BioMed Research International

Copyright © 2013 Ashley E. Beattie et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

1. A. H. Futerman and Y. A. Hannun, “The complex life of simple sphingolipids,” EMBO Reports, vol. 5, no. 8, pp. 777–782, 2004. View at Publisher · View at Google Scholar · View at Scopus
2. H. Fyrst and J. D. Saba, “An update on sphingosine-1-phosphate and other sphingolipid mediators,” Nature Chemical Biology, vol. 6, no. 7, pp. 489–497, 2010. View at Publisher · View at Google Scholar · View at Scopus
3. A. H. Merrill Jr., “De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway,” Journal of Biological Chemistry, vol. 277, no. 29, pp. 25843–25846, 2002. View at Publisher · View at Google Scholar · View at Scopus
4. T. Kolter and K. Sandhoff, “Sphingolipid metabolism diseases,” Biochimica et Biophysica Acta, vol. 1758, no. 12, pp. 2057–2079, 2006. View at Publisher · View at Google Scholar · View at Scopus
5. G. van Echten-Deckert and J. Walter, “Sphingolipids: critical players in Alzheimer's disease,” Progress in Lipid Research, vol. 51, no. 4, pp. 378–393, 2012. View at Publisher · View at Google Scholar
6. J. Lowther, J. H. Naismith, T. M. Dunn, and D. J. Campopiano, “Structural, mechanistic and regulatory studies of serine palmitoyltransferase,” Biochemical Society Transactions, vol. 40, no. 3, pp. 547–554, 2012. View at Publisher · View at Google Scholar
7. B. A. Yard, L. G. Carter, K. A. Johnson et al., “The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis,” Journal of Molecular Biology, vol. 370, no. 5, pp. 870–886, 2007. View at Publisher · View at Google Scholar · View at Scopus
8. H. Ikushiro, H. Hayashi, and H. Kagamiyama, “A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain: purification, characterization, cloning, and overproduction,” Journal of Biological Chemistry, vol. 276, no. 21, pp. 18249–18256, 2001. View at Publisher · View at Google Scholar · View at Scopus
9. J. Lowther, G. Charmier, M. C. Raman, H. Ikushiro, H. Hayashi, and D. J. Campopiano, “Role of a conserved arginine residue during catalysis in serine palmitoyltransferase,” FEBS Letters, vol. 585, no. 12, pp. 1729–1734, 2011. View at Publisher · View at Google Scholar · View at Scopus
10. M. C. C. Raman, K. A. Johnson, B. A. Yard et al., “The external aldimine form of serine palmitoyltransferase: structural, kinetic and spectroscopic analysis of the wild-type enzyme and HSAN1 mutant mimics,” Journal of Biological Chemistry, vol. 284, no. 25, pp. 17328–17339, 2009. View at Publisher · View at Google Scholar · View at Scopus
11. Y. Shiraiwa, H. Ikushiro, and H. Hayashi, “Multifunctional role of His159 in the catalytic reaction of Serine palmitoyltransferase,” Journal of Biological Chemistry, vol. 284, no. 23, pp. 15487–15495, 2009. View at Publisher · View at Google Scholar · View at Scopus
12. R. Buede, C. Rinker-Schaffer, W. J. Pinto, R. L. Lester, and R. C. Dickson, “Cloning and characterization of LCB1, a Saccharomyces gene required for biosynthesis of the long-chain base component of sphingolipids,” Journal of Bacteriology, vol. 173, no. 14, pp. 4325–4332, 1991. View at Google Scholar · View at Scopus
13. M. M. Nagiec, J. A. Baltisberger, G. B. Wells, R. L. Lester, and R. C. Dickson, “The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 17, pp. 7899–7902, 1994. View at Publisher · View at Google Scholar · View at Scopus
14. C. Zhao, T. Beeler, and T. Dunn, “Suppressors of the Ca²⁺-sensitive yeast mutant (csg2) identify genes involved in sphingolipid biosynthesis. Cloning and characterization of SCS1, a gene required for serine palmitoyltransferase activity,” Journal of Biological Chemistry, vol. 269, no. 34, pp. 21480–21488, 1994. View at Google Scholar · View at Scopus
15. T. Hornemann, S. Richard, M. F. Rütti, Y. Wei, and A. von Eckardstein, “Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase,” Journal of Biological Chemistry, vol. 281, no. 49, pp. 37275–37281, 2006. View at Publisher · View at Google Scholar · View at Scopus
16. M. M. Nagiec, R. L. Lester, and R. C. Dickson, “Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase,” Gene, vol. 177, no. 1-2, pp. 237–241, 1996. View at Publisher · View at Google Scholar · View at Scopus
17. B. Weiss and W. Stoffel, “Human and murine serine-palmitoyl-CoA transferase—cloning, expression and characterization of the key enzyme in sphingolipid synthesis,” European Journal of Biochemistry, vol. 249, no. 1, pp. 239–247, 1997. View at Google Scholar · View at Scopus
18. G. Han, S. D. Gupta, K. Gable et al., “Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 20, pp. 8186–8191, 2009. View at Publisher · View at Google Scholar · View at Scopus
19. K. Hanada, T. Hara, and M. Nishijima, “Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques,” Journal of Biological Chemistry, vol. 275, no. 12, pp. 8409–8415, 2000. View at Publisher · View at Google Scholar · View at Scopus
20. S. Yasuda, M. Nishijima, and K. Hanada, “Localization, topology, and function of the LCB1 subunit of serine palmitoyltransferase in mammalian cells,” Journal of Biological Chemistry, vol. 278, no. 6, pp. 4176–4183, 2003. View at Publisher · View at Google Scholar · View at Scopus
21. T. Hornemann, Y. Wei, and A. von Eckardstein, “Is the mammalian serine palmitoyltransferase a high-molecular-mass complex?” Biochemical Journal, vol. 405, no. 1, pp. 157–164, 2007. View at Publisher · View at Google Scholar · View at Scopus
22. T. Hornemann, A. Penno, M. F. Rütti et al., “The SPTLC3 subunit of serine palmitoyltransferase generates short chain sphingoid bases,” Journal of Biological Chemistry, vol. 284, no. 39, pp. 26322–26330, 2009. View at Publisher · View at Google Scholar · View at Scopus
23. K. Gable, H. Slife, D. Bacikova, E. Monaghan, and T. M. Dunn, “Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity,” Journal of Biological Chemistry, vol. 275, no. 11, pp. 7597–7603, 2000. View at Publisher · View at Google Scholar · View at Scopus
24. D. K. Breslow, S. R. Collins, B. Bodenmiller et al., “Orm family proteins mediate sphingolipid homeostasis,” Nature, vol. 463, no. 7284, pp. 1048–1053, 2010. View at Publisher · View at Google Scholar · View at Scopus
25. S. Han, M. A. Lone, R. Schneiter, and A. Chang, “Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 13, pp. 5851–5856, 2010. View at Publisher · View at Google Scholar · View at Scopus
26. D. K. Breslow and J. S. Weissman, “Membranes in balance: mechanisms of sphingolipid homeostasis,” Molecular Cell, vol. 40, no. 2, pp. 267–279, 2010. View at Publisher · View at Google Scholar · View at Scopus
27. M. Liu, C. Huang, S. R. Polu, R. Schneiter, and A. Chang, “Regulation of sphingolipid synthesis through Orm1 and Orm2 in yeast,” Journal of Cell Science, vol. 125, part 10, pp. 2428–2435, 2012. View at Publisher · View at Google Scholar
28. F. M. Roelants, D. K. Breslow, A. Muir, J. S. Weissman, and J. Thorner, “Protein kinase Ypk1 phosphorylates regulatory proteins Orm1 and Orm2 to control sphingolipid homeostasis in Saccharomyces cerevisiae,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 48, pp. 19222–19227, 2011. View at Publisher · View at Google Scholar · View at Scopus
29. K. Bejaoui, C. Wu, M. D. Scheffler et al., “SPTLC1 is mutated in hereditary sensory neuropathy, type 1,” Nature Genetics, vol. 27, no. 3, pp. 261–262, 2001. View at Publisher · View at Google Scholar · View at Scopus
30. J. L. Dawkins, D. J. Hulme, S. B. Brahmbhatt, M. Auer-Grumbach, and G. A. Nicholson, “Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I,” Nature Genetics, vol. 27, no. 3, pp. 309–312, 2001. View at Publisher · View at Google Scholar · View at Scopus
31. K. Gable, S. D. Gupta, G. Han, S. Niranjanakumari, J. M. Harmon, and T. M. Dunn, “A disease-causing mutation in the active site of serine palmitoyltransferase causes catalytic promiscuity,” Journal of Biological Chemistry, vol. 285, no. 30, pp. 22846–22852, 2010. View at Publisher · View at Google Scholar · View at Scopus
32. A. Penno, M. M. Reilly, H. Houlden et al., “Hereditary sensory neuropathy type 1 is caused by the accumulation of two neurotoxic sphingolipids,” Journal of Biological Chemistry, vol. 285, no. 15, pp. 11178–11187, 2010. View at Publisher · View at Google Scholar · View at Scopus
33. A. Rotthier, A. Penno, B. Rautenstrauss et al., “Characterization of two mutations in the SPTLC1 subunit of serine palmitoyltransferase associated with hereditary sensory and autonomic neuropathy type I,” Human Mutation, vol. 32, no. 6, pp. E2211–E2225, 2011. View at Publisher · View at Google Scholar · View at Scopus
34. K. Bejaoui, Y. Uchida, S. Yasuda et al., “Hereditary sensory neuropathy type 1 mutations confer dominant negative effects on serine palmitoyltransferase, critical for sphingolipid synthesis,” Journal of Clinical Investigation, vol. 110, no. 9, pp. 1301–1308, 2002. View at Publisher · View at Google Scholar · View at Scopus
35. K. Gable, G. Han, E. Monaghan et al., “Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase,” Journal of Biological Chemistry, vol. 277, no. 12, pp. 10194–10200, 2002. View at Publisher · View at Google Scholar · View at Scopus
36. B. Rautenstrauss, B. Neitzel, C. Muench, J. Haas, E. Holinski-Feder, and A. Abicht, “Late onset hereditary sensory neuropathy type 1 (Hsn1) caused by a novel P.C133r missense mutation in Sptlc1,” Journal of the Peripheral Nervous System, vol. 14, pp. 124–125, 2009. View at Google Scholar
37. A. Rotthier, J. Baets, E. De Vriendt et al., “Genes for hereditary sensory and autonomic neuropathies: a genotype-phenotype correlation,” Brain, vol. 132, part 10, pp. 2699–2711, 2009. View at Publisher · View at Google Scholar · View at Scopus
38. M. Auer-Grumbach, H. Bode, T. R. Pieber et al., “Mutations at Ser331 in the HSN type I gene SPTLC1 are associated with a distinct syndromic phenotype,” European Journal of Medical Genetics, vol. 56, no. 5, pp. 266–269, 2013. View at Publisher · View at Google Scholar
39. A. Rotthier, M. Auer-Grumbach, K. Janssens et al., “Mutations in the SPTLC2 subunit of serine palmitoyltransferase cause hereditary sensory and autonomic neuropathy type I,” American Journal of Human Genetics, vol. 87, no. 4, pp. 513–522, 2010. View at Publisher · View at Google Scholar · View at Scopus
40. T. Hornemann, A. Penno, S. Richard et al., “A systematic comparison of all mutations in hereditary sensory neuropathy type I (HSAN I) reveals that the G387A mutation is not disease associated,” Neurogenetics, vol. 10, no. 2, pp. 135–143, 2009. View at Publisher · View at Google Scholar · View at Scopus
41. K. Verhoeven, K. Coen, E. De Vriendt et al., “SPTLC1 mutation in twin sisters with hereditary sensory neuropathy type I,” Neurology, vol. 62, no. 6, pp. 1001–1002, 2004. View at Google Scholar · View at Scopus
42. S. M. Murphy, D. Ernst, Y. Wei et al., “Hereditary sensory and autonomic neuropathy type 1 (HSANI) caused by a novel mutation in SPTLC2,” Neurology, vol. 80, no. 23, pp. 2106–2111, 2013. View at Google Scholar
43. H. Liu and J. H. Naismith, “An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol,” BMC Biotechnology, vol. 8, article 91, 2008. View at Publisher · View at Google Scholar · View at Scopus
44. J. M. Harmon, D. Bacikova, K. Gable et al., “Topological and functional characterization of the ssSPTs, small activating subunits of serine palmitoyltransferase,” Journal of Biological Chemistry, vol. 288, no. 14, pp. 10144–10153, 2013. View at Publisher · View at Google Scholar
45. H. Ikushiro, S. Fujii, Y. Shiraiwa, and H. Hayashi, “Acceleration of the substrate Cα deprotonation by an analogue of the second substrate palmitoyl-CoA in serine palmitoyltransferase,” Journal of Biological Chemistry, vol. 283, no. 12, pp. 7542–7553, 2008. View at Publisher · View at Google Scholar · View at Scopus
46. W. L. DeLano, The PyMol Molecular Graphics System, DeLano Scientific, San Carlos, Calif, USA, 2002.
47. A. Rotthier, J. Baets, V. Timmerman, and K. Janssens, “Mechanisms of disease in hereditary sensory and autonomic neuropathies,” Nature Reviews Neurology, vol. 8, no. 2, pp. 73–85, 2012. View at Publisher · View at Google Scholar · View at Scopus
48. G. A. Nicholson, J. L. Dawkins, I. P. Blair, M. Auer-Grumbach, S. B. Brahmbhatt, and D. J. Hulme, “Hereditary sensory neuropathy type I: haplotype analysis shows founders in southern England and Europe,” American Journal of Human Genetics, vol. 69, no. 3, pp. 655–659, 2001. View at Publisher · View at Google Scholar · View at Scopus
49. F. S. Eichler, T. Hornemann, A. McCampbell et al., “Overexpression of the wild-type SPT1 subunit lowers desoxysphingolipid levels and rescues the phenotype of HSAN1,” Journal of Neuroscience, vol. 29, no. 46, pp. 14646–14651, 2009. View at Publisher · View at Google Scholar · View at Scopus
50. K. Garofalo, A. Penno, B. P. Schmidt et al., “Oral L-serine supplementation reduces production of neurotoxic deoxysphingolipids in mice and humans with hereditary sensory autonomic neuropathy type 1,” Journal of Clinical Investigation, vol. 121, no. 12, pp. 4735–4745, 2011. View at Publisher · View at Google Scholar · View at Scopus