CERT-mediated trafficking of ceramide

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1791, Issue 7, 2009, Pages 684-691

  Hanada, Kentaro ^a   Kumagai, Keigo ^a   Tomishige, Nario ^a   Yamaji, Toshiyuki ^a  

^a NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

Author keywords

FFAT motif; Membrane contact site; PH domain; START domain

Indexed keywords

CARRIER PROTEIN; CERAMIDE; MEMBRANE PROTEIN; METHYL BETA CYCLODEXTRIN; PLECKSTRIN; PROTEIN CERT; PROTEIN VAP; SPHINGOMYELIN; STEROIDOGENIC ACUTE REGULATORY PROTEIN; UNCLASSIFIED DRUG;

BIOGENESIS; BIOSYNTHESIS; CELL MEMBRANE; CELL MIGRATION; CELL MUTANT; DOWN REGULATION; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; HUMAN; INTRACELLULAR TRANSPORT; LIPID TRANSPORT; LIPOGENESIS; MAMMAL CELL; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; REVIEW; TRANS GOLGI NETWORK; TRANSPORT VESICLE;

AMINO ACID SEQUENCE; ANIMALS; BIOLOGICAL TRANSPORT; CERAMIDES; ENDOPLASMIC RETICULUM; GOLGI APPARATUS; MOLECULAR SEQUENCE DATA; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN-SERINE-THREONINE KINASES;

MAMMALIA;

EID: 67649271093     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2009.01.006     Document Type: Review

References (111)

1. Hannun Y.A., and Obeid L.M. Principles of bioactive lipid signalling: lessons from sphingolipids. Nat. Rev., Mol. Cell Biol. 9 (2008) 139-150
2. Lemmon M.A. Membrane recognition by phospholipid-binding domains. Nat. Rev., Mol. Cell Biol. 9 (2008) 99-111
3. van Meer G., Voelker D.R., and Feigenson G.W. Membrane lipids: where they are and how they behave. Nat. Rev., Mol. Cell Biol. 9 (2008) 112-124
4. Lee M.C., Miller E.A., Goldberg J., Orci L., and Schekman R. Bi-directional protein transport between the ER and Golgi. Annu. Rev. Cell Dev. Biol. 20 (2004) 87-123
5. Watson P., and Stephens D.J. ER-to-Golgi transport: form and formation of vesicular and tubular carriers. Biochim. Biophys. Acta 1744 (2005) 304-315
6. Pagano R.E., Puri V., Dominguez M., and Marks D.L. Membrane traffic in sphingolipid storage diseases. Traffic 1 (2000) 807-815
7. Mayor S., and Pagano R.E. Pathways of clathrin-independent endocytosis. Nat. Rev., Mol. Cell Biol. 8 (2007) 603-612
8. Soccio R.E., and Breslow J.L. Intracellular cholesterol transport. Arterioscler. Thromb. Vasc. Biol. 24 (2004) 1150-1160
9. Ikonen E. Cellular cholesterol trafficking and compartmentalization. Nat. Rev., Mol. Cell Biol. 9 (2008) 125-138
10. Holthuis J.C., and Levine T.P. Lipid traffic: floppy drives and a superhighway. Nat. Rev., Mol. Cell Biol. 6 (2005) 209-220
11. Vance J.E. Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum. J. Biol. Chem. 266 (1991) 89-97
12. Voelker D.R. New perspectives on the regulation of intermembrane glycerophospholipid traffic. J. Lipid Res. 44 (2003) 441-449
13. Kaplan M.R., and Simoni R.D. Transport of cholesterol from the endoplasmic reticulum to the plasma membrane. J. Cell Biol. 101 (1985) 446-453
14. Maxfield F.R., and Wustner D. Intracellular cholesterol transport. J. Clin. Invest. 110 (2002) 891-898
15. Hanada K. Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide. Mol. Cell. Biochem. 286 (2006) 23-31
16. Hanada K., Kumagai K., Tomishige N., and Kawano M. CERT and intracellular trafficking of ceramide. Biochim. Biophys. Acta 1771 (2007) 644-653
17. Merrill Jr. A.H. De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. J. Biol. Chem. 277 (2002) 25843-25846
18. Hanada K. Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim. Biophys. Acta 1632 (2003) 16-30
19. 2+-sensitive csg2Delta mutant. J. Biol. Chem. 273 (1998) 30688-30694
20. Kihara A., and Igarashi Y. 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 (2004) 49243-49250
21. Guillas I., Kirchman P.A., Chuard R., Pfefferli M., Jiang J.C., Jazwinski S.M., and Conzelmann A. C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p. EMBO J. 20 (2001) 2655-2665
22. Schorling S., Vallee B., Barz W.P., Riezman H., and Oesterhelt D. Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisiae. Mol. Biol. Cell 12 (2001) 3417-3427
23. Pewzner-Jung Y., Ben-Dor S., and Futerman A.H. When do Lasses (longevity assurance genes) become CerS (ceramide synthases)?: insights into the regulation of ceramide synthesis. J. Biol. Chem. 281 (2006) 25001-25005
24. Ternes P., Franke S., Zahringer U., Sperling P., and Heinz E. Identification and characterization of a sphingolipid delta 4-desaturase family. J. Biol. Chem. 277 (2002) 25512-25518
25. Mandon E.C., Ehses I., Rother J., van Echten G., and Sandhoff K. Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver. J. Biol. Chem. 267 (1992) 11144-11148
26. Huitema K., van den Dikkenberg J., Brouwers J.F., and Holthuis J.C. Identification of a family of animal sphingomyelin synthases. EMBO J. 23 (2004) 33-44
27. Yamaoka S., Miyaji M., Kitano T., Umehara H., and Okazaki T. Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J. Biol. Chem. 279 (2004) 18688-18693
28. Tafesse F.G., Huitema K., Hermansson M., van der Poel S., van den Dikkenberg J., Uphoff A., Somerharju P., and Holthuis J.C. Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J. Biol. Chem. 282 (2007) 17537-17547
29. Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P.J., and Hirabayashi Y. Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 4638-4663
30. Futerman A.H., and Pagano R.E. Determination of the intracellular sites and topology of glucosylceramide synthesis in rat liver. Biochem. J. 280 (1991) 295-302
31. Jeckel D., Karrenbauer A., Burger K.N.J., van Meer G., and Wieland F. Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions. J. Cell Biol. 117 (1992) 259-267
32. Ardail D., Popa I., Bodennec J., Louisot P., Schmitt D., and Portoukalian J. The mitochondria-associated endoplasmic-reticulum subcompartment (MAM fraction) of rat liver contains highly active sphingolipid-specific glycosyltransferases. Biochem. J. 371 (2003) 1013-1019
33. Kohyama-Koganeya A., Sasamura T., Oshima E., Suzuki E., Nishihara S., Ueda R., and Hirabayashi Y. Drosophila glucosylceramide synthase: a negative regulator of cell death mediated by proapoptotic factors. J. Biol. Chem. 279 (2004) 35995-36002
34. Halter D., Neumann S., van Dijk S.M., Wolthoorn J., de Maziere A.M., Vieira O.V., Mattjus P., Klumperman J., van Meer G., and Sprong H. Pre- and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis. J. Cell Biol. 179 (2007) 101-115
35. D'Angelo G., Polishchuk E., Di Tullio G., Santoro M., Di Campli A., Godi A., West G., Bielawski J., Chuang C.C., van der Spoel A.C., Platt F.M., Hannun Y.A., Polishchuk R., Mattjus P., and De Matteis M.A. Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature 449 (2007) 62-67
36. Collins R.N., and Warren G. Sphingolipid transport in mitotic HeLa cells. J. Biol. Chem. 267 (1992) 24906-24911
37. Moreau P., Cassagne C., Keenan T.W., and Morre D.J. Ceramide excluded from cell-free vesicular lipid transfer from endoplasmic reticulum to Golgi apparatus. Evidence for lipid sorting. Biochim. Biophys. Acta 1146 (1993) 9-16
38. Kok J.W., Babia T., Klappe K., Egea G., and Hoekstra D. Ceramide transport from endoplasmic reticulum to Golgi apparatus is not vesicle-mediated. Biochem. J. 333 (1998) 779-786
39. Fukasawa M., Nishijima M., and Hanada K. Genetic evidence for ATP-dependent endoplasmic reticulum-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in Chinese hamster ovary cells. J. Cell Biol. 144 (1999) 673-685
40. Funakoshi T., Yasuda S., Fukasawa M., Nishijima M., and Hanada K. Reconstitution of ATP- and cytosol-dependent transport of de novo synthesized ceramide to the site of sphingomyelin synthesis in semi-intact cells. J. Biol. Chem. 275 (2000) 29938-29945
41. Hanada K., Kumagai K., Yasuda S., Miura Y., Kawano M., Fukasawa M., and Nishijima M. Molecular machinery for non-vesicular trafficking of ceramide. Nature 426 (2003) 803-809
42. Hanada K., Hara T., Fukasawa M., Yamaji A., Umeda M., and Nishijima M. Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase. J. Biol. Chem. 273 (1998) 33787-33794
43. Ohvo-Rekila H., Ramstedt B., Leppimaki P., and Slotte J.P. Cholesterol interactions with phospholipids in membranes. Prog. Lipid Res. 41 (2002) 66-97
44. Fukasawa M., Nishijima M., Itabe H., Takano T., and Hanada K. Reduction of sphingomyelin level without accumulation of ceramide in Chinese hamster ovary cells affects detergent-resistant membrane domains and enhances cellular cholesterol efflux to methyl-beta-cyclodextrin. J. Biol. Chem. 275 (2000) 34028-34034
45. Raya A., Revert F., Navarro S., and Saus J. Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human Goodpasture antigen. J. Biol. Chem. 274 (1999) 12642-12649
46. Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E., Vieites B., Granero F., Forteza J., and Saus J. Goodpasture antigen-binding protein, the kinase that phosphorylates the Goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis. J. Biol. Chem. 275 (2000) 40392-40399
47. Ponting C.P., and Aravind L. START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins. Trends Biochem. Sci. 24 (1999) 130-132
48. Lemmon M.A., and Ferguson K.M. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350 (2000) 1-18
49. De Matteis M., Godi A., and Corda D. Phosphoinositides and the Golgi complex. Curr. Opin. Cell Biol. 14 (2002) 434-447
50. Levine T.P., and Munro S. Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components. Curr. Biol. 12 (2002) 695-704
51. Wang Y.J., Wang J., Sun H.Q., Martinez M., Sun Y.X., Macia E., Kirchhausen T., Albanesi J.P., Roth M.G., and Yin H.L. Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. Cell 114 (2003) 299-310
52. Godi A., Di Campli A., Konstantakopoulos A., Di Tullio G., Alessi D.R., Kular G.S., Daniele T., Marra P., Lucocq J.M., and De Matteis M.A. FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat. Cell Biol. 6 (2004) 393-404
53. Dowler S., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P., and Alessi D.R. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 351 (2000) 19-31
54. Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B., Murray D., Emr S.D., and Lemmon M.A. Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains. Mol. Cell 13 (2004) 677-688
55. Munro S. Organelle identity and the organization of membrane traffic. Nat. Cell Biol. 6 (2004) 469-472
56. Christenson L.K., and Strauss III J.F. Steroidogenic acute regulatory protein (StAR) and the intramitochondrial translocation of cholesterol. Biochim. Biophys. Acta 1529 (2000) 175-187
57. Stocco D.M. StAR protein and the regulation of steroid hormone biosynthesis. Annu. Rev. Physiol. 63 (2001) 193-213
58. Miller W.L. Steroidogenic acute regulatory protein (StAR), a novel mitochondrial cholesterol transporter. Biochim. Biophys. Acta 1771 (2007) 663-676
59. Soccio R.E., and Breslow J.L. StAR-related lipid transfer (START) proteins: mediators of intracellular lipid metabolism. J. Biol. Chem. 278 (2003) 22183-22186
60. Alpy F., and Tomasetto C. Give lipids a START: the StAR-related lipid transfer (START) domain in mammals. J. Cell. Sci. 118 (2005) 2791-2801
61. Schrick K., Nguyen D., Karlowski W.M., and Mayer K.F. START lipid/sterol-binding domains are amplified in plants and are predominantly associated with homeodomain transcription factors. Genome Biol. 5 (2004) R41
62. Barros M.H., Johnson A., Gin P., Marbois B.N., Clarke C.F., and Tzagoloff A. The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration. J. Biol. Chem. 280 (2005) 42627-42635
63. Kallen C.B., Billheimer J.T., Summers S.A., Stayrook S.E., Lewis M., and Strauss III J.F. Steroidogenic acute regulatory protein (StAR) is a sterol transfer protein. J. Biol. Chem. 273 (1998) 26285-26288
64. Tsujishita Y., and Hurley J.H. Structure and lipid transport mechanism of a StAR-related domain. Nat. Struct. Biol. 7 (2000) 408-414
65. Wirtz K.W.A. Phospholipid transfer proteins. Ann. Rev. Biochem. 60 (1991) 73-99
66. Olayioye M.A., Vehring S., Muller P., Herrmann A., Schiller J., Thiele C., Lindeman G.J., Visvader J.E., and Pomorski T. StarD10, a START domain protein overexpressed in breast cancer, functions as a phospholipid transfer protein. J. Biol. Chem. 280 (2005) 27436-27442
67. Tabunoki H., Sugiyama H., Tanaka Y., Fujii H., Banno Y., Jouni Z.E., Kobayashi M., Sato R., Maekawa H., and Tsuchida K. Isolation, characterization, and cDNA sequence of a carotenoid binding protein from the silk gland of Bombyx mori larvae. J. Biol. Chem. 277 (2002) 32133-32140
68. Hatch G.M., Gu Y., Xu F.Y., Cizeau J., Neumann S., Park J.S., Loewen S., and Mowat M.R. StARD13(Dlc-2) RhoGap mediates ceramide activation of phosphatidylglycerolphosphate synthase and drug response in Chinese hamster ovary cells. Mol. Biol. Cell 19 (2008) 1083-1092
69. Simon Jr. C.G., Holloway P.W., and Gear A.R. Exchange of C(16)-ceramide between phospholipid vesicles. Biochemistry 38 (1999) 14676-14682
70. Kumagai K., Yasuda S., Okemoto K., Nishijima M., Kobayashi S., and Hanada K. CERT mediates intermembrane transfer of various molecular species of ceramides. J. Biol. Chem. 280 (2005) 6488-6495
71. Roderick S.L., Chan W.W., Agate D.S., Olsen L.R., Vetting M.W., Rajashankar K.R., and Cohen D.E. Structure of human phosphatidylcholine transfer protein in complex with its ligand. Nat. Struct. Biol. 9 (2002) 507-511
72. Romanowski M.J., Soccio R.E., Breslow J.L., and Burley S.K. Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 6949-6954
73. Kudo N., Kumagai K., Tomishige N., Yamaji T., Wakatsuki S., Nishijima M., Hanada K., and Kato R. Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 488-493
74. Nishimura Y., Hayashi M., Inada H., and Tanaka T. Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins. Biochem. Biophys. Res. Commun. 254 (1999) 21-26
75. Skehel P.A., Martin K.C., Kandel E.R., and Bartsch D. A VAMP-binding protein from Aplysia required for neurotransmitter release. Science 269 (1995) 1580-1583
76. Weir M.L., Klip A., and Trimble W.S. Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP. Biochem. J. 333 (1998) 247-251
77. Kawano M., Kumagai K., Nishijima M., and Hanada K. Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT. J. Biol. Chem. 281 (2006) 30279-30288
78. Soussan L., Burakov D., Daniels M.P., Toister-Achituv M., Porat A., Yarden Y., and Elazar Z. ERG30, a VAP-33-related protein, functions in protein transport mediated by COPI vesicles. J. Cell. Biol. 146 (1999) 301-311
79. Kaiser S.E., Brickner J.H., Reilein A.R., Fenn T.D., Walter P., and Brunger A.T. Structural basis of FFAT motif-mediated ER targeting. Structure 13 (2005) 1035-1045
80. Perry R.J., and Ridgway N.D. Oxysterol-binding protein and VAMP-associated protein are required for sterol-dependent activation of the ceramide transport protein. Mol. Biol. Cell 17 (2006) 2604-2616
81. Lev S., Ben Halevy D., Peretti D., and Dahan N. The VAP protein family: from cellular functions to motor neuron disease. Trends Cell Biol. 18 (2008) 282-290
82. Tsuda H., Han S.M., Yang Y., Tong C., Lin Y.Q., Mohan K., Haueter C., Zoghbi A., Harati Y., Kwan J., Miller M.A., and Bellen H.J. The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell 133 (2008) 963-977
83. Beckers C.J.M., Keller D.S., and Balch W.E. Semi-intact cells permeable to macromolecules: use in reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex. Cell 50 (1987) 523-534
84. Ladinsky M.S., Mastronarde D.N., McIntosh J.R., Howell K.E., and Staehelin L.A. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J. Cell Biol. 144 (1999) 1135-1149
85. Marsh B.J., Mastronarde D.N., Buttle K.F., Howell K.E., and McIntosh J.R. Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 2399-2406
86. Kumagai K., Kawano M., Shinkai-Ouchi F., Nishijima M., and Hanada K. Interorganelle trafficking of ceramide is regulated by phosphorylation-dependent cooperativity between the PH and START domains of CERT. J. Biol. Chem. 282 (2007) 17758-17766
87. Munro S. Cell biology: earthworms and lipid couriers. Nature 426 (2003) 775-776
88. Chandran S., and Machamer C.E. Acute perturbations in Golgi organization impact de novo sphingomyelin synthesis. Traffic 9 (2008) 1894-1904
89. Funato K., and Riezman H. Vesicular and nonvesicular transport of ceramide from ER to the Golgi apparatus in yeast. J. Cell Biol. 155 (2001) 949-959
90. Raychaudhuri S., Im Y.J., Hurley J.H., and Prinz W.A. Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides. J. Cell Biol. 173 (2006) 107-119
91. D'Angelo G., Vicinanza M., Di Campli A., and De Matteis M.A. The multiple roles of PtdIns(4)P - not just the precursor of PtdIns(4,5)P2. J. Cell. Sci. 121 (2008) 1955-1963
92. Toth B., Balla A., Ma H., Knight Z.A., Shokat K.M., and Balla T. Phosphatidylinositol 4-kinase IIIbeta regulates the transport of ceramide between the endoplasmic reticulum and Golgi. J. Biol. Chem. 281 (2006) 36369-36377
93. Lopez-Montero I., Rodriguez N., Cribier S., Pohl A., Velez M., and Devaux P.F. Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes. J. Biol. Chem. 280 (2005) 25811-25819
94. Fugmann T., Hausser A., Schoffler P., Schmid S., Pfizenmaier K., and Olayioye M.A. Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein. J. Cell Biol. 178 (2007) 15-22
95. Bard F., and Malhotra V. The formation of TGN-to-plasma-membrane transport carriers. Annu. Rev. Cell Dev. Biol. 22 (2006) 439-455
96. Godi A., Pertile P., Meyers R., Marra P., Di Tullio G., Iurisci C., Luini A., Corda D., and De Matteis M.A. ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex. Nat. Cell Biol. 1 (1999) 280-287
97. Hausser A., Storz P., Martens S., Link G., Toker A., and Pfizenmaier K. Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex. Nat. Cell Biol. 7 (2005) 880-886
98. Tomishige N., Kumagai K., Kusuda J., Nishijima M., and Hanada K. Casein kinase I 782 gamma 2 down-regulates trafficking of ceramide in the synthesis of sphingo- 783 myelin. Mol. Biol. Cell. 20 (2009) 348-357
99. Saito S., Matsui H., Kawano M., Kumagai K., Tomishige N., Hanada K., Echigo S., Tamura S., and Kobayashi T. Protein phosphatase 2Cepsilon is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes. J. Biol. Chem. 283 (2007) 6584-6593
100. Perry R.J., and Ridgway N.D. Molecular mechanisms and regulation of ceramide transport. Biochim. Biophys. Acta 1734 (2005) 220-234
101. Loewen C.J., Roy A., and Levine T.P. A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP. EMBO J. 22 (2003) 2025-2035
102. Peretti D., Dahan N., Shimoni E., Hirschberg K., and Lev S. Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport. Mol. Biol. Cell 19 (2008) 3871-3884
103. Rao R.P., Yuan C., Allegood J.C., Rawat S.S., Edwards M.B., Wang X., Merrill Jr. A.H., Acharya U., and Acharya J.K. Ceramide transfer protein function is essential for normal oxidative stress response and lifespan. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 11364-11369
104. Revert F., Ventura I., Martinez-Martinez P., Granero-Molto F., Revert-Ros F., Macias J., and Saus J. Goodpasture antigen-binding protein is a soluble exportable protein which interacts with type IV collagen: identification of novel membrane-bound isoforms. J. Biol. Chem. 283 (2008) 30246-30255
105. Revert F., Merino R., Monteagudo C., Macias J., Peydro A., Alcacer J., Muniesa P., Marquina R., Blanco M., Iglesias M., Revert-Ros F., Merino J., and Saus J. Increased Goodpasture antigen-binding protein expression induces type IV collagen disorganization and deposit of immunoglobulin A in glomerular basement membrane. Am. J. Pathol. 171 (2007) 1419-1430
106. Granero-Molto F., Sarmah S., O'Rear L., Spagnoli A., Abrahamson D., Saus J., Hudson B.G., and Knapik E.W. Goodpasture antigen-binding protein and its spliced variant, ceramide transfer protein, have different functions in the modulation of apoptosis during zebrafish development. J. Biol. Chem. 283 (2008) 20495-20504
107. Swanton C., Marani M., Pardo O., Warne P.H., Kelly G., Sahai E., Elustondo F., Chang J., Temple J., Ahmed A.A., Brenton J.D., Downward J., and Nicke B. Regulators of mitotic arrest and ceramide metabolism are determinants of sensitivity to paclitaxel and other chemotherapeutic drugs. Cancer Cell 11 (2007) 498-512
108. Yasuda S., Kitagawa H., Ueno M., Ishitani H., Fukasawa M., Nishijima M., Kobayashi S., and Hanada K. A novel inhibitor of ceramide trafficking from the endoplasmic reticulum to the site of sphingomyelin synthesis. J. Biol. Chem. 276 (2001) 43994-44002
109. Stiban J., Caputo L., and Colombini M. Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins. J. Lipid Res. 49 (2008) 625-634
110. Levine T. Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol. 14 (2004) 483-490
111. de Brito O.M., and Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456 (2008) 605-610