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The Transcriptional Factor Tcf-4 Contains Different Binding Sites for β-Catenin and Plakoglobin*
- S. Miravet, J. Piedra, F. Miró, E. Itarte, A. García de Herreros, M. Duñach
- Biology, ChemistryThe Journal of Biological Chemistry
- 18 January 2002
It is shown here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58–Ser-59– Ser-60, and that simultaneous binding of the two armadillo proteins to TCF-4 is possible.
Osmotic Stress Regulates the Stability of Cyclin D1 in a p38SAPK2-dependent Manner*
- O. Casanovas, F. Miró, J. M. Estanyol, E. Itarte, N. Agell, O. Bachs
- BiologyThe Journal of Biological Chemistry
- 10 November 2000
It is found that p38SAPK2 phosphorylates cyclin D1 in vitro at Thr286 and that this phosphorylation triggers the ubiquitination of cyclin L1, which will help to understand the molecular mechanisms by which stress transduction pathways regulate the cell cycle machinery and take control over cell proliferation.
PP1/PP2A phosphatases inhibitors okadaic acid and calyculin A block ERK5 activation by growth factors and oxidative stress
HAVCR/KIM-1 activates the IL-6/STAT-3 pathway in clear cell renal cell carcinoma and determines tumor progression and patient outcome.
The results suggest that HAVCR/KIM-1 upregulation in tumors might represent a novel mechanism to activate tumor growth and angiogenesis and that pSTAT-3 S727 is an independent prognostic factor for ccRCC patients.
Phosphorylation of maize RAB-17 protein by casein kinase 2.
Hepatitis A virus cellular receptor 1/kidney injury molecule-1 is a susceptibility gene for clear cell renal cell carcinoma and hepatitis A virus cellular receptor/kidney injury molecule-1 ectodomain…
Apigenin and LY294002 prolong EGF‐stimulated ERK1/2 activation in PC12 cells but are unable to induce full differentiation
The regulatory beta subunit of protein kinase CK2 contributes to the recognition of the substrate consensus sequence. A study with an eIF2 beta-derived peptide.
Results demonstrate that this peptide still displays phosphorylation features similar to full-length eIF2beta and the CK2 beta subunit also contributes to recognition of the protein substrate by establishing both polar and hydrophobic interactions with specificity determinants located downstream from the phosphoacceptor site.
Unbalanced activation of ERK1/2 and MEK1/2 in apigenin-induced HeLa cell death.