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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 [PubMed 10600115]).[supplied by OMIM, Mar 2008].. Additionally we are shipping Leucine Carboxyl Methyltransferase 1 Antibodies (62) and Leucine Carboxyl Methyltransferase 1 Proteins (8) and many more products for this protein.
LCMT1-PME-1 (show PPME1 ELISA Kits) methylation equilibrium is critical for regulating mitotic spindle size and thereby proper cell division
alterations in the membrane localization of PP2A and Tau following down-regulation of LCMT1 may lead to PP2A and Tau dysfunction in AD.
Data indicate that PP2A (show PPP2R4 ELISA Kits) holoenzyme biogenesis and activity are controlled by five PP2A (show PPP2R4 ELISA Kits) modulators, consisting of alpha4, PTPA (show PPP2R4 ELISA Kits), LCMT1, PME-1 (show PPME1 ELISA Kits) and TIPRL1, which serve to prevent promiscuous phosphatase activity until the holoenzyme is completely assembled.
GSK-3beta (show GSK3b ELISA Kits) can inhibit PP2A (show PPP2R4 ELISA Kits) by increasing the inhibitory L309-demethylation involving upregulation of PME-1 (show PPME1 ELISA Kits) and inhibition of PPMT1
determined crystal structures of human LCMT-1 in isolation and in complex with PP2A stabilized by a cofactor mimic. The structures show that the LCMT-1 active-site pocket recognizes the carboxyl terminus of PP2A
X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet (show MAT1A ELISA Kits)) 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, a reported target of the methylation-dependent PP4R1-PP4c complex. Collectively, our data suggest that LCMT-1 coordinately regulates the carboxyl methylation of PP2A-related phosphatases and, consequently, their holoenzyme assembly and function.
In LCMT1 deficiency enzyme activity and methylation of PP2A are reduced in a coordinate fashion, suggesting that LCMT1 is the only PP2A 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