Four cholesterol-sensing proteins

Current Opinion in Structural Biology

Volumn 8, Issue 4, 1998, Pages 435-439

  Lange, Yvonne ^a   Steck, Theodore L ^b  

^a RUSH UNIVERSITY MEDICAL CENTER   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANE PROTEIN; CHOLESTEROL; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; PROTEIN C;

CELL LEVEL; CHOLESTEROL TRANSPORT; HOLOPROSENCEPHALY; HOMEOSTASIS; HUMAN; HUMAN CELL; LAMELLAR BODY; LIPIDOSIS; LYSOSOME; NIEMANN PICK DISEASE; PRIORITY JOURNAL; REVIEW;

EID: 0032143349     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80119-X     Document Type: Article

References (55)

1. Bloom M, Evans E, Mouritsen O. Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective. Q Rev Biophys. 24:1991;293-397.
2. Mouritsen OG, Jorgensen K. Dynamical order and disorder in lipid bilayers. Chem Phys Lipids. 73:1994;3-25.
3. Hua X, Nohturfft A, Goldstein JL, Brown M. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell. 87:1996;415-426.
4. Beachy PA, Cooper MK, Young KE, von Kessler DP, Park W-J, Tanaka Hall TM, Leahy DJ, Porter J. Multiple roles of cholesterol in hedgehog protein biogenesis and signaling. of outstanding interest Cold Spring Harb Symp Quant Biol. 62:1997;191-204 Multiple connections are noted between cholesterol and early embryonic development. First is the tethering of a morphogenetic signal protein (Hedgehog) to the cell surface through a novel covalent bond to cholesterol. Secondly, an integral membrane protein (Patched), which is responsive to Hedgehog signals, has a putative sterol-sensing domain. Third, certain teratogens perturb cholesterol homeostasis.
5. Lange Y, Echevarria F, Steck TL. Movement of zymosterol, a precursor of cholesterol, among three membranes in human fibroblasts. J Biol Chem. 266:1991;21439-21443.
6. Uittenbogaard A, Ying Y-s, Smart EJ. Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking. of outstanding interest J Biol Chem. 273:1998;6525-6532 A fraction of caveolin is reported to form a soluble immunophilin - chaperone complex, which stimulates the movement of intracellular cholesterol to the plasma membrane.
7. Lange Y, Strebel F, Steck TL. Role of the plasma membrane in cholesterol esterification in rat hepatoma cells. J Biol Chem. 268:1993;13838-13843.
8. Brasaemle DL, Attie AD. Rapid intracellular transport of LDL-derived cholesterol to the plasma membrane in cultured fibroblasts. J Lipid Res. 31:1990;103-112.
9. Lange Y, Ye J, Steck TL. Circulation of cholesterol between lysosomes and the plasma membrane. J Biol Chem. 273:1998;18915-18922.
10. Underwood KW, Jacobs NL, Howley A, Liscum L. Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane. J Biol Chem. 273:1998;4266-4274.
11. Lange Y, Ye J, Chin J. The fate of cholesterol exiting lysosomes. J Biol Chem. 272:1997;17018-17022.
12. Freeman DA. Plasma membrane cholesterol: removal and insertion into the membrane and utilization as substrate for steroidogenesis. Endocrinology. 124:1989;2527-2534.
13. Lange Y, Steck TL. Cholesterol homeostasis. Modulation by amphiphiles. J Biol Chem. 269:1994;29371-29374.
14. Conrad PA, Smart EJ, Ying YS, Anderson RG, Bloom G. Caveolin cycles between plasma membrane caveolae and the Golgi complex bymicrotubule-dependent and microtubule-independent steps. J Cell Biol. 131:1995;1421-1433.
15. Lange Y, Swaisgood MH, Ramos B, Steck TL. Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts. J Biol Chem. 264:1989;3786-3793.
16. Liscum L, Underwood K. Intracellular cholesterol transport and compartmentation. J Biol Chem. 270:1995;15443-15446.
17. Harder T, Simons K. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr Opin Cell Biol. 9:1997;534-542.
18. Brown DA, London E. Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes? of special interest Biochem Biophys Res Commun. 240:1997;1-7 The significance of cholesterol-rich membrane bilayer domains that are stable in nonionic detergents is critically evaluated.
19. Scheiffele P, Verkade P, Fra AM, Virta H, Simons K, Ikonen E. Caveolin-1 and -2 in the exocytic pathway of MDCK cells. of special interest J Cell Biol. 140:1998;795-806 This paper provides evidence for both the vectorial movement of nascent caveolin isoforms and their role in targeting proteins to the surfaces of polarized epithelial cells.
20. Keller P, Simons K. Cholesterol is required for surface transport of influenza virus hemaggliutinin. of special interest J Cell Biol. 140:1998;137-1367 The fact that cholesterol-sphingolipid rafts are vehicles in targeted exocytosis traffic is persuasively documented.
21. Fielding CJ, Fielding PE. Intracellular cholesterol transport. of special interest J Lipid Res. 38:1997;1503-1521 A broad review, featuring the mechanisms that mediate cholesterol import from and export to high density lipoproteins.
22. Antonenkov V, Van Veldhoven P, Waelkens E, Mannaerts G. Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2 3 -oxoacyl-CoA thiolase purified from normal rat liver peroxisomes. Sterol carrier protein 2 3 -oxoacyl-CoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates. of special interest J Biol Chem. 272:1997;26023-26031 A strong contribution to the growing evidence suggesting that so-called 'sterol carrier proteins' may not serve this function in vivo.
23. Ikonen E. Molecular mechanisms of intracellular cholesterol transport. Curr Opin Lipidol. 8:1997;60-64.
24. Babitt J, Trigatti B, Rigotti A, Smart EJ, Anderson RG, Xu S, Krieger M. Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae. of special interest J Biol Chem. 272:1997;13242-13249 Caveolae are sterol-rich membrane domains that appear to carry out multiple structural and functional roles at the cell surface and in the cell interior. SR-BI, the receptor that mediates the transfer of cholesterol between plasma membranes and high-density plasma lipoproteins and therefore plays an important role in both cell and whole-body cholesterol homeostasis, is shown to be concentrated in caveolae.
25. Bist A, Fielding PE, Fielding C. Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol. of special interest Proc Natl Acad Sci USA. 94:1997;10693-10698 Cholesterol is shown to positively regulate the expression of caveolin.
26. Hailstones D, Sleer LS, Parton RG, Stanley K. Regulation of caveolin and caveolae by cholesterol in MDCK cells. of special interest J Lipid Res. 39:1998;369-379 Cholesterol is shown to positively regulate the expression of caveolin.
27. Stocco D. A review of the characteristics of the protein required for the acute regulation of steroid hormone biosynthesis: the case for the steroidogenic acute regulatory (StAR) protein. of special interest Proc Soc Exp Biol Med. 217:1998;123-129 An up-to-date overview of a newly discovered mitochondrial protein that regulates steroidogenesis.
28. Goldstein JL, Brown M. Regulation of the mevalonate pathway. Nature. 343:1990;425-430.
29. Brown MS, Goldstein JL. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. of outstanding interest Cell. 89:1997;331-340 An overview of the system by which ER transcription factors regulate the expression of ER proteins that mediate cholesterol homeostasis.
30. Lange Y, Steck TL. The role of intracellular cholesterol transport in cholesterol homeostasis. Trends Cell Biol. 6:1996;205-208.
31. Lange Y, Steck TL. Quantification of the pool of cholesterol associated with acyl-CoA cholesterol acyltransferase in human fibroblasts. of outstanding interest J Biol Chem. 272:1997;13103-13108 Most of the proteins that control the level of cholesterol in cells are located in the endoplasmic reticulum (ER). The pool of cholesterol in the ER membrane is shown to be very small and very responsive to physiological stimuli. The size of the ER cholesterol compartment therefore appears to be regulated so as to serve as a critical element in cholesterol homeostasis.
32. Cheng D, Chang CC, Qu X, Chang T. Activation of acyl-coenzyme A:cholesterol acyltransferase by cholesterol or by oxysterol in a cell-free system. J Biol Chem. 270:1995;685-695.
33. Chang TY, Chang CC, Cheng D. Acyl-coenzyme A:cholesterol acyltransferase. of special interest Annu Rev Biochem. 66:1997;613-638 A definitive review of a critical element in cholesterol homeostasis.
34. Olender EH, Simoni R. The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase. J Biol Chem. 267:1992;4223-4235.
35. McGee TP, Cheng HH, Kumagai H, Omura S, Simon R. Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J Biol Chem. 271:1996;25630-25638.
36. Sakai J, Duncan EA, Rawson RB, Hua X, Brown MS, Goldstein J. Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell. 85:1996;1037-1046.
37. Sakai J, Nohturfft A, Cheng D HY, Brown MS, Goldstein J. Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein. J Biol Chem. 272:1997;20213-20221.
38. Sakai J, Nohturfft A, Goldstein JL, Brown MS. Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies. of special interest J Biol Chem. 273:1998;5785-5793 SREBPs are transcription factors that are activated by cleavage from the endoplasmic reticulum (ER) membrane under cholesterol control. The ER protein SCAP (SREBP cleavage-activating protein) is thought to regulate this proteolytic process, presumably using its sterol-sensing domain. This study provides evidence for the direct association of SCAP with its target, the SREBPs.
39. Scheek S, Brown MS, Goldstein J. Sphingomyelin depletion in cultured cells blocks proteolysis of sterol regulatory element binding proteins at site 1. of special interest Proc Natl Acad Sci USA. 94:1997;11179-11183 The authors describe direct evidence that the proteolytic activation of SREBP is made in response to ER levels of cholesterol.
40. Hruban Z. Pulmonary and generalized lysosomal storage induced by amphiphilic drugs. Environ Health Perspect. 55:1984;53-76.
41. Schmitz G, Muller G. Structure and function of lamellar bodies, lipid-protein complexes involved in storage and secretion of cellular lipids. J Lipid Res. 32:1991;1539-1570.
42. McGookey DJ, Anderson R. Morphological characterization of the cholesteryl ester cycle in cultured mouse macrophage foam cells. J Cell Biol. 97:1983;1156-1168.
43. Butler JD, Blanchette-Mackie J, Goldin E, O'Neill RR, Carstea G, Roff CF, Patterson MC, Patel S, Comly ME, Cooney A, et al. Progesterone blocks cholesterol translocation from lysosomes. J Biol Chem. 267:1992;23797-23805.
44. Mazzone T, Krishna M, Lange Y. Progesterone blocks intracellular translocation of free cholesterol derived from cholesterol ester in macrophages. J Lipid Res. 36:1995;544-551.
45. Metherall JE, Waugh K, Li H. Progesterone inhibits cholesterol biosynthesis in cultured cells. Accumulation of cholesterol precursors. J Biol Chem. 271:1996;2627-2633.
46. Metherall JE, Li H, Waugh K. Role of multidrug resistance P-glycoproteins in cholesterol biosynthesis. J Biol Chem. 271:1996;2634-2640.
47. Field FJ, Born E, Murthy S, Mathur S. Transport of cholesterol from the endoplasmic reticulum to the plasma membrane is constitutive in CaCo-2 cells and differs from the transport of plasma membrane cholesterol to the endoplasmic reticulum. J Lipid Res. 39:1998;333-343.
48. Debry P, Nash EA, Neklason DW, Metherall J. Role of multidrug resistance P-glycoproteins in cholesterol esterification. J Biol Chem. 272:1997;1026-1031.
49. Pentchev PG, Vanier MT, Suzuki K, Patterson MC. Niemann-Pick disease type C: a cellular cholesterol lipidosis. Scriver CR, Beaudet AL, Sly WS, Valle D, Stanbury JB, Wyngaarden JB, Fredrickson DS. The Metabolic and Molecular Bases of Inherited Disease. 1995;2625-2639 McGraw-Hill, New York.
50. Carstea ED, Morris JA, Coleman KG, Loftus SK, Zhang D, Cummings C, Gu J, Rosenfeld MA, Pavan WJ, Krizman DB, et al. Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. of outstanding interest Science. 277:1997;228-231 The identification of NPC1, the gene for a fatal cholesterol storage disease, suggests that it is an integral membrane glycoprotein with a sterol-sensing domain.
51. Loftus SK, Morris JA, Carstea ED, Gu JZ, Cummings C, Brown A, Ellison J, Ohno K, Rosenfeld MA, Tagle DA, et al. Murine model of Niemann-Pick C disease: mutation in a cholesterol homeostasis gene. Science. 277:1997;232-235.
52. Pentchev PG, Brady RO, Blanchette-Mackie EJ, Vanier MT, Carstea ED, Parker CC, Goldin E, Roff CF. The Niemann-Pick C lesion and its relationship to the intracellular distribution and utilization of LDL cholesterol. Biochim Biophys Acta. 1225:1994;235-243.
53. Herz J, Willnow TE, Farese RJ. Cholesterol, hedgehog and embryogenesis. Nat Genet. 15:1997;123-124.
54. Porter JA, Young KE, Beachy P. Cholesterol modification of hedgehog signaling proteins in animal development. Science. 274:1996;255-259.
55. Cooper MK, Porter JA, Young KE, Beachy P. Teratogen-mediated inhibition of target tissue response in Sonic hedgehog signaling. of outstanding interest Science. 280:1998;1603-1607 Amphiphiles that perturb sterol homeostasis affect the morphogenetic control system, which responds to Hedgehog. The target of these amphiphiles may be Patched, a sterol-sensing receptor for Hedgehog.