Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation.

Article Details

Citation

Wen Z, Zhong Z, Darnell JE Jr

Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation.

Cell. 1995 Jul 28;82(2):241-50.

PubMed ID
7543024 [ View in PubMed
]
Abstract

Stat1 and Stat3 are latent transcriptional factors activated initially through phosphorylation on single tyrosine residues induced by cytokine and growth factor occupation of cell surface receptors. Here we show that phosphorylation on a single serine (residue 727) in each protein is also required for maximal transcriptional activity. Both cytokines and growth factors are capable of inducing the serine phosphorylation of Stat1 and Stat3. These experiments show that gene activation by Stat1 and Stat3, which obligatorily require tyrosine phosphorylation to become active, also depends for maximal activation on one or more of the many serine kinases.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Signal transducer and activator of transcription 1-alpha/betaP42224Details