Tsc10p and FVT1: Topologically distinct short-chain reductases required for long-chain base synthesis in yeast and mammals

Journal of Lipid Research

Volumn 50, Issue 8, 2009, Pages 1630-1640

  Gupta, Sita D ^a   Gable, Kenneth ^a   Han, Gongshe ^a   Borovitskaya, Anna ^a   Selby, Luke ^a   Dunn, Teresa M ^a   Harmon, Jeffrey M ^a  

^a UNIFORMED SERVICES UNIVERSITY OF THE HEALTH SCIENCES   (United States)

Author keywords

3 Ketososphinganine reductase; Membrane protein topology; Sphingolipids

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LONG CHAIN FATTY ACID; MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEINASE; SHORT CHAIN FATTY ACID; SPHINGOLIPID; 3 KETODIHYDROSPHINGOSINE REDUCTASE; 3 KETOSPHINGANINE REDUCTASE; 3-KETODIHYDROSPHINGOSINE REDUCTASE; 3-KETOSPHINGANINE REDUCTASE; ALCOHOL DEHYDROGENASE; GLYCOSPHINGOLIPID; MUTANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL STRAIN HEK293; CHO CELL; CONTROLLED STUDY; CYTOPLASM; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME LOCALIZATION; ENZYME REGULATION; EUKARYOTE; FATTY ACID SYNTHESIS; GENE MUTATION; GENE SILENCING; HUMAN; HUMAN CELL; LIPOGENESIS; MAMMAL CELL; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN TARGETING; YEAST; AMINO ACID SEQUENCE; ANIMAL; BIOSYNTHESIS; CELL LINE; CHEMISTRY; CRICETULUS; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETIC TRANSFECTION; GENETICS; GLYCOSYLATION; HAMSTER; METABOLISM; MICROSOME; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN TRANSPORT; RNA INTERFERENCE; SACCHAROMYCES CEREVISIAE; ULTRASTRUCTURE;

ALCOHOL OXIDOREDUCTASES; AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CELL LINE; CHO CELLS; CRICETINAE; CRICETULUS; ENDOPLASMIC RETICULUM; GLYCOSPHINGOLIPIDS; GLYCOSYLATION; HUMANS; MEMBRANE PROTEINS; MICROSOMES; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; RNA INTERFERENCE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TRANSFECTION;

EID: 69449087658     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M800580-JLR200     Document Type: Article

References (29)

1. Merrill, A. H., Jr. 2002. De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. J. Biol. Chem. 277: 25843-25846.
2. Riezman, H. 2006. Organization and functions of sphingolipid biosynthesis in yeast. Biochem. Soc. Trans. 34: 367-369.
3. 2+-sensitive csg2Δ mutant. J. Biol. Chem. 273: 30688-30694.
4. Kihara, A., and Y. Igarashi. 2004. FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane. J. Biol. Chem. 279: 49243-49250.
5. Jackson, M. R., T. Nilsson, and P. A. Peterson. 1993. Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121: 317-333.
6. Krebs, S., I. Medugorac, S. Rother, K. Strasser, and M. Forster. 2007. A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy. Proc. Natl. Acad. Sci. USA. 104: 6746-6751.
7. Tanabe, T., N. Tanaka, K. Uchikawa, T. Kabashima, K. Ito, T. Nonaka, Y. Mitsui, M. Tsuru, and T. Yoshimoto. 1998. Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7α-hydroxysteroid dehydrogenase from Escherichia coli. J. Biochem. 124: 634-641.
8. Gilstring, C. F., and P. O. Ljungdahl. 2000. A method for determining the in vivo topology of yeast polytopic membrane proteins demonstrates that Gap1p fully integrates into the membrane independently of Shr3p. J. Biol. Chem. 275: 31488-31495.
9. Han, G., K. Gable, L. Yan, M. Natarajan, J. Krishnamurthy, S. D. Gupta, A. Borovitskaya, J. M. Harmon, and T. M. Dunn. 2004. The topology of the Lcb1p subunit of yeast serine palmitoyltransferase. J. Biol. Chem. 279: 53707-53716.
10. Paul, S., K. Gable, and T. M. Dunn. 2007. A six-membrane-spanning topology for yeast and Arabidopsis Tsc13p, the enoyl reductases of the microsomal fatty acid elongating system. J. Biol. Chem. 282: 19237-19246.
11. Sherman, F., G. R. Fink, and J. B. Hicks. 1986. Methods in Yeast Genetics: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
12. Kohlwein, S. D., S. Eder, C. S. Oh, C. E. Martin, K. Gable, D. Bacikova, and T. Dunn. 2001. Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol. Cell. Biol. 21: 109-125.
13. Gable, K., H. Slife, D. Bacikova, E. Monaghan, and T. M. Dunn. 2000. Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity. J. Biol. Chem. 275: 7597-7603.
14. Romano, J. D., and S. Michaelis. 2001. Topological and mutational analysis of Saccharomyces cerevisiae Ste14p, founding member of the isoprenylcysteine carboxyl methyltransferase family. Mol. Biol. Cell. 12: 1957-1971.
15. Feramisco, J. D., J. L. Goldstein, and M. S. Brown. 2004. Membrane topology of human insig-1, a protein regulator of lipid synthesis. J. Biol. Chem. 279: 8487-8496.
16. El-Kabbani, O., S. Ishikura, C. Darmanin, V. Carbone, R. P. Chung, N. Usami, and A. Hara. 2004. Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis. Proteins. 55: 724-732.
17. Filling, C., K. D. Berndt, J. Benach, S. Knapp, T. Prozorovski, E. Nordling, R. Ladenstein, H. Jornvall, and U. Oppermann. 2002. Critical residues for structure and catalysis in short-chain dehydrogenases/ reductases. J. Biol. Chem. 277: 25677-25684.
18. Ou, W. J., P. H. Cameron, D. Y. Thomas, and J. J. Bergeron. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature. 364: 771-776.
19. Hornemann, T., S. Richard, M. F. Rutti, Y. Wei, and A. von Eckardstein. 2006. Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase. J. Biol. Chem. 281: 37275-37281.
20. Hegde, R. S., and H. D. Bernstein. 2006. The surprising complexity of signal sequences. Trends Biochem. Sci. 31: 563-571.
21. Ghosh, D., M. Sawicki, V. Pletnev, M. Erman, S. Ohno, S. Nakajin, and W. L. Duax. 2001. Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases. J. Biol. Chem. 276: 18457-18463.
22. Oppermann, U., C. Filling, M. Hult, N. Shafqat, X. Wu, M. Lindh, J. Shafqat, E. Nordling, Y. Kallberg, B. Persson, et al. 2003. Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chem. Biol. Interact. 143-144: 247-253.
23. Tusnady, G. E., and I. Simon. 2001. The HMMTOP transmembrane topology prediction server. Bioinformatics. 17: 849-850.
24. Hofmann, K., and W. Stoffel. 1993. TMbase - a database of membrane spanning proteins segments. Biol. Chem. Hoppe Seyler. 374: 166.
25. von Heijne, G. 1992. Membrane protein structure prediction: hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225: 487-494.
26. Jones, D. T., W. R. Taylor, and J. M. Thornton. 1994. A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry. 33: 3038-3049.
27. Krogh, A., B. Larsson, G. von Heijne, and E. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305: 567-580.
28. Rost, B., G. Yachdav, and J. Liu. 2004. The PredictProtein server. Nucleic Acids Res. 32: W321-W326.
29. Arai, M., H. Mitsuke, M. Ikeda, J. X. Xia, T. Kikuchi, M. Satake, and T. Shimizu. 2004. ConPred II: a consensus prediction method for obtaining transmembrane topology models with high reliability. Nucleic Acids Res. 32: W390-W393.