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Results indicate the postembryonic functions of N-myristoyltransferases NMT1 involve regulation of the functional and morphological integrity of the plant endomembranes.
Protein N-myristoylation is systematically associated with shoot meristem development and that SnRK1 (for SNF1-related kinase (show SNRK Proteins)) is one of its essential primary targets. [NMT1]
These observations point at a previously unrecognized contribution of calnexin (show CANX Proteins) to the retention of NMT1 at the ER membrane.
findings suggest that both NMT1 and hnRNP A2/B1 (show HNRNPA2B1 Proteins) take part in the regulation of HIV-1 RNA expression through their mutual opposite effects on the viral RNA expression in HIV-1-producing cells
we propose a model of the Nef:NMT complex in which only the myristoyl moiety holds the two proteins together in complex and speculate that perhaps NMT chaperones Nef to the membrane and thereby protects the myristic acid group from the cytosol
In this study, we found decreases in the mRNA levels of human NMT isoforms and the NMT activities in the course of HIV-1 infection in the human T-cell line
role of HSC70 in the regulation of NMT
NMT1 and NMT2 (show NMT2 Proteins) have only partially overlapping functions; NMT1 is critical for tumor cell proliferation
Nef is preferentially myristoylated by NMT2 (show NMT2 Proteins), suggesting that selective inhibition of NMT2 (show NMT2 Proteins) may provide a novel means of blocking HIV virulence.
This is the first report demonstrating expression of N-myristoyltransferase (NMT) in normal and inflamed lungs and a novel role for NMT in regulation of neutrophil lifespan.
Nmt1 is not essential for the viability of mammalian cells but is required for development and is the principal N-myristoyltransferase in early embryogenesis
NMT1 is essential for proper monocytic differentiation of the mouse bone marrow cells.
Myristate, a rare 14-carbon saturated fatty acid, is cotranslationally attached by an amide linkage to the N-terminal glycine residue of cellular and viral proteins with diverse functions. N-myristoyltransferase (NMT\; EC 184.108.40.206) catalyzes the transfer of myristate from CoA to proteins. N-myristoylation appears to be irreversible and is required for full expression of the biologic activities of several N-myristoylated proteins, including the alpha subunit of the signal-transducing guanine nucleotide-binding protein (G protein) GO (GNAO1\; MIM 139311) (Duronio et al., 1992
, N-myristoyltransferase 1
, glycylpeptide N-tetradecanoyltransferase 1-like
, NMT 1
, alternative, short form NMT-S
, glycylpeptide N-tetradecanoyltransferase 1
, long form, NMT-L
, myristoyl-CoA:protein N-myristoyltransferase 1
, peptide N-myristoyltransferase 1
, type I N-myristoyltransferase