Editing CD36 (section)

== Function ==

The protein itself belongs to the class B [[scavenger receptor (immunology)|scavenger receptor]] family which includes receptors for selective cholesteryl ester uptake, [[SCARB1|scavenger receptor class B type I]] (SR-BI) and [[SCARB2|lysosomal integral membrane protein II]] (LIMP-II).

CD36 interacts with a number of ligands, including [[collagen]] types I and IV, [[thrombospondin]], [[erythrocyte]]s parasitized with ''[[Plasmodium falciparum]]'', platelet-agglutinating protein p37, oxidized [[low density lipoprotein]] and [[long-chain fatty acid]]s.<ref>{{cite journal | vauthors = Armesilla AL, Vega MA | title = Structural organization of the gene for human CD36 glycoprotein | journal = The Journal of Biological Chemistry | volume = 269 | issue = 29 | pages = 18985–91 | date = July 1994 | doi = 10.1016/S0021-9258(17)32263-9 | pmid = 7518447 | doi-access = free | hdl = 2436/7744 | hdl-access = free }}</ref>

On [[macrophages]] CD36 forms part of a [[non-opsonic receptor]] (the scavenger receptor CD36/[[alpha-v beta-3]] complex) and is involved in [[phagocytosis]].<ref>{{cite journal | vauthors = Erdman LK, Cosio G, Helmers AJ, Gowda DC, Grinstein S, Kain KC | title = CD36 and TLR interactions in inflammation and phagocytosis: implications for malaria | journal = Journal of Immunology | volume = 183 | issue = 10 | pages = 6452–9 | date = November 2009 | pmid = 19864601 | pmc = 2853812 | doi = 10.4049/jimmunol.0901374 }}</ref>

CD36 has also been implicated in [[hemostasis]], [[thrombosis]], [[malaria]], [[inflammation]], [[lipid]] [[metabolism]] and [[atherogenesis]].<ref>{{cite journal | vauthors = Daviet L, McGregor JL | title = Vascular biology of CD36: roles of this new adhesion molecule family in different disease states | journal = Thrombosis and Haemostasis | volume = 78 | issue = 1 | pages = 65–9 | date = July 1997 | pmid = 9198129 | doi = 10.1055/s-0038-1657502 | s2cid = 21113427 }}</ref>

On binding a ligand the protein and ligand are internalized. This internalization is independent of [[macropinocytosis]] and occurs by an actin dependent mechanism requiring the activation Src-family kinases, JNK and Rho-family GTPases.<ref name="pmid19740737">{{cite journal | vauthors = Collins RF, Touret N, Kuwata H, Tandon NN, Grinstein S, Trimble WS | title = Uptake of oxidized low density lipoprotein by CD36 occurs by an actin-dependent pathway distinct from macropinocytosis | journal = The Journal of Biological Chemistry | volume = 284 | issue = 44 | pages = 30288–97 | date = October 2009 | pmid = 19740737 | pmc = 2781584 | doi = 10.1074/jbc.M109.045104 | doi-access = free }}</ref> Unlike macropinocytosis this process is not affected by [[PI3K inhibitor|inhibitors of phosphatidylinositol 3-kinase]] or Na<sup>+</sup>/H<sup>+</sup> exchange.

CD36 ligands have also been shown to promote sterile inflammation through assembly of a [[Toll-like receptor]] 4 and 6 heterodimer.<ref name="pmid20037584">{{cite journal | vauthors = Stewart CR, Stuart LM, Wilkinson K, van Gils JM, Deng J, Halle A, Rayner KJ, Boyer L, Zhong R, Frazier WA, Lacy-Hulbert A, El Khoury J, Golenbock DT, Moore KJ | display-authors = 6 | title = CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer | journal = Nature Immunology | volume = 11 | issue = 2 | pages = 155–61 | date = February 2010 | pmid = 20037584 | pmc = 2809046 | doi = 10.1038/ni.1836 }}</ref>

Recently, CD36 was linked to store-operated calcium flux, [[Phospholipase A2|phospholipase A<sub>2</sub>]] activation, and production of [[prostaglandin E2|prostaglandin E<sub>2</sub>]]<ref name="pmid21454644">{{cite journal | vauthors = Kuda O, Jenkins CM, Skinner JR, Moon SH, Su X, Gross RW, Abumrad NA | title = CD36 protein is involved in store-operated calcium flux, phospholipase A2 activation, and production of prostaglandin E2 | journal = The Journal of Biological Chemistry | volume = 286 | issue = 20 | pages = 17785–95 | date = May 2011 | pmid = 21454644 | pmc = 3093854 | doi = 10.1074/jbc.M111.232975 | doi-access = free }}</ref>

CD36 function in long-chain fatty acid uptake and signaling can be irreversibly inhibited by [[sulfo-N-succinimidyl oleate]] (SSO), which binds lysine 164 within a hydrophobic pocket shared by several CD36 ligands, e.g. fatty acid and oxLDL.<ref name="pmid23603908"/> Recent research concluded that CD36 is involved in the fat taste transduction ([[oleogustus]]).