Protein phosphatase PPM1G regulates protein translation and cell growth by dephosphorylating 4E binding protein 1 (4E-BP1)

Jianyu Liu, Payton D. Stevens, Nichole E. Eshleman, Tianyan Gao

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

Background: Phosphorylation of 4E-BP1 plays a critical role in controlling its ability to inhibit protein translation. Results: PPM1G is identified as a protein phosphatase that dephosphorylates 4E-BP1 in vitro and in cells. Conclusion: PPM1G negatively regulates protein translation by controlling the phosphorylation of 4E-BP1. Significance: PPM1G-mediated dephosphorylation of 4E-BP1 provides a novel mechanism in the regulation of protein translation.

Original languageEnglish
Pages (from-to)23225-23233
Number of pages9
JournalJournal of Biological Chemistry
Volume288
Issue number32
DOIs
StatePublished - Aug 9 2013

Funding

FundersFunder number
American Cancer SocietyRSG0822001TBE
National Institutes of Health (NIH)R01 CA133429-01A1
National Childhood Cancer Registry – National Cancer InstituteR01CA133429

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Fingerprint

    Dive into the research topics of 'Protein phosphatase PPM1G regulates protein translation and cell growth by dephosphorylating 4E binding protein 1 (4E-BP1)'. Together they form a unique fingerprint.

    Cite this