Negative regulation of cytokine signaling by the SOCS proteins
NA Nicola, SE Nicholson, D Metcalf… - Cold Spring Harbor …, 1999 - symposium.cshlp.org
Cold Spring Harbor Symposia on Quantitative Biology, 1999•symposium.cshlp.org
Figure 1. Negative regulation of the cytokine-activated JAK/STAT signaling pathway.
Receptor aggregation by cytokine leads to cross-phosphorylation and activation of the
tyrosine kinase activity of associated JAKs which also phosphorylate the receptors. STATs
bind to these sites, are phosphorylated, dissociate from the receptor and form dimers that
translocate to the nucleus, and activate transcription. Transcription of SOCS genes also
occurs, and the proteins either inhibit JAK activity or bind to the receptor and block further …
Receptor aggregation by cytokine leads to cross-phosphorylation and activation of the
tyrosine kinase activity of associated JAKs which also phosphorylate the receptors. STATs
bind to these sites, are phosphorylated, dissociate from the receptor and form dimers that
translocate to the nucleus, and activate transcription. Transcription of SOCS genes also
occurs, and the proteins either inhibit JAK activity or bind to the receptor and block further …
Figure 1. Negative regulation of the cytokine-activated JAK/STAT signaling pathway. Receptor aggregation by cytokine leads to cross-phosphorylation and activation of the tyrosine kinase activity of associated JAKs which also phosphorylate the receptors. STATs bind to these sites, are phosphorylated, dissociate from the receptor and form dimers that translocate to the nucleus, and activate transcription. Transcription of SOCS genes also occurs, and the proteins either inhibit JAK activity or bind to the receptor and block further association of STATs. In addition, the tyrosine phosphatase SHP-1 can deactivate JAKs and the receptor, whereas PIAS proteins bind to activated STATs and inhibit transcriptional activation.
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