Phospholipid metabolism and membrane dynamics

Current Opinion in Cell Biology

Volumn 8, Issue 4, 1996, Pages 534-541

  Alb Jr , James G ^a   Kearns, Melissa A ^a   Bankaitis, Vytas A ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PHOSPHATIDYLINOSITOL; PHOSPHOLIPID;

EUKARYOTE; NONHUMAN; PHOSPHOLIPID METABOLISM; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION; YEAST;

EUKARYOTA;

EID: 0030222106     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80032-9     Document Type: Article

References (46)

1. 1. Jackowski S: Coordination of membrane phospholipid synthesis with the cell cycle. J Biol Chem 1994, 269:3858-3867
2. 2. Cui Z, Houweling M, Vance DE: Suppression of rat hepatoma cell growth by expression of phosphatidylethanolamine N-methyltransferase-2. J Biol Chem 1994, 269:24531-24533.
3. 3. Houweling M, Cui Z, Vance DE: Expression of phosphatidylethanolamine N-methyltransferase-2 cannot compensate for an impaired CDP-choline pathway in mutant chinese hamster ovary cells. J Biol Chem 1995, 270:16277-16282. Using a mutant Chinese hamster ovary (CHO) cell line that has a temperature-sensitive CCTase, the authors ask whether PC synthesis via the PE-methylation pathway can satisfy the PC deficit which these mutant CHO cells suffer from as a result of impaired CDP-choline pathway activity at restrictive temperatures. The interesting result is that restoration of wild-type PC levels to these cells by PE methylation pathway activity cannot rescue the growth defect associated with CDP-choline pathway insufficiency. It is not known, however, if the PEMT2-driven rate of PC biosynthesis occurs with kinetics similar to those of PC biosynthesis via the CDP-choline pathway.
4. 4. Van Meer G: Lipid traffic in animal cells. Annu Rev Cell Biol 1989, 5:247-275.
5. 5. Pagano RE: Lipid traffic in eukaryotic cells: mechanisms for intracellular transport and organelle-specific enrichment of lipids. Curr Opin Cell Biol 1990, 2:652-663.
6. 6. Voelker DE: Intracellular lipid movement in eukaryotes. Microbiol Rev 1990, 55:543-560.
7. 7. Moreau P, Cassagne C: Phospholipid trafficking and membrane biogenesis. Biochim Biophys Acta 1994, 1197:257-290.
8. 8. Wirtz KWA: Phospholipid transfer proteins. Annu Rev Biochem 1991, 60:73-99.
9. 9. Bankaitis VA, Fry MR, Cartee RT, Kagiwada S: Phospholipid Transfer Proteins: Emerging Roles in Vesicle Trafficking, Signal Transduction, and Metabolic Regulation. Austin, Texas: RG Landes Co; 1996.
10. 10. Voelker DE: Disruption of phosphatidylserine translocation to the mitochondrion in baby hamster kidney cells. J Biol Chem 1985, 260:14671-14676.
11. 11. Voelker D: Reconstitution of phosphatidylserine import into rat liver mitochondria. J Biol Chem 1989, 264:8019-8025.
12. 12. Vance JE: Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and rat liver. J Biol Chem 1991, 266:89-97.
13. 13. Vance JE: Phospholipid synthesis in a membrane fraction associated with mitochondria. J Biol Chem 1990, 265:7248-7256.
14. 14. Trotter PJ, Pedretti J, Voelker DR: Phosphatidylserine decarboxylase from Saccharomyces cerevisiae: isolation of mutants, cloning of gene, and creation of a null allele. J Biol Chem 1993, 268:21416-21424.
15. 15. Clancy CJ, Chang SD, Dowhan W: Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from Saccharomyces cerevisiae. J Biol Chem 1995, 270:16277-16282. The authors detect the first non-mitochondrial PSD activity, thereby demonstrating that the milochondrial PSD is not the only such enzyme in cells. This finding raises the probability that back transfer of PE from the mitochondrion to the ER is not necessary for the supply of PE to other cellular compartments. See also [16•].
16. 16. Trotter PJ, Voelker DR: Identification of a non-mitochondrial phosphatidylserine decarboxylase activity (PSD2) in the yeast Saccharomyces cerevisiae. J Biol Chem 1995, 270:6062-6070. The authors detect a second non-mitochondrial PSD activity. See also annotation [15•].
17. 17. Trotter PJ, Pedretti J, Yates R, Voelker DR: Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae: isolation of mutants, cloning of gene, and creation of null allele. J Biol Chem 1995, 270:6071-6080. This paper describes the characterization of the non-mitochondrial PSD, and also demonstrates that this activity is responsible for the generation of bulk PE from PS when ethanolamine is absent from the growth medium of yeast cells.
18. 18. Rusinol AE, Cui Z, Chen MH, Vance JE: A unique mitochondrialassociated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-golgi secretory proteins including nascent lipoproteins. J Biol Chem 1995, 269:27494-27502. This paper describes the isolation and characterization of an MAM fraction that exhibits the properties of a pre-Golgi compartment.
19. 19. Shiao YJ, Lupo G, Vance JE: Evidence that phosphatidylserine is imported into mitochondria via a mitochondrial-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine. J Biol Chem 1995, 270:11190-11198. The authors demonstrate that pulse-radiolabeled PS specifically accumulates in the MAM under conditions in which PS transport to the mitochondrion is blocked by energy depletion. The data therefore satisfy one critical criterion for demonstration that the MAM does indeed represent part of the pathway of PS transport to the mitochondrion. In the future, a demonstration that release of the transport block leads to depletion of accumulated PS from the MAM, with subsequent accumulation of radiolabeled mitochondrial PE, would conclusively demonstrate that the MAM functions in PS transport to the mitochondrion.
20. 20. Zachowski A: Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem J 1993, 294:1-14.
21. 21. Savill J, Fadok V, Henson P, Haslett C: Phagocyte recognition of cells undergoing apoptosis. Immunol Today 1993, 14:131-136.
22. 22. Hanada K, Pagano RE: A Chinese hamster ovary cell mutant defective in the non-endocytic uptake of fluorescent analogs of phosphatidylserine: isolation using a cytosol acidification protocol. J Cell Biol 1995, 128:793-804. The authors employ a cytosolic acidification regimen to stimulate non-endocytic uptake of fluorescently labeled PS, and subsequently use fluorescence to screen for mutant Chinese hamster ovary cells that are unable to take up the fluorescent phospholipid efficiently. A mutant cell line is developed that exhibits specific defects in non-endocytic PS uptake in a manner that is not obviously related either to accelarated efflux of fluorescent reporter or to defects in endocytosis (both of which are situations which would result in reduced intracellular fluorescence). This mutant may be defective in the translocation of PS from the outer leaflet of the plasma membrane to the cytosolic leaflet.
23. 23. Kean LS, Fuller RS, Nichols JW: Retrograde lipid traffic in yeast: identification of two distinct pathways for internalization of fluorescent-labeled phosphatidylcholine from the plasma membrane. J Cell Biol 1993, 123:1403-1419
24. 24. Cleves AE, McGee TP, Bankaitis VA: Phospholipid transfer proteins: a biological debut. Trends Cell Biol 1991, 1:30-34.
25. 25. Bankaitis VA, Malehorn DE, Emr SD, Greene R: The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J Cell Biol 1989, 108:1271-1281.
26. 26. Bankaitis VA, Aitken JR, Cleves AE, Dowhan W: An essential role for a phospholipid transfer protein in yeast Golgi function. Nature 1990, 347:561-562.
27. 27. Cleves AE, McGee TP, Whitters EA, Champion KM, Aitken JR, Dowhan W, Goebl M, Bankaitis VA: Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cell 1991, 64:789-800.
28. 28. McGee TP, Skinner HB, Whitters EA, Henry SA, Bankaitis VA: A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes. J Cell Biol 1994, 124:273-287.
29. 29. Skinner HB, McGee TP, McMaster CR, Fry MR, Bell RM, Bankaitis VA: The Saccharomyces cerevisiae phosphatidylinositol transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity. Proc Natl Acad Sci USA 1995, 92:112-116. This paper reports both in vitro and in vivo data which indicate that Sec14p acts to specifically downregulate the activity of CCTase, the rate-determining enzyme of the CDP-choline pathway for PC biosynthesis. The in vitro data further suggest that it is the PC-bound form of Sec14p that acts as the active effector. The collective data are incorporated into the sensor model which proposes that the phospholipid-exchange activity of Sec14p functions as a molecular switch through which the CCTase-directed negative effector activity of Sec14p is itself regulated. The authors suggest that Sec14p does not function in the catalysis of phospholipid transport in vivo.
30. 30. Kagiwada S, Kearns BG, McGee TP, Fang M, Hosaka K, Bankaitis VA: The yeast BSD2-1 mutation influences both the cellular requirement for phosphatidylinositol transfer protein function and the activity of the pathway for derepression of phospholipid biosynthetic gene expression. Genetics 1996, 143:685-697. The authors demonstrate that accelerated turnover of PI represents one mechanism by which yeast can be rendered independent of the essential Sec14p requirement for Golgi secretory function and cell viability. The data suggest that the toxicity of the CDP-choline pathway is the result of a nonproductive consumption of a phospholipid precursor pool, whose presence is critical to Golgi secretory function, from Golgi membranes. This precursor is suggested to be converted into PC.
31. 31. Carmen-Lopez M, Nicaud JM, Skinner HB, Vergnolle C, Kader JC, Bankaitis VA, Gaillardin C: A phosphatidylinositol/phosphatidylcholine transfer protein is required for differentiation of the dimorphic yeast Yarrowia lipolytica from the yeast to the mycelial form. J Cell Biol 1994, 124:113-127.
32. 32. Tanaka S, Hosaka K: Cloning of a cDNA encoding a second phosphatidylinositol transfer protein by complementation of the yeast sec14 mutation. J Biochem 1994, 115:981-984.
33. 33. Westerman J, De Vries KJ, Somerharju P, Timmermans-Hereijgers JLPM, Snoek GT, Wirtz KWA: A sphingomyelin-transferring protein from chicken liver. J Biol Chem 1995, 270:14263-14266. The authors demonstrate that the newly recognized β isoform of mammalian PITP is capable of transferring sphingomyelin, in addition to PI and PC, in vitro. Although the functional significance of this feature is unclear, the data nonetheless indicate a relaxed lipid-backbone specificity for PITPβ, which can accommodate either a diacylglycerol or a ceramide lipid backbone, compared with PITPα which can accommodate only a diacylglycerol backbone.
34. 34. Hay JC, Martin TFJ: Resolution of regulated secretion into sequential MgATP-dependent and calcium-independent stages mediated by distinct cytosolic proteins. J Cell Biol 1992, 119:139-151.
35. 2+-activated secretion. Nature 1993, 366:572-575.
36. 2 synthesis.
37. 37 Ohashi M, De Vries KJ, Frank R, Snoek G, Bankaitis V, Wirtz K, Huttner WB: A role for phosphatidylinositol transfer protein in secretory vesicle formation. Nature 1995, 377:544-547. This paper demonstrates that both PITPα and PITPβ function as cytosolic factors that stimulate the budding of both constitutive secretory vesicles and immature secretory granules from the TGN of neuroendocrine cells, and that yeast Sec14p can substitute for mammalian PITP in these assays. These data suggest a conservation of execution point for PITP in yeast and mammalian cells.
38. 38. Skinner HB, Alb JG Jr, Whitters EA, Helmkamp GM Jr, Bankaitis VA: Phospholipid transfer activity is relevant to but not sufficient for the essential function of the yeast SEC14 gene product. EMBC J 1993, 12:4775-4784.
39. 2, and for ultimate hydrolysis, is defined by the PITP-bound PI pool.
40. 2-hydrolytic) reactions are also shown to be very similar, suggesting the possibility that PITP is intimately involved in driving the rate-determining PI 4-kinase reaction. Native co-immunoprecipitation data further suggest that PITP enters into a physical interaction with the EGFR, PI 4-kinase, and PLCγ1.
41. 2+-activated secretion in permeable neuroendocrine cells. Cell 1992, 70:765-775.
42. 42. Thomas GMH, Cunningham E, Fensome A, Ball A, Totty NF, Truong O, Hsuan JJ, Cockroft S: An essential role for phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling. Cell 1993, 74:919-928.
43. 2.
44. 44. Monaco ME, Gershengorn MC: Subcellular organization of receptor-mediated phosphoinositide turnover. Endocr Rev 1992, 13:707-718.
45. 45. Alb JG Jr, Gedvilaite A, Cartee RT, Skinner HB, Bankartis VA: Mutant rat phosphatidylinositol/phosphatidylcholine transfer proteins specifically defective in phosphatidylinositol transfer: implications for the regulation of phospholipid transfer activity. Proc Natl Acad Sci USA 1995, 92:8826-8830. The authors describe the use of a surrogate yeast genetic system to obtain mutant mammalian PITPs that exhibit specific defects in PI-transfer activity but unadulterated PC-transfer activity. The data implicate protein kinase C as a candidate regulator of PITP activity in mammalian cells. Moreover, the mutant PITPs define biochemical reagents that will be useful in the dissection of the individual functional roles of both PI transfer and PC transfer in the context of metazoan PITP function.
46. 46. Liscovitch M, Cantley LC: Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell 1995, 81:659-662. This review incorporates recent experimental data from a number of laboratories into a speculative model for how acidic phospholipids, particularly phosphoinositides and phosphatidic acid, might control aspects of transport vesicle biogenesis and consumption. A specific, and universal, role for PITPs is suggested. This review presents many excellent ideas that demand experimental scrutiny. However, key data regarding demonstrated functions for PITP in vivo do not easily conform to significant aspects of the proposed scheme.