acid transport protein 1
    • Lewis, S. E., L. L. Listenberger, D. S. Ory, and J. E. Schaffer. 2001. Membrane topology of the murine fatty acid transport protein 1. J. Biol. Chem. 276: 37042-37050.
    • (2001) J. Biol. Chem , vol.276 , pp. 37042-37050
    • Lewis, S.E.1    Listenberger, L.L.2    Ory, D.S.3    Schaffer, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.