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serine hydroxymethyltransferase 2 (SHMT2) is acetylated at K95 in colorectal cancer (CRC) cells. SHMT2-K95-Ac disrupts its functional tetramer structure and inhibits its enzymatic activity. SHMT2-K95-Ac promotes its degradation via the K63-ubiquitin-lysosome pathway in a glucose-dependent manner. SHMT2-K95-Ac is decreased in human CRC samples which is correlated with poorer postoperative overall survival.
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Findings support the hypothesis that age-associated respiration defects in fibroblasts of elderly humans are caused not by mtDNA mutations but by epigenetic regulation of nuclear genes including SHMT2.
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SHMT2 Desuccinylation is associated with Cancer Cell Proliferation.
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The one-carbon donor formate generally rescues cells from SHMT inhibition, but paradoxically increases the inhibitor's cytotoxicity in diffuse large B-cell lymphoma (DLBCL); this effect is rooted in defective glycine uptake in DLBCL cell lines, rendering them uniquely dependent upon SHMT enzymatic activity to meet glycine demand.
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Our data confirm the heterogeneity of breast tumors at a functional proteomic level and dissects the relationship between metabolism-related proteins, pathological features and patient survival. These observations highlight the importance of SHMT2 and ASCT2 as valuable individual prognostic markers and potential targets for personalized breast cancer therapy
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Data suggest that serine hydroxymethyltransferase 2 (SHMT2) may be a potential target in the treatment of hepatocellular carcinoma (HCC).
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High SHMT2 expression is associated with idiopathic pulmonary fibrosis.
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Site-directed mutagenesis experiments on SHMT1 demonstrate that selective enzyme inhibition relies on the presence of a cysteine residue at the active site of SHMT1 (Cys204) that is absent in SHMT2.
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These results indicate that SHMT2 may be a valuable prognostic biomarker in ER-negative breast cancer cases
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our results for the first time showed that miR-615-5p prevents proliferation and migration through negatively regulating SHMT2 in HCC.
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The SHMT-2 is the direct targets of miR-370 and miR-373, respectively, in human articular chondrocytes.
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High SHMT2 expression increases glycine-dependent nucleotide synthesis leading to bladder cancer growth.
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SHMT2 is required for glioblastoma multiforme cells to adapt to the tumour environment, but also renders these cells sensitive to glycine cleavage system inhibition
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SHMT1 exists in solution as a tetramer, both in the absence and presence of PLP, while SHMT2 undergoes a dimer-to-tetramer transition.
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The present study not only describes individual genetic variation that directly affects SHMT1 and SHMT2 activity, but provided insight into the overall regulation of the Folate and Methionine Cycles.
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SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
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This paper compares the mitochondrial and cytoplasmic forms of this enzyme and suggests that the two genes are a result of a single gene duplication.
