Reactome | IL12A binds IL12B

IL12A binds IL12B

Stable Identifier

R-HSA-8950113

Type

Reaction [uncertain]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen

Synonyms

Interleukin-12 subunit alpha binds Interleukin-12 subunit beta by protein disulfide isomerase

ReviewStatus

5/5

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The Interleukin-12 heterodimer (IL-12) is formed by Interleukin-12 subunit alpha (IL12A, IL-12p35) and Interleukin-12 subunit beta (IL12B, IL-12p40) (Podlaski et al. 1992, Kobayashi et al. 1989, Stern et al.1990). Heterodimerization occurs due to charged residue interactions (Yoon et al. 2000) and is stabilized by disulfide bounding.
IL12 heterodimerization is believed to occur in the endoplasmic reticulum (ER) because inhibition of the enzyme Prolyl 4-hydroxylase subunit beta (P4HB), referred to in this article as Protein disulfide isomerase (PDI), by bacitracin causes IL-12 retention in the ER (Alloza & Vandenbroek 2005).

Literature References

PubMed ID	Title	Journal	Year
10899108	Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12 Tobin, JF, Yoon, C, Tang, J, Stahl, M, Johnston, SC, Somers, WS	EMBO J	2000
1347984	Molecular characterization of interleukin 12 Stern, AS, Levin, W, Hulmes, JD, Chizzonite, R, Nanduri, VB, Gately, MK, Danho, W, Podlaski, FJ, Pan, YC	Arch. Biochem. Biophys.	1992
15720785	The metallopeptide antibiotic bacitracin inhibits interleukin-12 alphabeta and beta2 secretion Vandenbroeck, K, Alloza, I	J. Pharm. Pharmacol.	2005