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Updated: Nov 9, 2025
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Published on: June 6, 2025
Changes in the phosphorylation of nucleotide metabolism‑associated proteins by leukemia inhibitory factor in mouse
Hwa-Ryung Song1, Han-Kyu Kim1, Seung-Gook Kim1
1Department of Microbiology, Jeonbuk National University Medical School, Jeonju, Jeollabuk 54896, Republic of Korea.
Insights
Leukemia inhibitory factor (LIF) maintains mouse embryonic stem cell self-renewal by altering protein phosphorylation. This study reveals LIF
Area of Science:
- Stem cell biology
- Molecular signaling
- Proteomics
Background:
- Leukemia inhibitory factor (LIF) is crucial for maintaining mouse embryonic stem cell (mESC) self-renewal.
- LIF signals through a receptor complex involving gp130, activating key intracellular pathways.
- Understanding LIF's downstream effects on protein phosphorylation is vital for stem cell research.
Purpose of the Study:
- To comprehensively profile protein phosphorylation changes induced by LIF in mESCs.
- To identify specific proteins and pathways modulated by LIF signaling.
- To elucidate the molecular mechanisms underlying LIF's role in stem cell maintenance.
Main Methods:
- Proteomic analysis of LIF-treated and untreated mESCs.
- Two-dimensional differential in-gel electrophoresis (2D-DIGE) for protein separation.
- Mass spectrometry (MALDI-TOF MS) for protein identification and phosphoprotein analysis.
Main Results:
- LIF treatment resulted in altered phosphorylation of 50 proteins (16 increased, 34 decreased).
- Enriched Gene Ontology terms included 'organonitrogen compound metabolic process' and 'regulation of mRNA splicing via spliceosome'.
- LIF significantly modulated phosphorylation of proteins involved in nucleotide metabolism.
Conclusions:
- LIF influences mESC self-renewal through extensive modulation of protein phosphorylation.
- The findings highlight LIF's role in regulating nucleotide metabolism pathways in stem cells.
- This study provides novel insights into the molecular underpinnings of LIF-mediated stem cell maintenance.
Abstract:
Leukemia inhibitory factor (LIF) is a stem cell growth factor that maintains self‑renewal of mouse embryonic stem cells (mESCs). LIF is a cytokine in the interleukin‑6 family and signals via the common receptor subunit gp130 and ligand‑specific LIF receptor. LIF causes heterodimerization of the LIF receptor and gp130, activating the Janus kinase/STAT and MAPK pathways, resulting in changes in protein phosphorylation. The present study profiled LIF‑mediated protein phosphorylation changes in mESCs via proteomic analysis. mESCs treated in the presence or absence of LIF were analyzed via two‑dimensional differential in‑gel electrophoresis and protein and phosphoprotein staining. Protein identification was performed by matrix‑assisted laser desorption/ionization‑time of flight mass spectrophotometry. Increased phosphorylation of 16 proteins and decreased phosphorylation of 34 proteins in response to LIF treatment was detected. Gene Ontology terms enriched in these proteins included 'organonitrogen compound metabolic process', 'regulation of mRNA splicing via spliceosome' and 'nucleotide metabolic process'. The present results revealed that LIF modulated phosphorylation levels of nucleotide metabolism‑associated proteins, thus providing insight into the mechanism underlying LIF action in mESCs.
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