TY - JOUR
T1 - Post-translational modifications of CD36 (SR-B2): Implications for regulation of myocellular fatty acid uptake
AU - Luiken, Joost J. F. P.
AU - Chanda, Dipanjan
AU - Nabben, Miranda
AU - Neumann, Dietbert
AU - Glatz, Jan F. C.
PY - 2016/12
Y1 - 2016/12
N2 - The membrane-associated protein CD36, now officially designated as SR-B2, is present in various tissues and fulfills multiple cellular functions. In heart and muscle, CD36 is the main (long-chain) fatty acid transporter, regulating myocellular fatty acid uptake via its vesicle-mediated reversible trafficking (recycling) between intracellular membrane compartments and the cell surface. CD36 is subject to various types of post-translational modification. This review focusses on the role of these modifications in further regulation of myocellular fatty acid uptake. Glycosylation, ubiquitination and palmitoylation are involved in regulating CD36 stability, while phosphorylation at extracellular sites affect the rate of fatty acid uptake. In addition, CD36 modification by O-linked N-acetylglucosamine may regulate the translocation of CD36 from endosomes to the cell surface. Acetylation of CD36 has also been reported, but possible effects on CD36 expression and/or functioning have not yet been addressed. Taken together, CD36 is subject to a multitude of post-translational modifications of which their functional implications are beginning to be understood. Moreover, further investigations are needed to disclose whether these post-translational modifications play a role in altered fatty acid uptake rates seen in several pathologies of heart and muscle. This article is part of a special issue entitled: The role of post-translational protein modifications on heart and vascular metabolism edited by Jason R.B. Dyck and Jan F.C. Glatz.
AB - The membrane-associated protein CD36, now officially designated as SR-B2, is present in various tissues and fulfills multiple cellular functions. In heart and muscle, CD36 is the main (long-chain) fatty acid transporter, regulating myocellular fatty acid uptake via its vesicle-mediated reversible trafficking (recycling) between intracellular membrane compartments and the cell surface. CD36 is subject to various types of post-translational modification. This review focusses on the role of these modifications in further regulation of myocellular fatty acid uptake. Glycosylation, ubiquitination and palmitoylation are involved in regulating CD36 stability, while phosphorylation at extracellular sites affect the rate of fatty acid uptake. In addition, CD36 modification by O-linked N-acetylglucosamine may regulate the translocation of CD36 from endosomes to the cell surface. Acetylation of CD36 has also been reported, but possible effects on CD36 expression and/or functioning have not yet been addressed. Taken together, CD36 is subject to a multitude of post-translational modifications of which their functional implications are beginning to be understood. Moreover, further investigations are needed to disclose whether these post-translational modifications play a role in altered fatty acid uptake rates seen in several pathologies of heart and muscle. This article is part of a special issue entitled: The role of post-translational protein modifications on heart and vascular metabolism edited by Jason R.B. Dyck and Jan F.C. Glatz.
KW - CD36
KW - SR-B2
KW - Post-translational modification
KW - Cardiac fatty acid uptake
U2 - 10.1016/j.bbadis.2016.09.004
DO - 10.1016/j.bbadis.2016.09.004
M3 - Article
C2 - 27615427
SN - 0925-4439
VL - 1862
SP - 2253
EP - 2258
JO - Biochimica et Biophysica Acta-Molecular Basis of Disease
JF - Biochimica et Biophysica Acta-Molecular Basis of Disease
IS - 12
ER -