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LCMT1 catalyzes the methylation of the carboxyl group of the C-terminal leucine residue (leu309) of the catalytic subunit of protein phosphatase-2A (PPP2CA; MIM 176915) (De Baere et al., 1999. Additionally we are shipping Leucine Carboxyl Methyltransferase 1 Proteins (8) and many more products for this protein.
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LCMT1-PME-1 (show PPME1 Antibodies) methylation equilibrium is critical for regulating mitotic spindle size and thereby proper cell division
alterations in the membrane localization of PP2A (show PPP2R4 Antibodies) and Tau following down-regulation of LCMT1 may lead to PP2A (show PPP2R4 Antibodies) and Tau dysfunction in AD.
Data indicate that PP2A (show PPP2R4 Antibodies) holoenzyme biogenesis and activity are controlled by five PP2A (show PPP2R4 Antibodies) modulators, consisting of alpha4, PTPA (show PPP2R4 Antibodies), LCMT1, PME-1 (show PPME1 Antibodies) and TIPRL1, which serve to prevent promiscuous phosphatase activity until the holoenzyme is completely assembled.
GSK-3beta (show GSK3b Antibodies) can inhibit PP2A (show PPP2R4 Antibodies) by increasing the inhibitory L309-demethylation involving upregulation of PME-1 (show PPME1 Antibodies) and inhibition of PPMT1
determined crystal structures of human LCMT-1 in isolation and in complex with PP2A (show PPP2R4 Antibodies) stabilized by a cofactor mimic. The structures show that the LCMT-1 active-site pocket recognizes the carboxyl terminus of PP2A (show PPP2R4 Antibodies)
X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet (show MAT1A Antibodies)) has been solved to a resolution of 2 A.
LCMT-1 is important for normal progression through mitosis and cell survival and is essential for embryonic development
LCMT-1 homozygous knock-out MEFs exhibited hyperphosphorylation of HDAC3 (show HDAC3 Antibodies), a reported target of the methylation-dependent PP4R1 (show PPP4R1 Antibodies)-PP4c (show PPP4C Antibodies) complex. Collectively, our data suggest that LCMT-1 coordinately regulates the carboxyl methylation of PP2A (show PPP2R2B Antibodies)-related phosphatases and, consequently, their holoenzyme assembly and function.
In LCMT1 deficiency enzyme activity and methylation of PP2A (show PPP2R2B Antibodies) are reduced in a coordinate fashion, suggesting that LCMT1 is the only PP2A (show PPP2R2B Antibodies) methyltransferase.
Enhanced expression of LCMT1 in cultured neuroblastoma cells, which increases endogenous methylated catalytic C subunit and Balpha levels, induces changes in F-actin organization.
LCMT1 catalyzes the methylation of the carboxyl group of the C-terminal leucine residue (leu309) of the catalytic subunit of protein phosphatase-2A (PPP2CA\; MIM 176915) (De Baere et al., 1999
leucine carboxyl methyltransferase 1
, [Phosphatase 2A protein]-leucine-carboxy methyltransferase 1
, protein phosphatase methyltransferase 1
, protein-leucine O-methyltransferase