Tyrosine Phosphorylation Profiling in FGF-2 Stimulated Human Embryonic Stem Cells
Author Information
Author(s): Ding Vanessa M. Y., Boersema Paul J., Foong Leong Yan, Preisinger Christian, Koh Geoffrey, Natarajan Subaashini, Lee Dong-Yup, Boekhorst Jos, Snel Berend, Lemeer Simone, Heck Albert J. R., Choo Andre
Primary Institution: Stem Cell Group, Bioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore
Hypothesis
The role of fibroblast growth factor-2 (FGF-2) in maintaining undifferentiated human embryonic stem cells (hESC) was investigated using a targeted phosphoproteomics approach.
Conclusion
The study identified 735 unique tyrosine phosphorylation sites on 430 proteins in hESC, highlighting the importance of FGF-2 signaling in maintaining pluripotency.
Supporting Evidence
- 735 unique tyrosine phosphorylation sites on 430 proteins were identified, the largest inventory to date for hESC.
- All four FGFRs were activated upon FGF-2 stimulation.
- Induced tyrosine phosphorylation of members of both MAPK and PI3-K pathways was observed.
- Src kinase family members were activated by FGF-2, suggesting their role in maintaining undifferentiated hESC.
- Blocking FGFR signaling leads to rapid differentiation of hESC.
Takeaway
Researchers looked at how a growth factor called FGF-2 helps keep stem cells from changing into other types of cells, finding many important changes in proteins when FGF-2 is added.
Methodology
A targeted phosphoproteomics approach was used to profile tyrosine phosphorylation events following FGF-2 stimulation, involving stable isotope dimethyl labeling and LC-MS analysis.
Limitations
The study primarily focused on tyrosine phosphorylation and may not capture other important phosphorylation events.
Digital Object Identifier (DOI)
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