Stat1 Phosphorylation Determines Ras Oncogenicity by Regulating p27Kip1
نویسندگان
چکیده
منابع مشابه
Stat1 Phosphorylation Determines Ras Oncogenicity by Regulating p27Kip1
Inactivation of p27 Kip1 is implicated in tumorigenesis and has both prognostic and treatment-predictive values for many types of human cancer. The transcription factor Stat1 is essential for innate immunity and tumor immunosurveillance through its ability to act downstream of interferons. Herein, we demonstrate that Stat1 functions as a suppressor of Ras transformation independently of an inte...
متن کاملRegulation of RAS oncogenicity by acetylation.
Members of the RAS small GTPase family regulate cellular responses to extracellular stimuli by mediating the flux through downstream signal transduction cascades. RAS activity is strongly dependent on its subcellular localization and its nucleotide-binding status, both of which are modulated by posttranslational modification. We have determined that RAS is posttranslationally acetylated on lysi...
متن کاملSTAT1 represses Skp2 gene transcription to promote p27Kip1 stabilization in Ras-transformed cells.
The S-phase kinase-associated protein 2 (Skp2) is an F-box protein that serves as a subunit of the Skp1-Cullin-F-box ubiquitin protein ligase complex. Skp2 is overexpressed in many tumors and promotes tumor formation through its ability to induce the degradation of proteins with antiproliferative and tumor-suppressor functions, such as p27(Kip1). The signal transducer and activator of transcrip...
متن کاملRetinoic acid induces p27Kip1 nuclear accumulation by modulating its phosphorylation.
All-trans-retinoic acid (ATRA), the most biologically active metabolite of vitamin A, controls cell proliferation, apoptosis, and differentiation depending on the cellular context. These activities point to ATRA as a candidate for cancer therapy. A pivotal effect of the molecule is the modulation of p27Kip1, a cyclin-dependent kinase (CDK) inhibitor (CDKI). Here, we investigate the mechanisms b...
متن کاملSTAT1 signaling is not regulated by a phosphorylation-acetylation switch.
The treatment of cells with histone deacetylase inhibitors (HDACi) was reported to reveal the acetylation of STAT1 at lysine 410 and lysine 413 (O. H. Krämer et al., Genes Dev. 20:473-485, 2006). STAT1 acetylation was proposed to regulate apoptosis by facilitating binding to NF-κB and to control immune responses by suppressing STAT1 tyrosine phosphorylation, suggesting that STAT1 acetylation is...
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ژورنال
عنوان ژورنال: PLoS ONE
سال: 2008
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0003476