Pseudophosphatase STYX modulates cell-fate decisions and cell migration by spatiotemporal regulation of ERK1/2
Copyright policy )Pseudophosphatase STYX modulates cell-fate decisions and cell migration by spatiotemporal regulation of ERK1/2
Significance The role of catalytically inactive phosphatases (pseudophosphatases) remains enigmatic. Using a combination of experiments and modeling, we identified the pseudophosphatase serine/threonine/tyrosine-interacting protein (STYX) as a nuclear anchor and modulator of ERK signaling. Thereby, STYX regulates the morphology of the Golgi apparatus and its polarization in migrating cells. Consequently, STYX influences directional cell motility, a process that determines the invasive and metastatic ability of cancer cells. By controlling spatiotemporal ERK signaling, STYX plays a role in cell-fate decisions, such as PC12 cell differentiation.
- University College Dublin Ireland
- University of Konstanz Germany
- Biotechnology Institute Thurgau Switzerland
Cell Nucleus, Mitogen-Activated Protein Kinase 1, 570, Mitogen-Activated Protein Kinase 3, MAP Kinase Signaling System, Intracellular Signaling Peptides and Proteins, Golgi Apparatus, Nuclear Proteins, Computational modeling, Cell Differentiation, MAPK, PC12 Cells, Rats, Enzyme Activation, Cell Movement, Gene Knockdown Techniques, Animals, Dual-Specificity Phosphatases, Humans, Mitogen-Activated Protein Kinase Phosphatases, Carrier Proteins
Cell Nucleus, Mitogen-Activated Protein Kinase 1, 570, Mitogen-Activated Protein Kinase 3, MAP Kinase Signaling System, Intracellular Signaling Peptides and Proteins, Golgi Apparatus, Nuclear Proteins, Computational modeling, Cell Differentiation, MAPK, PC12 Cells, Rats, Enzyme Activation, Cell Movement, Gene Knockdown Techniques, Animals, Dual-Specificity Phosphatases, Humans, Mitogen-Activated Protein Kinase Phosphatases, Carrier Proteins
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