IL12B dimerizes

Stable Identifier
Reaction [transition]
Homo sapiens
Interleukin-12 subunit beta binds Interleukin-12 subunit beta forming Interleukin-12 beta homodimer, IL-12B binds IL-12B to for a IL12B homodimer
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Murine cells have been shown to produce Interleukin-12 homodimer (IL-12p80) (Gillessen et al. 1995). In a cell-free system porcine Interleukin 12 homodimer (IL-12p80) is formed from two subunits of Interleukin 12 subunit beta (IL12B, IL-12p40), stabilized by a disulfide link. The cysteine in position 197 of IL12B is required for homodimer formation. Prolyl 4-hydroxylase subunit beta (P4HB), in this article referred to as protein disulfide isomerase (PDI), can act as a chaperone to induce homodimer formation (Martens et al. 2000). Human cells do not produce IL-12p80 under normal conditions (Ling et al. 1995), when however expressed acts as an antagonist of Interleukin-12 signaling, competing with the Interleukin 12 heterodimer (IL12) for its receptor (Ling et al. 1995).
Literature References
PubMed ID Title Journal Year
7527811 Human IL-12 p40 homodimer binds to the IL-12 receptor but does not mediate biologic activity

Stern, AS, Hollfelder, K, Su, C, Hakimi, J, Gubler, U, Gately, MK, Lin, P, Pan, YC, Ling, P

J. Immunol. 1995
25259790 Recombinant p35 from bacteria can form Interleukin (IL-)12, but Not IL-35

Garbers, C, Plöhn, S, Lang, PA, Grötzinger, J, Lokau, J, Moll, JM, Aparicio-Siegmund, S, Scheller, J, Schröder, J, Grusdat, M, Rose-John, S

PLoS ONE 2014
11054122 Protein disulfide isomerase-mediated cell-free assembly of recombinant interleukin-12 p40 homodimers

Vandenbroeck, K, Billiau, A, Alloza, I, Scott, CJ, Martens, E

Eur. J. Biochem. 2000
Catalyst Activity

protein disulfide isomerase activity of P4HB [endoplasmic reticulum lumen]

Orthologous Events
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