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Article

Regulation of erythropoietin-induced STAT serine phosphorylation by distinct mitogen-activated protein kinases.

The Journal of biological chemistry - 10 May 2002

Haq Rizwan, Halupa Adrienne, Beattie Bryan K, Mason Jacqueline M, Zanke Brent W, Barber Dwayne L

Abstract excerpt

The STAT proteins are a family of latent transcription factors that are activated by a wide variety of cytokines. Upon receptor engagement, STATs become tyrosine phosphorylated, translocate to the nucleus, and induce expression of target genes. In addition to tyrosine phosphorylation, maximal activation of some STAT proteins requires serine phosphorylation within the transactivation domain. Here we focus on STAT...

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Source

Identifiers

PMID: 11875080
DOI: 10.1074/jbc.M201842200

Genes

EPO
STAT1
STAT3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Regulation of erythropoietin-induced STAT serine phosphorylation by distinct mitogen-activated protein kinases.PMID 11875080Read ↗

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