JAK-STAT signaling pathway
A cellular signaling system in which cytokine receptors activate Janus kinases, which activate STAT proteins that regulate gene expression.
Cytokine receptor: A cell-surface receptor that binds a cytokine and initiates intracellular signaling. Cytokine binding brings receptor-associated Janus kinases into an activating arrangement.
Cytokine: A small signaling protein that helps cells communicate, especially in immune and inflammatory responses. Cytokines are the extracellular signals that commonly initiate this pathway.
Interferon signaling: Cellular responses to interferons, including antiviral, immune-regulatory, and growth-inhibitory effects. Interferons use JAK-STAT signaling to induce many of their characteristic gene programs.
MAPK/ERK pathway: A kinase cascade that regulates processes including cell growth, differentiation, and survival. It is a distinct signaling route that often operates alongside cytokine-activated JAK-STAT.
Janus kinase: A family of non-receptor tyrosine kinases that transmit signals from cytokine receptors. JAKs phosphorylate receptor tails and STAT proteins after receptor activation.
Receptor tyrosine kinase: A cell-surface receptor whose own intracellular domain has tyrosine kinase activity. Unlike these receptors, cytokine receptors generally rely on separate, receptor-associated JAK enzymes.
Interleukin-6: A cytokine that regulates inflammation, immune responses, and aspects of blood-cell production. Its receptor activates JAK-STAT signaling and contributes to inflammatory disease.
NF-κB: A family of transcription factors central to immune, inflammatory, and stress-response gene regulation. Many inflammatory signals activate NF-κB rather than, or alongside, JAK-STAT.
STAT protein: A signal-responsive transcription factor activated by phosphorylation and regulated dimerization. STAT proteins carry the receptor-generated signal into the nucleus.
SH2 domain: A protein domain that binds phosphotyrosine-containing sequences. STAT SH2 domains recognize phosphorylated receptor sites and promote STAT dimerization.