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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].. Zusätzlich bieten wir Ihnen Leucine Carboxyl Methyltransferase 1 Antikörper (73) und viele weitere Produktgruppen zu diesem Protein an.
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We demonstrate that NNMT outcompetes leucine carboxyl methyl transferase 1 (LCMT1) for methyl transfer from principal methyl donor SAM in biological systems. Inhibiting NNMT increased the availability of methyl groups for LCMT1 to methylate PP2A, resulting in the inhibition of oncogenic serine/threonine kinases (STK).
LCMT1-PME-1 (zeige PPME1 Proteine) methylation equilibrium is critical for regulating mitotic spindle size and thereby proper cell division
alterations in the membrane localization of PP2A (zeige PPP2R4 Proteine) and Tau following down-regulation of LCMT1 may lead to PP2A (zeige PPP2R4 Proteine) and Tau dysfunction in AD.
Data indicate that PP2A (zeige PPP2R4 Proteine) holoenzyme biogenesis and activity are controlled by five PP2A (zeige PPP2R4 Proteine) modulators, consisting of alpha4, PTPA (zeige PPP2R4 Proteine), LCMT1, PME-1 (zeige PPME1 Proteine) and TIPRL1, which serve to prevent promiscuous phosphatase activity until the holoenzyme is completely assembled.
GSK-3beta can inhibit PP2A (zeige PPP2R4 Proteine) by increasing the inhibitory L309-demethylation involving upregulation of PME-1 (zeige PPME1 Proteine) and inhibition of PPMT1
determined crystal structures of human LCMT-1 in isolation and in complex with PP2A (zeige PPP2R4 Proteine) stabilized by a cofactor mimic. The structures show that the LCMT-1 active-site pocket recognizes the carboxyl terminus of PP2A (zeige PPP2R4 Proteine)
X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet (zeige MAT1A Proteine)) 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 (zeige HDAC3 Proteine), a reported target of the methylation-dependent PP4R1 (zeige PPP4R1 Proteine)-PP4c (zeige PPP4C Proteine) complex. Collectively, our data suggest that LCMT-1 coordinately regulates the carboxyl methylation of PP2A (zeige PPP2R2B Proteine)-related phosphatases and, consequently, their holoenzyme assembly and function.
In LCMT1 deficiency enzyme activity and methylation of PP2A (zeige PPP2R2B Proteine) are reduced in a coordinate fashion, suggesting that LCMT1 is the only PP2A (zeige PPP2R2B Proteine) 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