Introduction
Two NF-κB signaling pathways have been identified including classical and non-canonical activation pathways.
The classical signaling pathway is mainly triggered by the combination of the ligands and T cell receptor (TCR), B cell receptor (BCR) or toll-like receptor (TLR) - interleukin-1 receptor (IL-1R) family members. And it terminates in the transcription of target genes encoding chemokines, cytokines, adhesion molecules, inflammatory responses, and cell survival.
When the cells are in a resting state, NF-κB usually binds to the inhibitory proteins IκBs (IκBα, IκBβ, IκBε) and exists in the cytoplasm in an inactive form and the combination of the two masks the nuclear localization signal of NF-κB. When the cells are stimulated, the inducer of NF-κB activates the IKK in the cytoplasm through the cell membrane to phosphorylate the serine at positions 32 and 36 of IκBα. Phosphorylated IκB is rapidly ubiquitinated by ubiquitin-binding enzymes and is rapidly degraded by the 26s proteasome. The free NF-κB in the cytoplasm is transported into the nucleus and binds to the NF-κB binding site in the promoter region of the DNA molecule target gene, thereby initiating transcription of the target gene to generate corresponding mRNA and protein.
The classical signaling pathway is mainly triggered by the combination of the ligands and T cell receptor (TCR), B cell receptor (BCR) or toll-like receptor (TLR) - interleukin-1 receptor (IL-1R) family members. And it terminates in the transcription of target genes encoding chemokines, cytokines, adhesion molecules, inflammatory responses, and cell survival.
When the cells are in a resting state, NF-κB usually binds to the inhibitory proteins IκBs (IκBα, IκBβ, IκBε) and exists in the cytoplasm in an inactive form and the combination of the two masks the nuclear localization signal of NF-κB. When the cells are stimulated, the inducer of NF-κB activates the IKK in the cytoplasm through the cell membrane to phosphorylate the serine at positions 32 and 36 of IκBα. Phosphorylated IκB is rapidly ubiquitinated by ubiquitin-binding enzymes and is rapidly degraded by the 26s proteasome. The free NF-κB in the cytoplasm is transported into the nucleus and binds to the NF-κB binding site in the promoter region of the DNA molecule target gene, thereby initiating transcription of the target gene to generate corresponding mRNA and protein.
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