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Full-Text Articles in Medicine and Health Sciences
Phosphoproteomics Profiling Of Nonsmall Cell Lung Cancer Cells Treated With A Novel Phosphatase Activator, Danica Wiredja, Marzieh Ayati, Sahar Mazhar, Jaya Sangodkar, Sean Maxwell, Daniela Schlatzer, Goutham Narla, Mehmet Koyutürk, Mark R. Chance
Phosphoproteomics Profiling Of Nonsmall Cell Lung Cancer Cells Treated With A Novel Phosphatase Activator, Danica Wiredja, Marzieh Ayati, Sahar Mazhar, Jaya Sangodkar, Sean Maxwell, Daniela Schlatzer, Goutham Narla, Mehmet Koyutürk, Mark R. Chance
Computer Science Faculty Publications and Presentations
Activation of protein phosphatase 2A (PP2A) is a promising anti-cancer therapeutic strategy, as this tumor suppressor has the ability to coordinately downregulate multiple pathways involved in the regulation of cellular growth and proliferation. In order to understand the systems-level perturbations mediated by PP2A activation, we carried out mass spectrometry-based phosphoproteomic analysis of two KRAS mutated non-small cell lung cancer (NSCLC) cell lines (A549 and H358) treated with a novel Small Molecule Activator of PP2A (SMAP). Overall, this permitted quantification of differential signaling across over 1,600 phosphoproteins and 3,000 phosphosites. Kinase activity assessment and pathway enrichment implicated collective downregulation of RAS …
Calmodulin Lobes Facilitate Dimerization And Activation Of Estrogen Receptor-Alpha, Zhigang Li, Yonghong Zhang, Andrew C. Hedman, James B. Ames, David B. Sacks
Calmodulin Lobes Facilitate Dimerization And Activation Of Estrogen Receptor-Alpha, Zhigang Li, Yonghong Zhang, Andrew C. Hedman, James B. Ames, David B. Sacks
Chemistry Faculty Publications and Presentations
Estrogen receptor α (ER-α) is a nuclear hormone receptor that controls selected genes, thereby regulating proliferation and differentiation of target tissues, such as breast. Gene expression controlled by ER-α is modulated by Ca2+ via calmodulin (CaM). Here we present the NMR structure of Ca2+-CaM bound to two molecules of ER-α (residues 287–305). The two lobes of CaM bind to the same site on two separate ER-α molecules (residues 292, 296, 299, 302, and 303), which explains why CaM binds two molecules of ER-α in a 1:2 complex and stabilizes ER-α dimerization. Exposed glutamate residues in CaM (Glu-11, …