Importance of the carboxyl terminus of FAT/CD36 for plasma membrane localization and function in long-chain fatty acid uptake

This study investigates the role of the cytoplasmic C terminus of fatty acid translocase (FAT/CD36) in localization of the molecule to the plasma membrane, its insertion into lipid rafts, and its ability to enhance long-chain fatty acid uptake in transfected H4IIE rat hepatoma cells. In these cells, wild-type FAT/CD36 is localized to both lipid raft and nonraft domains of the plasma membrane. Interestingly, a FAT/CD36 truncation mutant lacking the final 10 amino acids of the cytoplasmic C terminus was retained within the cell in detergent-resistant membranes, and unlike wild-type FAT/CD36, it did not enhance oleate uptake. Furthermore, expression of FAT/CD36 in these cells increased the incorporation of oleate into diacylglycerol, a property that was not shared by truncated FAT/CD36. To examine whether the C terminus itself has an intrinsic ability to dictate the plasma membrane localization of FAT/CD36, this region was fused in-frame to enhanced green fluorescent protein (EGFP). This domain was sufficient to attach EGFP to cellular membranes, suggesting an involvement in the intracellular traffic of the molecule. We conclude that the C terminus of FAT/CD36 is required for localization of the receptor to the cell surface and its ability to enhance cellular oleate uptake. This study investigates the role of the cytoplasmic C terminus of fatty acid translocase (FAT/CD36) in localization of the molecule to the plasma membrane, its insertion into lipid rafts, and its ability to enhance long-chain fatty acid uptake in transfected H4IIE rat hepatoma cells. In these cells, wild-type FAT/CD36 is localized to both lipid raft and nonraft domains of the plasma membrane. Interestingly, a FAT/CD36 truncation mutant lacking the final 10 amino acids of the cytoplasmic C terminus was retained within the cell in detergent-resistant membranes, and unlike wild-type FAT/CD36, it did not enhance oleate uptake. Furthermore, expression of FAT/CD36 in these cells increased the incorporation of oleate into diacylglycerol, a property that was not shared by truncated FAT/CD36. To examine whether the C terminus itself has an intrinsic ability to dictate the plasma membrane localization of FAT/CD36, this region was fused in-frame to enhanced green fluorescent protein (EGFP). This domain was sufficient to attach EGFP to cellular membranes, suggesting an involvement in the intracellular traffic of the molecule. We conclude that the C terminus of FAT/CD36 is required for localization of the receptor to the cell surface and its ability to enhance cellular oleate uptake. Fatty acid translocase (FAT; or CD36) is an ∼88 kDa glycoprotein that mediates the uptake of oxidized low density lipoprotein (OxLDL) by macrophages and is an important mediator of long-chain fatty acid (LCFA) uptake in muscle and adipose tissue (reviewed in Ref. 1Febbraio M. Hajjar D.P. Silverstein R.L. CD36: a class B scavenger receptor involved in angiogenesis, atherosclerosis, inflammation, and lipid metabolism. J. Clin. Invest. 2001; 108: 785-791Google Scholar). The generation and study of FAT/CD36 gene knockout mice and transgenic mice with muscle-specific overexpression of FAT/CD36 has demonstrated the importance of this molecule in fatty acid transport and metabolism (2Febbraio M. Abumrad N.A. Hajjar D.P. Sharma K. Cheng W. Pearce S.F. Silverstein R.L. A null mutation in murine CD36 reveals an important role in fatty acid and lipoprotein metabolism. J. Biol. Chem. 1999; 274: 19055-19062Google Scholar, 3Ibrahimi A. Bonen A. Blinn W.D. Hajri T. Li X. Zhong K. Cameron R. Abumrad N.A. Muscle-specific overexpression of FAT/CD36 enhances fatty acid oxidation by contracting muscle, reduces plasma triglycerides and fatty acids, and increases plasma glucose and insulin. J. Biol. Chem. 1999; 274: 26761-26766Google Scholar). Although LCFAs can diffuse across cell membranes (4Higgins C.F. Flip-flop: the transmembrane translocation of lipids. Cell. 1994; 79: 393-395Google Scholar), active transport via FAT/CD36 is particularly important in tissues with high metabolic demand for LCFAs, especially when plasma free fatty acid levels are low (2Febbraio M. Abumrad N.A. Hajjar D.P. Sharma K. Cheng W. Pearce S.F. Silverstein R.L. A null mutation in murine CD36 reveals an important role in fatty acid and lipoprotein metabolism. J. Biol. Chem. 1999; 274: 19055-19062Google Scholar, 5Abumrad N.A. el Maghrabi M.R. Amri E.Z. Lopez E. Grimaldi P.A. Cloning of a rat adipocyte membrane protein implicated in binding or transport of long-chain fatty acids that is induced during preadipocyte differentiation. J. Biol. Chem. 1993; 268: 17665-17668Google Scholar). Factors involved in regulating FAT/CD36 localization and activity are the subject of intense investigation. Like other class B scavenger receptors, such as scavenger receptor class B type I, FAT/CD36 is anchored in the plasma membrane by transmembrane domains at N and C termini and contains a large that is C.F. glycoprotein CD36: a of its in and Scholar, CD36 is both and cytoplasmic J. Biol. Chem. Scholar, R. M. CD36 is a glycoprotein with the domain implicated in intracellular Scholar). FAT/CD36 is at in the and cytoplasmic and it is that this to the of the molecule to the plasma membrane CD36 is both and cytoplasmic J. Biol. Chem. Scholar). Furthermore, is it the translocation of FAT/CD36 intracellular and the plasma membrane. at the of the molecule is for its localization to the cell surface or to enhanced binding and uptake of transfected cells E. E. R. The of the cytoplasmic of CD36 a domain implicated in the binding and of oxidized J. Scholar). the C terminus of FAT/CD36 is important of the in binding and uptake of and this is when the final amino acids are E. E. R. The of the cytoplasmic of CD36 a domain implicated in the binding and of oxidized J. Scholar). Furthermore, the in this region of the molecule is a of with C.F. glycoprotein CD36: a of its in and Scholar). the FAT/CD36 is to to plasma membrane as J. A. M. of membrane domains an for J. Biol. 1994; Scholar). are of the plasma membrane that are in and and implicated in of lipid metabolism (reviewed in Ref. to Biol. Scholar). the protein of is a kDa membrane protein expression and are both and sufficient to the of A. expression of in cells. A for the and study of J. Biol. Chem. Scholar, E. K. of in by expression of Scholar). Interestingly, uptake and lipid raft in a study J. A. R. W. long-chain fatty acid uptake in plasma membrane Biol. Cell. Scholar). study that the of uptake with and of lipid uptake by of with to the localization of FAT/CD36, and of oxidized low density lipoprotein scavenger receptor CD36 a lipid raft that not J. Biol. Chem. of FAT/CD36 and in transfected cells, both in detergent-resistant lipid This that FAT/CD36 can in lipid that are and that the of FAT/CD36 localized to and to lipid cell that FAT/CD36 is in X. R.L. acid translocase in and with the scavenger receptor Invest. Scholar), its localization and in these cells In the the localization of FAT/CD36 to lipid in transfected H4IIE rat hepatoma cells and rat Furthermore, the of FAT/CD36 expression uptake and metabolism in transfected H4IIE cells and the of truncation of the C terminus of the molecule these and its the of the cytoplasmic C terminus of FAT/CD36 to the of the molecule to membranes, lipid detergent-resistant membranes H4IIE rat hepatoma cells, cells, and cells in with 10 and 10 in a at and X. R.L. acid translocase in and with the scavenger receptor Invest. Scholar, K. M. of to by J. Scholar), as has the receptor M.R. of cells with a to the rat Scholar). The fluorescent protein and was and B was FAT/CD36 was A. Amri E.Z. Grimaldi Abumrad N.A. of the CD36 in fatty acid into and To a green fluorescent protein rat was by rat the and was in-frame into and The is To a a the region was into and To a FAT/CD36 lacking the final or 10 amino acid FAT/CD36 was into A as a to FAT/CD36 of by as as the and of the or are and that are with and and into and of To a the cytoplasmic of FAT/CD36 fused to the C terminus of EGFP the the final amino acid and and and into the and of and To a the membrane of A. a membrane within fused to the C terminus of EGFP the the and and and into the and of and by and a To H4IIE cell FAT/CD36, cells transfected with to the by the of and and for FAT/CD36 expression by demonstrated high expression of FAT/CD36 and was for H4IIE demonstrated expression of FAT/CD36 and was as a of these was transfected with as with To cell of the mutant FAT/CD36 H4IIE cells transfected with or as with cell and transfected with as to for To cell EGFP the C terminus of FAT/CD36 fused to EGFP or the membrane of fused to EGFP H4IIE cells transfected with or and with cells by cell a cell of cells to the cells at cells in or at cells and transfected a of surface was as A. M. E. and of for intracellular and cell surface J. Biol. Scholar). cells to in cell with and and with of in for at with This was and was for with and with in and by The protein in was by the of cellular to was with of and at by for The with at for in of and The with of cellular protein to and for for at in the of in The with for in and with the cells with rat for at was by for in the at with or and in rat the of intracellular in cells, was in and with and the cells and a and a and a of FAT/CD36 and in H4IIE hepatoma cells. and or and by to FAT/CD36 with with a a as by W. receptor that this plasma membrane domain is a for cells and Biol. Cell. Scholar), with cells to in tissue with and in of and of in to a a and and at of was in and In to a 10 and for at to and of the was to a and with an of in The was to a and the was with of and of in at for at the of the of to and cell in cell cells in of and the to as to as in the was the of by the for the of In the of the nonraft of protein was in to a final of and this was for of nonraft transmembrane and of the to and of cellular into and by and was as A. a membrane within Scholar). cells to in cell and with into of and the in of for a 10 and at for to and at for in a at and with of the in an of of and to and was as A. a membrane within Scholar). cell in cell with the of of and and for The with the of of to the of and to and to and to membranes for with in with at at at at or at in with and for with at or in with a and as J. A. W. of long-chain fatty acids in cells of a J. Scholar), with acid was by of acid with acid and in a fatty in to an of at a density of cells in tissue with of of acid at for the the acid was with of and in the was and the cells with and with and in of of the for protein by the and of To of was to of and a of acid into cellular was of cells with acid for as of cells, by with of The the was by and the in and acid and a of and triglycerides The by a acid and with and into for cell in for protein by the are as The of was by the H4IIE rat hepatoma cells for not FAT/CD36, rat can high levels of FAT/CD36 at the cell surface in X. R.L. acid translocase in and with the scavenger receptor Invest. and expression of FAT/CD36 has in E. X. A. expression of fatty acid in rat and Scholar). truncation to the that the C terminus of FAT/CD36 is required for localization of the molecule to the cell surface and these and an expression the of wild-type FAT/CD36 to the cells. expression of FAT/CD36 and truncation in the transfected H4IIE cells was by cell surface and of the that both wild-type FAT/CD36 and at the cell In was not in plasma membrane was by of cell that the molecule is retained in the of membranes with demonstrated that and the of for not was that the of was that of and wild-type FAT/CD36 of the H4IIE with that the of wild-type FAT/CD36 and the truncated that of was to the wild-type that the of wild-type FAT/CD36 and was In was in that it was not at the plasma membrane We that FAT/CD36 is by in rat in a X. R.L. acid translocase in and with the scavenger receptor Invest. Scholar). To examine whether FAT/CD36 is with lipid in to density to lipid of by and of the FAT/CD36 was with the In the receptor was that the not with nonraft of the FAT/CD36 in is with it with of detergent-resistant membranes rat and H4IIE hepatoma cells. of FAT/CD36 in rat of in at and the to the of the and to and or receptor both FAT/CD36 and of FAT/CD36 in transfected H4IIE cells wild-type FAT/CD36, or The of FAT/CD36 and with was in H4IIE cells transfected with wild-type FAT/CD36 and green fluorescent protein as in at to to and or as of FAT/CD36 in of FAT/CD36 or The of FAT/CD36 in was by and as a of with across are for of detergent-resistant membranes rat and H4IIE hepatoma cells. of FAT/CD36 in rat of in at and the to the of the and to and or receptor both FAT/CD36 and of FAT/CD36 in transfected H4IIE cells wild-type FAT/CD36, or The of FAT/CD36 and with was in H4IIE cells transfected with wild-type FAT/CD36 and green fluorescent protein as in at to to and or as of FAT/CD36 in of FAT/CD36 or The of FAT/CD36 in was by and as a of with across are for To the of truncation of the C terminus of FAT/CD36 its insertion into lipid rafts, transfected H4IIE cell the to of to membrane during transport to the cell Cell. Scholar). of the by and as in wild-type FAT/CD36 is in in transfected H4IIE cells Furthermore, truncation of the C terminus and not incorporation of the molecule into when the of FAT/CD36 and in was by it was that the of the wild-type protein that localized in the was that of the mutant protein of membranes with an the receptor membrane that the not with this nonraft protein not The of FAT/CD36 and FAT/CD36 truncation in the localization to and lipid lipid to H4IIE cells expression of by not are a of lipid that are to in at and are by and with To examine whether and the of the of FAT/CD36, a a protein was in the cell that are wild-type in and in of a in cells green fluorescent protein The of is by 1999; Scholar, J. A. of reveals a to the Biol. 2001; Scholar, K. M. are plasma membrane are not involved in Biol. Cell. Scholar). in H4IIE cells, the protein was in the Furthermore, the of a the of FAT/CD36 in cells transfected with with cells the of is not for the incorporation of FAT/CD36 into in cells of this rat FAT/CD36 with in cells. FAT/CD36 was in transfected H4IIE cells that that FAT/CD36 can in lipid raft domains that are The localization of FAT/CD36 was by cells with to lipid raft and with to FAT/CD36. FAT/CD36 was to with both at the cell surface and within cells and that FAT/CD36 is with lipid and that of these are The of and its with of wild-type FAT/CD36 not as in was of the H4IIE it was localized in cytoplasmic that with to cytoplasmic Although the density of FAT/CD36 with this not and lipid that D.P. J. of of Scholar, A. in cells detergent-resistant J. Biol. Scholar). was to examine whether FAT/CD36 to the membrane domains as when cells are transfected with in wild-type FAT/CD36 and in the plasma membranes of the cells. Furthermore, and of the was within large in the The of and its with In was localized to intracellular that shared with not To whether cell surface FAT/CD36 is with lipid J. A. R. W. long-chain fatty acid uptake in plasma membrane Biol. Cell. Scholar), transfected cells with of with the in FAT/CD36 was in and in the and membrane with that surface and that transmembrane with in these cells. To examine whether FAT/CD36 in the and the is the surface the with FAT/CD36 was both that the FAT/CD36 at the cell surface is with both membranes and of FAT/CD36 in both the and of this was by a with not the membrane with a in the the a to that of FAT/CD36 FAT/CD36, and with in transfected H4IIE cells, cytoplasmic of it was whether the FAT/CD36 that was with nonraft was with membranes in the of whether membrane to intracellular To examine cellular into and by and wild-type FAT/CD36 and the truncated FAT/CD36 in to with membrane To of truncation the of FAT/CD36 into membranes, the of FAT/CD36 and the truncation in at was as in The and by in wild-type and truncated of FAT/CD36 with the these that the wild-type and truncated FAT/CD36 are of the truncated protein within the the of a plasma membrane in the To this a the amino acid to the of the EGFP was transfected into H4IIE and cells. The of the protein in the was in membranes by and in and transfected with a the membrane of to EGFP A. a membrane within as a of the C terminus of FAT/CD36 was sufficient to a of the EGFP protein with membranes in H4IIE and cells EGFP was in with membranes cells the protein with the membrane was not in membranes H4IIE and was in in membranes transfected cells. Although of the EGFP protein the C terminus of FAT/CD36 was with the transfected cells, a was with the as was of the protein In EGFP was in the and of the protein not C terminus of FAT/CD36 membrane to transfected H4IIE cells and transfected cells to and the membrane was by the EGFP protein the amino acids of FAT/CD36 or cells as the and to and with the The of the in the was by of the cells with the and to and are of To whether the C terminus of FAT/CD36 the of EGFP with H4IIE in at and the was by Although EGFP and in that are to and nonraft membrane EGFP the C terminus of FAT/CD36 was in the at low levels a H4IIE cells to the in this protein was in the To the of the C terminus or its the localization of to cells wild-type FAT/CD36, or with acid to of fatty The of and the of fatty acid to within M. Silverstein R.L. Abumrad N.A. uptake and of fatty acids in muscle and adipose tissues of CD36 knockout J. Biol. Chem. Scholar). was in the H4IIE and cell and oleate uptake was increased in cells FAT/CD36 of FAT/CD36 or enhanced uptake at expression of was by a in uptake to H4IIE cells of that expression of FAT/CD36 in H4IIE cells in a in the incorporation of oleate into this was not in cells of the truncated Furthermore, overexpression of FAT/CD36 a in oleate incorporation into This was in cells expression of did not oleate incorporation into of the expression of wild-type FAT/CD36 and FAT/CD36 truncation the incorporation of acid into cell fatty acid and are as acid are for are of in a fatty acid and are as acid are for are of is in and muscle cells that are both surface and intracellular of FAT/CD36 and that can a in to such as and of A. A. Abumrad N.A. activity increases fatty acid metabolism and transport and FAT/CD36. J. 1999; Scholar, A. of fatty acid uptake the cellular of fatty acid J. Biol. Chem. Scholar, A. the translocation of the fatty acid FAT/CD36 to the plasma membrane. J. Scholar). In these cells, of FAT/CD36 to the cell surface a to the of the cell for is not whether cytoplasmic in other cell traffic of FAT/CD36 the to the plasma membrane. in that is required for the expression of FAT/CD36 at the plasma membrane A. J. W. is required for fatty acid translocase (FAT/CD36) localization and at the plasma membrane of Scholar), localization of FAT/CD36 to for the molecule to in transport J. A. R. W. long-chain fatty acid uptake in plasma membrane Biol. Cell. Scholar, A. J. W. is required for fatty acid translocase (FAT/CD36) localization and at the plasma membrane of Scholar). We that FAT/CD36 is by in rat X. R.L. acid translocase in and with the scavenger receptor Invest. Scholar). In this of the localization of FAT/CD36 in a rat cell and in rat with to the role of the C terminus in the intracellular traffic of the molecule and the with lipid and FAT/CD36 of a large that is anchored to the plasma membrane via cytoplasmic at the N and C termini CD36 is both and cytoplasmic J. Biol. Chem. Scholar, R. M. CD36 is a glycoprotein with the domain implicated in intracellular Scholar, and of glycoprotein J. Biol. Chem. Scholar). The transmembrane domain of FAT/CD36 is for its localization to the cell as of this region in in R. M. CD36 is a glycoprotein with the domain implicated in intracellular Scholar). We that FAT/CD36 lacking the 10 amino acid is retained in In was of the amino acids, suggesting that the is involved in membrane of FAT/CD36. the the of that are required for plasma membrane localization or for with an protein to the protein of scavenger receptor class B type (reviewed in Ref. A. A. M. of lipoprotein metabolism by the protein Scholar). of to the plasma membrane and to lipid to at such as fatty the of a region (reviewed in Ref. by membrane Biol. 1999; Scholar). The are at and in the C terminus of FAT/CD36 CD36 is both and cytoplasmic J. Biol. Chem. Scholar, R. M. CD36 is a glycoprotein with the domain implicated in intracellular Scholar). mutation of these not surface expression of the molecule in transfected cells E. E. R. The of the cytoplasmic of CD36 a domain implicated in the binding and of oxidized J. Scholar). the importance of the C terminus is by that truncation of the 10 amino acids the of FAT/CD36 with the plasma membrane in both H4IIE hepatoma cells and cells In a study in transfected cells demonstrated that at in the cytoplasmic C terminus did not the surface expression of FAT/CD36 J. K. to by the cytoplasmic J. Biol. Scholar). The for the these and in cells that it is the or of a cytoplasmic that is the of an EGFP protein the C terminus of FAT/CD36 not this these a role for the C terminus in the of FAT/CD36 to membranes, overexpression in H4IIE cells to the of a of the protein in membrane the of a large of the protein in the of that the for to membranes are or that of the EGFP an of the protein are required to the that the of FAT/CD36 to cellular membranes, lipid the C terminus is for the expression of FAT/CD36 at the plasma membrane, by of the molecule the A. in the Biol. the for the of that the truncated protein is and retained in the in transfected H4IIE cells this important of FAT/CD36 at the plasma membrane in and muscle cells is its with J. A. M. of membrane domains an for J. Biol. 1994; Scholar, M. uptake of by of fatty acid translocase in type Scholar, J. J. J. and of rat adipocyte J. Biol. Chem. Scholar, of fatty acid translocase in and muscle Biol. Scholar, K. Bonen A. FAT/CD36 in muscle with and is in type in type J. Scholar). with lipid is to important for the of FAT/CD36 in of lipid by with the and has to the uptake of by J. A. R. A. W. fatty acid uptake into lipid raft Scholar). Furthermore, has to fatty acids of as a fatty acid binding 1999; Scholar), and this to the that FAT/CD36 and in to uptake J. A. R. T. W. of cellular fatty acid role of fatty acid transport and of Scholar). In this FAT/CD36 transport or the of LCFAs across the plasma membrane, the of to LCFAs or at the and to intracellular or in transport within the in transfected H4IIE hepatoma cells that the expression of FAT/CD36 at the plasma membrane is not the of Furthermore, FAT/CD36 was localized to both detergent-resistant and of the plasma membrane in H4IIE cells that FAT/CD36 is with lipid was by with binding to Interestingly, retained in the truncation mutant was in to conclude that FAT/CD36 into lipid within membrane and that its localization to the plasma membrane the C terminus of the molecule. The of FAT/CD36 with the protein in H4IIE cells that FAT/CD36 can lipid to or that and can as a of with the of FAT/CD36 with in cells, the expression of did not the of or uptake in H4IIE hepatoma cells not this was in it was that uptake is in knockout mice A. J. W. is required for fatty acid translocase (FAT/CD36) localization and at the plasma membrane of Scholar). This was to intracellular of FAT/CD36 in these cells. the in are in with in hepatoma cells. that the expression for the expression of FAT/CD36 at the plasma membrane and for activity of the molecule in transport cell an FAT/CD36 and has not in cells of oxidized low density lipoprotein scavenger receptor CD36 a lipid raft that not J. Biol. Chem. Scholar, M. uptake of by of fatty acid translocase in type Scholar, J. J. J. and of rat adipocyte J. Biol. Chem. Scholar). is that in rat of the FAT/CD36 is with not with the other FAT/CD36 is with in transfected H4IIE hepatoma cells, not at in and cells, is not a the expression of and the localization of FAT/CD36 to or the of and the surface expression of FAT/CD36 or uptake. The expression of FAT/CD36 in H4IIE hepatoma cells in a in the of to that in in other cell A. Amri E.Z. Grimaldi Abumrad N.A. of the CD36 in fatty acid Scholar, M. R. M. M. E. fatty acid metabolism and localization of and FAT/CD36 in muscle cells. J. Scholar, W. of acid with the scavenger receptor CD36 fatty acid uptake by cells. 2001; Scholar). In the truncation is retained in cytoplasmic membranes, did not enhance uptake. A for the surface expression of FAT/CD36 can that increases in uptake with translocation of the molecule intracellular to the in and muscle (reviewed in Ref. D.P. Bonen A. fatty acid uptake and FAT/CD36 translocation in and Scholar). Although the of FAT/CD36 in the is these as in other cells, the molecule the uptake of LCFAs by Furthermore, that FAT/CD36 the intracellular of LCFAs in H4IIE cells FAT/CD36 uptake of acid with cells. This was by a in This with other in the overexpression of FAT/CD36 in was with incorporation of LCFAs into M. R. M. M. E. fatty acid metabolism and localization of and FAT/CD36 in muscle cells. J. Scholar, Hajri T. Grimaldi P.A. Abumrad N.A. CD36 in fatty acids to a that is to cell lipid and Scholar). In the of is by fatty acid and the activity of the J. in rat The role of J. Scholar, W. of in rat of fatty acid and 1994; Scholar). and M. Silverstein R.L. Abumrad N.A. uptake and of fatty acids in muscle and adipose tissues of CD36 knockout J. Biol. Chem. Scholar), that the low of for to that when the for and that the expression of FAT/CD36 in cells the of to FAT/CD36 or LCFAs levels and the of to The that membranes high levels of FAT/CD36, it to in the of LCFAs for by the molecule the of fatty acids within the cell Bonen A. A for fatty acid translocase involvement in fatty acid into the J. Biol. Chem. Scholar, Bonen A. of fatty acid translocase muscle role in fatty acid J. Scholar). H4IIE cells and cells low levels of oxidation J. for an long-chain fatty acid oxidation and in hepatoma cells. J. Scholar), increased of the of in the FAT/CD36 transfected cells. The of the C terminus of FAT/CD36 the of LCFAs it to that this domain that the intracellular localization of FAT/CD36 is for the of In this study an important role for the C terminus of FAT/CD36 in the of the molecule. Furthermore, or its this domain the of that cell or in the role of FAT/CD36 in metabolism and that these in whether the molecule is for localization to the cell surface and to lipid into the role of the C terminus of FAT/CD36 in the localization of the molecule to the involved in translocation of the molecule intracellular to the plasma membrane in adipose tissue and with was by of The are to and of of and for and in cell The for with B detergent-resistant membrane enhanced green fluorescent protein fatty acid translocase long-chain fatty acid oxidized low density lipoprotein