Glycogen synthase kinase-3ß regulates leucine-309 demethylation of protein phosphatase-2A via PPMT1 and PME-1.
FEBS Lett
; 586(16): 2522-8, 2012 Jul 30.
Article
in En
| MEDLINE
| ID: mdl-22732552
ABSTRACT
Protein phosphatase-2A (PP2A) activity is significantly suppressed in Alzheimer's disease. We have reported that glycogen synthase kinase-3ß (GSK-3ß) inhibits PP2A via upregulating the phosphorylation of PP2A catalytic subunit (PP2A(C)). Here we studied the effects of GSK-3ß on the inhibitory demethylation of PP2A at leucine-309 (dmL309-PP2A(C)). We found that GSK-3ß regulates dmL309-PP2A(C) level by regulating PME-1 and PPMT1. Knockdown of PME-1 or PPMT1 eliminated the effects of GSK-3ß on PP2A(C). GSK-3 could negatively regulate PP2A regulatory subunit protein level. We conclude that GSK-3ß can inhibit PP2A by increasing the inhibitory L309-demethylation involving upregulation of PME-1 and inhibition of PPMT1.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carboxylic Ester Hydrolases
/
Glycogen Synthase Kinase 3
/
Protein Phosphatase 2
/
Leucine
Limits:
Humans
Language:
En
Journal:
FEBS Lett
Year:
2012
Type:
Article