Interaction between O-GlcNAc Modification and Tyrosine Phosphorylation of Prohibitin: Implication for a Novel Binary Switch
2009
Interaction between O-GlcNAc Modification and Tyrosine Phosphorylation of Prohibitin
publication
Evidence: moderate
Author Information
Author(s): Ande Sudharsana R., Moulik Saby, Mishra Suresh
Primary Institution: University of Manitoba
Hypothesis
O-GlcNAc modification and tyrosine phosphorylation of prohibitin play an important role in signaling pathways.
Conclusion
The study suggests that O-GlcNAc modification and tyrosine phosphorylation of prohibitin interact and may act as a binary switch in cell signaling.
Supporting Evidence
- Prohibitin interacts with O-linked β-N-acetylglucosamine transferase (OGT) and is modified by O-GlcNAc.
- Insulin treatment enhances O-GlcNAc modification of prohibitin.
- Mutations in prohibitin affect its phosphorylation and O-GlcNAc modification.
Takeaway
This study shows that two chemical changes in a protein can work together like a switch to help cells respond to signals like insulin.
Methodology
The study used co-immunoprecipitation, confocal microscopy, and various biochemical assays to analyze the interactions and modifications of prohibitin.
Digital Object Identifier (DOI)
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