Title | Requirement of serine phosphorylation for formation of STAT-promoter complexes. |
Publication Type | Journal Article |
Year of Publication | 1995 |
Authors | Zhang X, Blenis J, Li HC, Schindler C, Chen-Kiang S |
Journal | Science |
Volume | 267 |
Issue | 5206 |
Pagination | 1990-4 |
Date Published | 1995 Mar 31 |
ISSN | 0036-8075 |
Keywords | 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cell Nucleus, Ciliary Neurotrophic Factor, Cytoplasm, DNA, DNA-Binding Proteins, Humans, Interleukin-6, Isoquinolines, Mice, Molecular Sequence Data, Nerve Tissue Proteins, Phosphorylation, Piperazines, Promoter Regions, Genetic, Serine, Signal Transduction, STAT1 Transcription Factor, STAT3 Transcription Factor, Threonine, Trans-Activators, Tumor Cells, Cultured, Tyrosine |
Abstract | Members of the interleukin-6 family of cytokines bind to and activate receptors that contain a common subunit, gp130. This leads to the activation of Stat3 and Stat1, two cytoplasmic signal transducers and activators of transcription (STATs), by tyrosine phosphorylation. Serine phosphorylation of Stat3 was constitutive and was enhanced by signaling through gp130. In cells of lymphoid and neuronal origins, inhibition of serine phosphorylation prevented the formation of complexes of DNA with Stat3-Stat3 but not with Stat3-Stat1 or Stat1-Stat1 dimers. In vitro serine dephosphorylation of Stat3 also inhibited DNA binding of Stat3-Stat3. The requirement of serine phosphorylation for Stat3-Stat3.DNA complex formation was inversely correlated with the affinity of Stat3-Stat3 for the binding site. Thus, serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3.DNA complexes. |
DOI | 10.1126/science.7701321 |
Alternate Journal | Science |
PubMed ID | 7701321 |
Grant List | CA46595 / CA / NCI NIH HHS / United States HL 21006 / HL / NHLBI NIH HHS / United States |
Related Lab:
Related Faculty:
Selina Chen-Kiang, Ph.D.