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617 results on '"Ottmann, C."'

7. Small molecule stabilizer for ERalpha and 14-3-3 (1075306)

Author

Konstantinidou, M., primary, Visser, E.J., additional, Vandenboorn, E.M.F., additional, Sheng, C., additional, Jaishankar, P., additional, Overmans, M.J.A.M., additional, Dutta, S., additional, Neitz, J., additional, Renslo, A., additional, Ottmann, C., additional, Brunsveld, L., additional, and Arkin, M., additional

Published
2023
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14. New Compound Classes: Protein–Protein Interactions

Author

Ottmann, C., Rosenthal, Walter, Editor-in-chief, Barrett, James E., Series editor, Flockerzi, Veit, Series editor, Frohman, Michael A., Series editor, Geppetti, Pierangelo, Series editor, Hofmann, Franz B., Series editor, Michel, Martin C., Series editor, Page, Clive P., Series editor, Thorburn, Andrew M., Series editor, Wang, KeWei, Series editor, Nielsch, Ulrich, editor, Fuhrmann, Ulrike, editor, and Jaroch, Stefan, editor

Published
2016
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15. Understanding the interaction of 14-3-3 proteins with hDMX and hDM2

Author

Srdanović, S, Wolter, M, Trinh, CH, Ottmann, C, Warriner, SL, Wilson, AJ, Chemical Biology, and ICMS Core

Subjects
Nuclear Proteins, Cell Cycle Proteins, Proto-Oncogene Proteins c-mdm2, 14-3-3 proteins, Cell Biology, Biochemistry, Proto-Oncogene Proteins, hDM2 and hDMX, Humans, structural biology, Tumor Suppressor Protein p53, p53 pathway, Molecular Biology, Protein Binding
Abstract

p53 plays a critical role in regulating diverse biological processes: DNA repair, cell cycle arrest, apoptosis and senescence. The p53 pathway has therefore served as the focus of multiple drug-discovery efforts. p53 is negatively regulated by hDMX and hDM2; prior studies have identified 14-3-3 proteins as hDMX and hDM2 client proteins. 14-3-3 proteins are adaptor proteins that modulate localization, degradation and interactions of their targets in response to phosphorylation. Thus, 14-3-3 proteins may indirectly modulate the interaction between hDMX or hDM2 and p53 and represent potential targets for modulation of the p53 pathway. In this manuscript, we report on the biophysical and structural characterization of peptide/protein interactions that are representative of the interaction between 14-3-3 and hDMX or hDM2. The data establish that proximal phosphosites spaced ~20–25 residues apart in both hDMX and hDM2 co-operate to facilitate high-affinity 14-3-3 binding and provide structural insight that can be utilized in future stabilizer/inhibitor discovery efforts.

Published
2022

17. Small molecule stabilizer (compound 2) for FOXO1 and 14-3-3

Author

Kenanova, D.N., primary, Visser, E.J., additional, Virta, J., additional, Sijbesma, E., additional, Centorrino, F., additional, Zhong, M., additional, Vickery, H., additional, Neitz, J., additional, Brunsveld, L., additional, Ottmann, C., additional, and Arkin, M.R., additional

Published
2023
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36. Fusicoccin-A Targets Cancerous Inhibitor of Protein Phosphatase 2A by Stabilizing a C-Terminal Interaction with 14-3-3

Author

Brink, H.J., Van Senten, J.R., De Vries-Van Leeuwen, I.J., Da Costa Pereira, D., Piersma, S.R., Jimenez, C.R., Centorrino, F., Ottmann, C., Siderius, M., Smit, M.J., De Boer, A.H., Brink, H.J., Van Senten, J.R., De Vries-Van Leeuwen, I.J., Da Costa Pereira, D., Piersma, S.R., Jimenez, C.R., Centorrino, F., Ottmann, C., Siderius, M., Smit, M.J., and De Boer, A.H.

Abstract

The cancerous inhibitor of protein phosphatase 2A (CIP2A) is an oncoprotein found overexpressed in many types of cancer. CIP2A has been shown to stabilize oncoproteins such as cMYC by shielding them from PP2A-mediated dephosphorylation. Here we report that the penultimate residue Ser904 in the C-terminus of CIP2A can be phosphorylated to create a binding site for the regulatory protein 14-3-3. We demonstrate that 14-3-3 is a new interaction partner of CIP2A. The 14-3-3/CIP2A C-terminal interaction complex can be targeted by the protein-protein interaction (PPI) stabilizer fusicoccin-A (FC-A), resulting in enhanced levels of phosphorylated Ser904. FC-A treatment of TNBC cells leads to the increased association of CIP2A with 14-3-3. We show that the composite interface between 14 and 3-3 and CIP2A's C-terminus can be targeted by the PPI stabilizer FC-A, providing a new interface that could potentially be exploited to modulate CIP2A's activity.

Published
2022
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