Your browser doesn't support javascript.
loading
Quantitative proteomics revealed new functions of ALKBH4.
Yu, Kailin; Qi, Tianyu F; Miao, Weili; Liu, Xiaochuan; Wang, Yinsheng.
Afiliación
  • Yu K; Department of Chemistry, University of California, Riverside, California, USA.
  • Qi TF; Environmental Toxicology Graduate Program, University of California, Riverside, California, USA.
  • Miao W; Department of Chemistry, University of California, Riverside, California, USA.
  • Liu X; Department of Chemistry, University of California, Riverside, California, USA.
  • Wang Y; Department of Chemistry, University of California, Riverside, California, USA.
Proteomics ; 22(7): e2100231, 2022 04.
Article en En | MEDLINE | ID: mdl-34951099
ABSTRACT
ALKBH4 is a versatile demethylase capable of catalyzing the demethylation of monomethylated lysine-84 on actin and N6 -methyladenine in DNA. In this study, we conducted a quantitative proteomic experiment to reveal the altered expression of proteins in HEK293T cells upon genetic ablation of ALKBH4. Our results showed markedly diminished levels of GSTP1 and HSPB1 proteins in ALKBH4-depleted cells, which emanate from an augmented expression level of DNA (cytosine-5)-methyltransferase 1 (DNMT1) and the ensuing elevated cytosine methylation in the promoter regions of GSTP1 and HSPB1 genes. Together, our results revealed a role of ALKBH4 in modulating DNA cytosine methylation through regulating the expression level of DNMT1 protein.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Metilación de ADN / Homólogo 4 de AlkB Lisina Desmetilasa Límite: Humans Idioma: En Revista: Proteomics Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Metilación de ADN / Homólogo 4 de AlkB Lisina Desmetilasa Límite: Humans Idioma: En Revista: Proteomics Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos