非经典途径不依赖IKK，而是依赖Tyr42上的IκBα磷酸化或IκBα

The non-canonical pathway does not depend on IKK, but on IκBα phosphorylation on Tyr42 or on Ser residues in the IκBα PEST domain to activate IKKα through NF-κB-inducible kinase (NIK), while the NIK-IKKα complex phosphorylates the p100 subunit base, p100 can be processed in a proteasome-dependent manner to generate the p52 subunit. <br>Through phosphorylation of the p100 subunit by the NIK-IKKα complex, p100 can be processed in a proteasome-dependent manner to generate the p52 subunit.

The nonclassical pathway does not depend on IKK, but on I on tyr42 κ B α Phosphorylation or I κ B α Ser residues in pest domain pass through NF- κ B-induced kinase (Nik) activates IKK α， Meanwhile, nik-ikk α The complex phosphorylates P100 subunit, which can be processed in a proteasome dependent manner to produce p52 subunit.<br>Through nik-ikk α The complex phosphorylates P100 subunit, which can be processed in a proteasome dependent manner to produce p52 subunit.

The classical approach does not depend on IKK, but on IκBα phosphorylation on Tyr42 or Ser residues in IκBα PEST domain to activate IKKα through NF-κB-induced kinase (NIK). At the same time, NIK-IKKα complex phosphorylates p100 subunit, which can be processed in a proteasome-dependent manner to produce p52 subunit. P100 can be processed in a proteasome-dependent manner by phosphorylation of p100 subunit by NIK-IKKα complex, resulting in p52 subunit.