SHMT2 promotes the tumorigenesis of renal cell carcinoma by regulating the m6A modification of PPAT

Genomics. 2022 Jul;114(4):110424. doi: 10.1016/j.ygeno.2022.110424. Epub 2022 Jul 5.

Abstract

Objective: Serine hydroxymethyltransferase 2 (SHMT2) is the first rate-limiting enzyme for serine/glycine biosynthesis and one carbon metabolism. Here, we explore the underlying mechanism of how SHMT2 functions in renal cell carcinoma (RCC) initiation.

Methods: In this study, SHMT2 expression was assessed in RCC tissues. In vitro experiments were performed to investigate the functional role of SHMT2. The detailed mechanisms of SHMT2-mediated PPAT were addressed.

Results: Increased SHMT2 facilitated RCC cell proliferation by inducing the G1/S phase transition. And SHMT2 promoted the expression of PPAT. Mechanism dissection revealed that SHMT2 enhanced the m6A modification through the endogenous methyl donor SAM mediated by SHMT2 via serine/glycine one carbon metabolic networks. SHMT2-catalyzed serine/glycine conversion regulated PPAT expression in an m6A-IGF2BP2-dependent manner. SHMT2 promoted RCC cell proliferation by upregulating PPAT expression.

Conclusions: SHMT2 promotes RCC tumorigenesis by increasing PPAT expression. Thus, SHMT2 may be a novel potential therapeutic target for RCC.

Keywords: Metabolism; N6-methyladenosine; PPAT; Renal cell carcinoma; SHMT2.

MeSH terms

  • Amidophosphoribosyltransferase* / metabolism
  • Carbon / metabolism
  • Carcinogenesis / genetics
  • Carcinoma, Renal Cell* / genetics
  • Cell Proliferation
  • Cell Transformation, Neoplastic
  • Glycine / metabolism
  • Glycine Hydroxymethyltransferase* / genetics
  • Glycine Hydroxymethyltransferase* / metabolism
  • Humans
  • Kidney Neoplasms* / genetics
  • RNA-Binding Proteins / metabolism
  • Serine / metabolism

Substances

  • IGF2BP2 protein, human
  • RNA-Binding Proteins
  • Serine
  • Carbon
  • Glycine Hydroxymethyltransferase
  • SHMT protein, human
  • Amidophosphoribosyltransferase
  • Glycine