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Literature summary for 2.1.1.20 extracted from

  • DebRoy, S.; Kramarenko, I.I.; Ghose, S.; Oleinik, N.V.; Krupenko, S.A.; Krupenko, N.I.
    A novel tumor suppressor function of glycine N-methyltransferase is independent of its catalytic activity but requires nuclear localization (2013), PLoS ONE, 8, e70062.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine GNMT is strongly downregulated in human cancers and is undetectable in cancer cell lines while the transient expression of the protein in cancer cells induces apoptosis and results in the activation of ERK1/2. The antiproliferative effect of GNMT can be partially reversed by treatment with the pancaspase inhibitor zVAD-fmk but not by supplementation with high folate or SAM. GNMT exerts the suppressor effect primarily in cells originated from malignant tumors. High levels of GNMT, detected in regenerating liver and in NIH3T3 mouse fibroblasts, do not produce cytotoxic effects. GNMT, a predominantly cytoplasmic protein, is translocated into nuclei upon transfection of cancer cells. The induction of apoptosis is associated with the GNMT nuclear localization but is independent of its catalytic activity or folate binding Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm main localization Homo sapiens 5737
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nucleus partial Homo sapiens 5634
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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