Genomes and Genes
- Pore-forming activity of BAD is regulated by specific phosphorylation and structural transitions of the C-terminal partLisa Polzien
Theodor Boveri Institute, Department of Microbiology, University of Wuerzburg, 97074 Wuerzburg, Germany
Biochim Biophys Acta 1810:162-9. 2011..Since the functional role of the BAD C-terminal part has not been considered so far, we have investigated here the interplay of the structure and function of this region...
- BAD contributes to RAF-mediated proliferation and cooperates with B-RAF-V600E in cancer signalingLisa Polzien
Department of Microbiology, Biocenter, University of Wurzburg, 97074 Wurzburg, Germany
J Biol Chem 286:17934-44. 2011..Collectively, our findings provide new insights into the regulation of BAD function by phosphorylation and its role in cancer signaling...
- Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylationLisa Polzien
Institute for Medical Radiation and Cell Research, University of Wuerzburg, 97078 Wuerzburg, Germany
J Biol Chem 284:28004-20. 2009..This pore-forming capacity was dependent on phosphorylation status and interaction with 14-3-3 proteins. Collectively, our findings provide new insights into the regulation of BAD function by phosphorylation...
- Single substitution within the RKTR motif impairs kinase activity but promotes dimerization of RAF kinaseAngela Baljuls
Theodor Boveri Institute of Bioscience, Department of Microbiology, University of Wuerzburg, Wuerzburg, Germany
J Biol Chem 286:16491-503. 2011..In summary, we provide evidence that each of the basic residues within the RKTR motif is indispensable for correct RAF function...