ArticleStem cell research & therapy2022
Dppa3 facilitates self-renewal of embryonic stem cells by stabilization of pluripotent factors.
Article in Stem cell research & therapy, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 11 citations in OpenAlex.
- Gene Expression Analysis of HPRT-Deficient Cells Maintained with Physiological Levels of Folic Acid.Cells · 2025Article
- Acrylamide and Its Metabolite Glycidamide Induce Reproductive Toxicity During In Vitro Maturation of Bovine Oocytes.Toxics · 2025Article
- PGC7 maintains the pluripotency of F9 embryonic carcinoma cells by promoting Nanog translation.Acta biochimica et biophysica Sinica · 2025Article
- PGC7 regulates maternal mRNA translation via AKT1-YBX1 interactions in mouse oocytes.Cell communication and signaling : CCS · 2024Article
- Regulatory mechanism and biological function of UHRF1-DNMT1-mediated DNA methylation.Functional & integrative genomics · 2022Review
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
backgroundDevelopmental pluripotency-associated 3 (Dppa3, also called Stella or PGC7) is a principal maternal protein specially expressed in pre-implantation embryos, embryonic stem cells (ES cells) and primordial germ cells (PGCs). It plays critical role in the regulating of DNA methylation in zygotes and oocytes. However, the effect of Dppa3 in ES cells on the stability of proteins is still unclear.
methodsIn this study, we first identified the potential interacting proteins with Dppa3 using immunoprecipitation-mass spectrometry (IP-MS). After GO analysis, we further constructed Dppa3-silenced ES cells and ES cell lines overexpressing with different lengths of Dppa3 to explore the mechanisms of Dppa3 on protein stability.
resultsIP-MS results showed that Dppa3 interacted with quite a few subunits of 26S proteasome. Full length of Dppa3 stabilized Uhrf1 and Nanog by inhibiting its degradation. Silencing Dppa3 promoted degradation of Nanog protein.
conclusionsOur results indicated that Dppa3 safeguard the stability of Uhrf1 and Nanog by inhibiting proteasome-associated degradation in ES cells. These findings shed light on new function of Dppa3 in maintaining stability of proteins and provides a valuable resource for understanding the roles of Dppa3 in embryonic stem cells.
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