STAT3 revs up the powerhouse.
Tyrosine phosphorylation of signal transducers and activators of transcription (STATs) promotes their dimerization and ability to bind target genes in the nucleus. However, evidence shows that one member of the STAT family, STAT3, has an additional property independent of its classical role in the nucleus. STAT3 modifed by serine phosphorylation augmented oxidative phosphorylation in mitochondria and supported cellular transformation by oncogenic Ras.
Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794, USA. nancy.reich@stonybrook.edu
Nancy C
NC
Reich
D000818:Animals; D002471:Cell Transformation, Neoplastic; D011905:Genes, ras; D006801:Humans; D008928:Mitochondria / Q000378:metabolism; D008954:Models, Biological; D009857:Oncogenes; D010085:Oxidative Phosphorylation; D010766:Phosphorylation; D050796:STAT3 Transcription Factor / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D012694:Serine / Q000737:chemistry; D015398:Signal Transduction / Q000502:physiology*; D014443:Tyrosine / Q000737:chemistry; D018631:ras Proteins / Q000378:metabolism
D050796:STAT3 Transcription Factor; D014443:Tyrosine; D012694:Serine; D018631:ras Proteins