Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.13/929536

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Title
Palmitoylation of CD36/FAT regulates the rate of its post-transcriptional processing in the endoplasmic reticulum
Author/Creator
Thorne, Rick F.;  Ralston, Kylie J.;  de Bock, Charles Edo;  Mhaidat, Nizar M.;  Zhang, Xu Dong;  Boyd, Andrew W.;  Burns, Gordon F.
Institution
The University of Newcastle. Faculty of Health, School of Biomedical Sciences and Pharmacy
Description
CD36/FAT is a transmembrane glycoprotein that functions in the cellular uptake of long-chain fatty acids and also as a scavenger receptor. As such it plays an important role in lipid homeostasis and, pathophysiologically, in the progression of type 2 diabetes and atherosclerosis. CD36 expression is tightly regulated at the levels of both transcription and translation. Here we show that its expression and location are also regulated post-translationally, by palmitoylation. Although palmitoylation of CD36 was not required for receptor maturation and cell surface expression, inhibition of palmitoylation either pharmacologically with cerulenin or by mutation of the relevant cysteines delayed processing at the ER and trafficking through the secretory pathway. The absence of palmitoylation also reduced the half life of the CD36 protein. Additionally, the CD36 palmitoylation mutant did not incorporate efficiently into lipid rafts, a site known to be required for its function of fatty acid uptake, and this reduced the efficiency of uptake of oxidized low density lipoprotein. These findings provide an added level of sophistication where translocation of CD36 to the plasma membrane may be physiologically regulated by palmitoylation.
Relation
Biochimica et Biophysica Acta: Molecular Cell Research Vol. 1803, Issue 11, p. 1298-1307
Publisher Link
http://dx.doi.org/10.1016/j.bbamcr.2010.07.002
Date
2010
Publisher
Elsevier
Keyword(s)
acylation;  CD36;  detergent-resistant membranes (DRMs);  endoplasmic reticulum (ER);  lipids rafts;  oxidised low density lipoprotein (oxLDL);  palmitoylation
Resource Type
journal article
Identifier
http://hdl.handle.net/1959.13/929536
Identifier
ISSN:0167-4889
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Subject
"Biochimica et Biophysica Acta: Molecular Cell Research"
 
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