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Leucine carboxyl methyltransferase 1

leucine carboxyl methyltransferase-1, leucine carboxyl methyltransferase, LCMT-1, protein phosphatase methyltransferase 1, LCMT
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] (from NCBI)
Top mentioned proteins: PP2A, PmeI, CAN, Replication Protein C, V1a
Papers on leucine carboxyl methyltransferase-1
Studies on the function and catalytic mechanism of O-methyltransferases SviOMT02, SviOMT03 and SviOMT06 from Streptomyces virginiae IBL14.
Tong et al., Hefei, China. In Enzyme Microb Technol, Jun 2015
As a result, the nine putative O-methyltransferases belong to methyltransf_2 superfamily, amdomet-MTases superfamily, and leucine carboxyl methyltransferase superfamily, and are phylogenetically close to those of Streptomyces sp. C. The products of genes sviOMT03 and sviOMT06 could catalyze O-methylation of caffeic acid to form ferulic acid.
Cross talk between PI3K-AKT-GSK-3β and PP2A pathways determines tau hyperphosphorylation.
Liu et al., Nantong, China. In Neurobiol Aging, 2015
Upregulation of GSK-3β led to an increase in the methylation and activity of PP2Ac through suppression of protein phosphatase methylesterase-1 expression and phosphorylation of leucine carboxyl methyltransferase 1. PP2A also regulated GSK-3β phosphorylation.
Altered protein phosphatase 2A methylation and Tau phosphorylation in the young and aged brain of methylenetetrahydrofolate reductase (MTHFR) deficient mice.
Bottiglieri et al., Newcastle, Australia. In Front Aging Neurosci, 2013
Relative to wild-type controls, decreased expression levels of PP2A and leucine carboxyl methyltransferase (LCMT1) were primarily observed in the hippocampus and cerebellum, and to a lesser extent in the cortex of young null Mthfr (-/-) and aged heterozygous Mthfr (+/-) mice.
Regulation of PP2AC carboxylmethylation and cellular localisation by inhibitory class G-protein coupled receptors in cardiomyocytes.
Snabaitis et al., Kingston upon Hull, United Kingdom. In Plos One, 2013
In the current study, we show that the enzymatic components that regulate the carboxylmethylation status of PP2AC, leucine carboxylmethyltransferase-1 (LCMT-1) and phosphatase methylesterase-1 (PME-1) are abundantly expressed in, and almost entirely localised in the cytoplasm of ARVM.
Mechanisms of the scaffold subunit in facilitating protein phosphatase 2A methylation.
Xing et al., Madison, United States. In Plos One, 2013
Here we showed that PP2A-specific methyltransferase, LCMT-1, exhibits a higher activity toward the core enzyme (A-C heterodimer) than free PP2Ac, and the A-subunit facilitates PP2A methylation via three distinct mechanisms: 1) stabilization of a proper protein fold and an active conformation of PP2Ac; 2) limiting the space of PP2Ac-tail movement for enhanced entry into the LCMT-1 active site; and 3) weak electrostatic interactions between LCMT-1 and the N-terminal HEAT repeats of the A-subunit.
Leucine carboxyl methyltransferase 1 (LCMT1)-dependent methylation regulates the association of protein phosphatase 2A and Tau protein with plasma membrane microdomains in neuroblastoma cells.
Sontag et al., Newcastle, Australia. In J Biol Chem, 2013
We have reported that altered leucine carboxyl methyltransferase (LCMT1)-dependent PP2A methylation is associated with down-regulation of PP2A holoenzymes containing the Bα subunit (PP2A/Bα) and subsequent accumulation of phosphorylated Tau in N2a cells, in vivo and in AD.
Characterization of streptonigrin biosynthesis reveals a cryptic carboxyl methylation and an unusual oxidative cleavage of a N-C bond.
Lin et al., Shanghai, China. In J Am Chem Soc, 2013
In this pathway, a cryptic methylation of lavendamycin was genetically and biochemically characterized to be catalyzed by a leucine carboxyl methyltransferase StnF2.
Molecular mechanisms underlying cardiac protein phosphatase 2A regulation in heart.
Mohler et al., Columbus, United States. In J Biol Chem, 2013
We show that past global read-outs of cellular PP2A activity more appropriately represent the collective activity of numerous individual PP2A holoenzymes, each displaying a specific subcellular localization (dictated by select PP2A regulatory subunits) as well as local specific post-translational catalytic subunit methylation and phosphorylation events that regulate local and rapid holoenzyme assembly/disassembly (via leucine carboxymethyltransferase 1/phosphatase methylesterase 1 (LCMT-1/PME-1).
Cornel Iridoid Glycoside Attenuates Tau Hyperphosphorylation by Inhibition of PP2A Demethylation.
Zhang et al., Beijing, China. In Evid Based Complement Alternat Med, 2012
However, CIG significantly elevated the activity of PP2A by reducing the demethylation of PP2A catalytic subunit (PP2Ac) at Leu309 and the ratio of PME-1/LCMT in the WT/GFX-treated cells.
Circumventing embryonic lethality with Lcmt1 deficiency: generation of hypomorphic Lcmt1 mice with reduced protein phosphatase 2A methyltransferase expression and defects in insulin signaling.
Clarke et al., Los Angeles, United States. In Plos One, 2012
PP2A assembly is governed by a variety of mechanisms, one of which is carboxyl-terminal methylation of the catalytic subunit by the leucine carboxyl methyltransferase LCMT1.
Glycogen synthase kinase-3β regulates leucine-309 demethylation of protein phosphatase-2A via PPMT1 and PME-1.
Liu et al., Wuhan, China. In Febs Lett, 2012
GSK-3beta can inhibit PP2A by increasing the inhibitory L309-demethylation involving upregulation of PME-1 and inhibition of PPMT1
Acute administration of L-DOPA induces changes in methylation metabolites, reduced protein phosphatase 2A methylation, and hyperphosphorylation of Tau protein in mouse brain.
Sontag et al., Dallas, United States. In J Neurosci, 2012
Modulation of the cellular SAM/SAH ratio can influence activity of methyltransferase enzymes, including leucine carboxyl methyltransferase that specifically methylates Ser/Thr protein phosphatase 2A (PP2A), a major Tau phosphatase.
Circumventing cellular control of PP2A by methylation promotes transformation in an Akt-dependent manner.
Pallas et al., Atlanta, United States. In Neoplasia, 2012
Reversible methylation of PP2Ac by leucine carboxyl methyltransferase 1 (LCMT-1) and protein phosphatase methylesterase 1 (PME-1) differentially regulates B-type subunit binding and thus PP2A function.
Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aα catalytic subunit.
Zanchin et al., Campinas, Brazil. In J Biol Chem, 2012
The catalytic subunit can also interact with α4, TIPRL (TIP41, TOR signaling pathway regulator-like), the methyl-transferase LCMT-1, and the methyl-esterase PME-1.
The structural basis for tight control of PP2A methylation and function by LCMT-1.
Xing et al., Madison, United States. In Mol Cell, 2011
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
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.
Djordjevic et al., London, United Kingdom. In Acta Crystallogr D Biol Crystallogr, 2011
X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 A.
Methylation of a phosphatase specifies dephosphorylation and degradation of activated brassinosteroid receptors.
Chory et al., Los Angeles, United States. In Sci Signal, 2010
SBI1 mRNA was induced by BRs, and SBI1 encodes a leucine carboxylmethyltransferase (LCMT) that methylated PP2A and controlled its membrane-associated subcellular localization.
Regulation of protein phosphatase 2A methylation by LCMT1 and PME-1 plays a critical role in differentiation of neuroblastoma cells.
Sontag et al., Newcastle, Australia. In J Neurochem, 2010
Enhanced expression of LCMT1 in cultured neuroblastoma cells, which increases endogenous methylated catalytic C subunit and Balpha levels, induces changes in F-actin organization.
Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells.
Pallas et al., Atlanta, United States. In J Biol Chem, 2007
LCMT-1 is important for normal progression through mitosis and cell survival and is essential for embryonic development
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