Journal of Biological Chemistry
Volume 271, Issue 37, 13 September 1996, Pages 22315-22320
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Cell Biology and Metabolism
CD36 Is Palmitoylated on Both N- and C-terminal Cytoplasmic Tails*

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The membrane protein CD36 has been reported to carry out a wide range of potential functions, including serving as a receptor for thrombospondin, collagen, oxidized low density lipoprotein, fatty acids, anionic phospholipids, and Plasmodium falciparum malaria parasitized erythrocytes. This implicates CD36 in cellular adhesion, human atherosclerotic lesion formation, lipid metabolism, and malaria. A presumed rat homolog of CD36 was previously reported to be palmitoylated. We confirmed that human CD36 is palmitoylated and identified cysteines 3, 7, 464, and 466 as the palmitoylation sites using a mutagenesis approach. This result suggests that both the N- and C-terminal tails of CD36 are cytoplasmic. Published models for the topology of CD36 have the C terminus located in the cytoplasm but differ as to whether the N terminus is cytoplasmic or extracellular. To address this question, a C-terminal truncation mutant of CD36 was made by introducing a stop codon just upstream of the C-terminal transmembrane domain. This mutant was found membrane-bound when expressed in human embryonic kidney 293 cells, indicating that the N-terminal hydrophobic domain serves as a transmembrane anchor, and thus supporting a CD36 topology with two transmembrane domains.

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*

This work was supported in part by National Institutes of Health Grant GM 41297. The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by National Institutes of Health Training Grant T32 HL07038.