Cited by 389Ubiquitin and proteasome pathwaysAutophagy in Disease and TherapyGenetics, Aging, and Longevity in Model Organisms

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Increased proteasome activity in human embryonic stem cells is regulated by PSMD11

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Vilchez, David, Boyer, Leah, Morantte, Ianessa, Lutz, Margaret, Merkwirth, Carsten, Joyce, Derek, Spencer, Brian, Page, Lesley, Masliah, Eliezer, Berggren, W. Travis, Gage, Fred H., Dillin, Andrew·2012·Nature

DOI 10.1038/nature11468PMC PMC5215918

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Abstract

Embryonic stem cells can replicate continuously in the absence of senescence and, therefore, are immortal in culture. Although genome stability is essential for the survival of stem cells, proteome stability may have an equally important role in stem-cell identity and function. Furthermore, with the asymmetric divisions invoked by stem cells, the passage of damaged proteins to daughter cells could potentially destroy the resulting lineage of cells. Therefore, a firm understanding of how stem cells maintain their proteome is of central importance. Here we show that human embryonic stem cells (hESCs) exhibit high proteasome activity that is correlated with increased levels of the 19S proteasome subunit PSMD11 (known as RPN-6 in Caenorhabditis elegans) and a corresponding increased assembly of the 26S/30S proteasome. Ectopic expression of PSMD11 is sufficient to increase proteasome assembly and activity. FOXO4, an insulin/insulin-like growth factor-I (IGF-I) responsive transcription factor associated with long lifespan in invertebrates, regulates proteasome activity by modulating the expression of PSMD11 in hESCs. Proteasome inhibition in hESCs affects the expression of pluripotency markers and the levels of specific markers of the distinct germ layers. Our results suggest a new regulation of proteostasis in hESCs that links longevity and stress resistance in invertebrates to hESC function and identity.

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Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors
Takahashi, K., & Yamanaka, S. (2006) · Cell · doi:10.1016/j.cell.2006.07.024 · Cited by 26,673
Induction of Pluripotent Stem Cells from Adult Human Fibroblasts by Defined Factors
Takahashi, K., Tanabe, K., Ohnuki, M., Narita, M., Ichisaka, T., Tomoda, K., & Yamanaka, S. (2007) · Cell · doi:10.1016/j.cell.2007.11.019 · Cited by 20,221
Embryonic Stem Cell Lines Derived from Human Blastocysts
Thomson, J. A., Itskovitz‐Eldor, J., Shapiro, S. S., Waknitz, M. A., Swiergiel, J. J., Marshall, V. S., & Jones, J. M. (1998) · Science · doi:10.1126/science.282.5391.1145 · Cited by 15,947
Induced Pluripotent Stem Cell Lines Derived from Human Somatic Cells
Yu, J., Vodyanik, M. A., Smuga-Otto, K., Antosiewicz-Bourget, J., Frane, J. L., Tian, S., Nie, J., Jonsdottir, G. A., Ruotti, V., Stewart, R., et al. (2007) · Science · doi:10.1126/science.1151526 · Cited by 10,310
Establishment in culture of pluripotential cells from mouse embryos
Evans, M. J., & Kaufman, M. H. (1981) · Nature · doi:10.1038/292154a0 · Cited by 8,623
A C. elegans mutant that lives twice as long as wild type
Kenyon, C., Chang, J., Gensch, E., Rudner, A., & Tabtiang, R. (1993) · Nature · doi:10.1038/366461a0 · Cited by 3,387
Tricine–SDS-PAGE
Schägger, H. (2006) · Nature Protocols · doi:10.1038/nprot.2006.4 · Cited by 2,519
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495
Self-citation
STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764

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Authors: Vilchez, D., Boyer, L., Morantte, I., Lutz, M., Merkwirth, C., Joyce, D., Spencer, B., Page, L., Masliah, E., Berggren, W. T., Gage, F. H., & Dillin, A.
Affiliations: Salk Institute for Biological Studies (US)
University of California San Diego (US)
Scripps Research Institute (US)
Corresponding author: Dillin, Andrew
ORCID: Boyer, Leah
Morantte, Ianessa
Merkwirth, Carsten
Spencer, Brian
Page, Lesley
Masliah, Eliezer
Gage, Fred H.
Dillin, Andrew
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2012-09
Volume: 489
Issue: 7415
Pages: 304-308
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature11468
PMC: PMC5215918
OpenAlex: W2089761608
Cited by: 388
References: 26
Citations by year: 2026: 7 · 2025: 25 · 2024: 24 · 2023: 17 · 2022: 24 · 2021: 42 · 2020: 39 · 2019: 35 · 2018: 36 · 2017: 30 · 2016: 24 · 2015: 31 · 2014: 30 · 2013: 19 · 2012: 5
FWCI: 10.92
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: Howard Hughes Medical Institute
National Institute on Aging (R37AG018440, P01AG031097)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords: proteasome activity, 19S proteasome, FOXO4, DAF-16, human embryonic stem cells, stem cell differentiation, proteostasis, Caenorhabditis elegans, glucagon-like peptide-1, lifespan extension, proteotoxic stress, genome stability, aging, insulin/IGF-1 signaling
MeSH terms: Cell Differentiation, Cell Line, Humans, Transcription Factors, Up-Regulation, Cell Cycle Proteins, Protein Subunits, Pluripotent Stem Cells, Proteasome Endopeptidase Complex, Forkhead Transcription Factors, Embryonic Stem Cells, HEK293 Cells, Proteasome Inhibitors

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Increased proteasome activity in human embryonic stem cells is regulated by PSMD11

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