PPM1G dephosphorylates eIF4E in control of mRNA translation and cell proliferation
0303 health sciences
Protein Phosphatase 2C
03 medical and health sciences
Eukaryotic Initiation Factor-4E
HEK293 Cells
Protein Biosynthesis
Phosphoprotein Phosphatases
Humans
Animals
RNA, Messenger
Phosphorylation
Research Articles
Cell Proliferation
Protein Binding
DOI:
10.26508/lsa.202402755
Publication Date:
2024-08-07T14:55:21Z
AUTHORS (14)
ABSTRACT
The mRNA 5′cap-binding eukaryotic translation initiation factor 4E (eIF4E) plays a critical role in the control of mRNA translation in health and disease. One mechanism of regulation of eIF4E activity is via phosphorylation of eIF4E by MNK kinases, which promotes the translation of a subset of mRNAs encoding pro-tumorigenic proteins. Work on eIF4E phosphatases has been paltry. Here, we show that PPM1G is the phosphatase that dephosphorylates eIF4E. We describe the eIF4E-binding motif in PPM1G that is similar to 4E-binding proteins (4E-BPs). We demonstrate that PPM1G inhibits cell proliferation by targeting phospho-eIF4E–dependent mRNA translation.
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