Title :
Snail1 is stabilized by O-GlcNAc modification in hyperglycaemic condition
Abstract :
- Protein O-phosphorylation often occurs reciprocally with O-GlcNAc modification and represents a regulatory principle for proteins
- O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1 , a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition ( EMT ) programme, results in its proteasomal degradation
- We show that by suppressing O-phosphorylation-mediated degradation, O-GlcNAc at serine112 stabilizes Snail1 and thus increases its repressor function, which in turn attenuates E-cadherin mRNA expression
- Hyperglycaemic condition enhances O-GlcNAc modification and initiates EMT by transcriptional suppression of E-cadherin through Snail1
- Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT
Output (sent_index, trigger,
protein,
sugar,
site):
- 3. serine112, , -, O-GlcNAc, serine112
- 5. EMT, , EMT, cellular glucose metabolism, -
- 5. Snail1, , Snail1, O-GlcNAc modification, -
- 5. modification, , Snail1, O-GlcNAc modification, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 3. Snail1, O-GlcNAc, serine112