EC Number   |
General Information |
Reference |
|---|
   2.1.1.233 | malfunction |
a dominant-negative leucine carboxyl methyltransferase 1 mutant attenuates the cell cycle without causing cell death, likely by inhibiting uncontrolled phosphatase activity |
716219 |
| 2.1.1.233 | malfunction |
alpha-synuclein (alpha-syn) overexpression induces increased alpha-syn phosphorylation at Ser129, and protein phosphatase 2A (PP2A) inhibition, in vitro and in vivo. alpha-Syn overexpression results in PP2A demethylation. This demethylation is mediated via downregulated leucine carboxyl methyltransferase (LCMT-1) expression, and upregulated protein phosphatase methylesterase (PME-1, EC 3.1.1.89) expression. Furthermore, LCMT-1 overexpression, or PME-1 inhibition, reverses alpha-syn-induced increases in alpha-syn phosphorylation and apoptosis |
-, 750614 |
| 2.1.1.233 | malfunction |
decreased phosphatase 2A protein catalytic subunit methylation is linked with decreased LCMT-1 expression causing human heart failure, overview |
722804 |
| 2.1.1.233 | malfunction |
deletion of phosphatase 2A protein methyltransferase PPM1 greatly reduces Cdc55p, Tpd3p, and Rts1p binding and leads to nocodazole sensitivity |
715450 |
| 2.1.1.233 | malfunction |
depletion of leucine carboxyl methyltransferase-1, LCMT1, or overexpression of protein phosphatase methylesterase-1, PME-1, lead to long spindles. In contrast, depletion of PME-1, pharmacological inhibition of PME-1 or overexpression of LCMT1 lead to short spindles. Perturbation of the LCMT1-PME-1 methylation equilibrium leads to mitotic arrest, spindle assembly checkpoint activation, defective cell divisions, induction of apoptosis and reduced cell viability, phenotype, overview |
735900 |
| 2.1.1.233 | malfunction |
homozygous gene trap knock-out of leucine carboxyl methyltransferase-1 in mice results in embryonic lethality |
715490 |
| 2.1.1.233 | malfunction |
hypomorphic Lcmt1 mice show reduced protein phosphatase 2A methyltransferase expression due to splicing around the insertion, Lcmt1 transcript and LCMT1 protein levels are reduced but not eliminated. LCMT1 activity and methylation of protein phosphatase 2A are reduced in a coordinate fashion, suggesting that LCMT1 is the only PP2A methyltransferase. The mice exhibit an insulin-resistance phenotype. Knockout of Lcmt1 in mice is lethal during embryonic development. Male Lcmt1-/- animals display increased glucose-stimulated insulin secretion, increased insulin resistance, and decreased methylation of phosphatase 2A protein |
737114 |
| 2.1.1.233 | malfunction |
increased expression of NNMT selectively affects LCMT1 resulting in lower PP2A activation. Decreased LCMT1 expression or SAH concentration decreases endogenous activated PP2A |
756498 |
| 2.1.1.233 | malfunction |
leucine carboxyl methyltransferase-1 (LCMT-1) knockdown reduces the formation of protein phosphatase 2A heterotrimers containing the Balpha regulatory subunit and, in a subset of the cells, induces apoptosis, characterized by caspase activation, nuclear condensation/fragmentation, and membrane blebbing. LCMT-1 knockdown cells are more sensitive to the spindle-targeting drug nocodazole |
715490 |
| 2.1.1.233 | malfunction |
mouse embryonic fibroblasts derived from LCMT-1 knock-out mouse embryos have reduced levels of PP2A B regulatory subunit and PP4R1 relative to control mouse embryonic fibroblasts, indicating that LCMT-1 is important for maintaining normal levels of these subunits. LCMT-1 homozygous knock-out mouse embryonic fibroblasts exhibit hyperphosphorylation of HDAC3, a reported target of the methylation-dependent PP4R1-PP4c complex |
751067 |
