Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28

Research output: Contribution to journalJournal article

Standard

Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28. / Hernebring, Malin; Fredriksson, Asa; Liljevald, Maria; Cvijovic, Marija; Norrman, Karin; Wiseman, John; Semb, Tor Henrik; Nyström, Thomas.

In: Scientific Reports, Vol. 3, 05.03.2013, p. 1381.

Research output: Contribution to journalJournal article

Harvard

Hernebring, M, Fredriksson, A, Liljevald, M, Cvijovic, M, Norrman, K, Wiseman, J, Semb, TH & Nyström, T 2013, 'Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28', Scientific Reports, vol. 3, pp. 1381. https://doi.org/10.1038/srep01381

APA

Hernebring, M., Fredriksson, A., Liljevald, M., Cvijovic, M., Norrman, K., Wiseman, J., ... Nyström, T. (2013). Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28. Scientific Reports, 3, 1381. https://doi.org/10.1038/srep01381

Vancouver

Hernebring M, Fredriksson A, Liljevald M, Cvijovic M, Norrman K, Wiseman J et al. Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28. Scientific Reports. 2013 Mar 5;3:1381. https://doi.org/10.1038/srep01381

Author

Hernebring, Malin ; Fredriksson, Asa ; Liljevald, Maria ; Cvijovic, Marija ; Norrman, Karin ; Wiseman, John ; Semb, Tor Henrik ; Nyström, Thomas. / Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28. In: Scientific Reports. 2013 ; Vol. 3. pp. 1381.

Bibtex

@article{8c40a8e1a7ff47e2a5f2e17902670372,
title = "Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28",
abstract = "In embryonic stem cells, removal of oxidatively damaged proteins is triggered upon the first signs of cell fate specification but the underlying mechanism is not known. Here, we report that this phase of differentiation encompasses an unexpected induction of genes encoding the proteasome activator PA28a{\ss} (11S), subunits of the immunoproteasome (20Si), and the 20Si regulator TNFa. This induction is accompanied by assembly of mature PA28-20S(i) proteasomes and elevated proteasome activity. Inhibiting accumulation of PA28a using miRNA counteracted the removal of damaged proteins demonstrating that PA28a{\ss} has a hitherto unidentified role required for resetting the levels of protein damage at the transition from self-renewal to cell differentiation.",
keywords = "Faculty of Health and Medical Sciences, Embryonic Stem Cells, PROTEIN QUALITY control, STEM-CELL DIFFERENTIATION, PROTEASOME",
author = "Malin Hernebring and Asa Fredriksson and Maria Liljevald and Marija Cvijovic and Karin Norrman and John Wiseman and Semb, {Tor Henrik} and Thomas Nystr{\"o}m",
year = "2013",
month = "3",
day = "5",
doi = "10.1038/srep01381",
language = "English",
volume = "3",
pages = "1381",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Removal of damaged proteins during ES cell fate specification requires the proteasome activator PA28

AU - Hernebring, Malin

AU - Fredriksson, Asa

AU - Liljevald, Maria

AU - Cvijovic, Marija

AU - Norrman, Karin

AU - Wiseman, John

AU - Semb, Tor Henrik

AU - Nyström, Thomas

PY - 2013/3/5

Y1 - 2013/3/5

N2 - In embryonic stem cells, removal of oxidatively damaged proteins is triggered upon the first signs of cell fate specification but the underlying mechanism is not known. Here, we report that this phase of differentiation encompasses an unexpected induction of genes encoding the proteasome activator PA28aß (11S), subunits of the immunoproteasome (20Si), and the 20Si regulator TNFa. This induction is accompanied by assembly of mature PA28-20S(i) proteasomes and elevated proteasome activity. Inhibiting accumulation of PA28a using miRNA counteracted the removal of damaged proteins demonstrating that PA28aß has a hitherto unidentified role required for resetting the levels of protein damage at the transition from self-renewal to cell differentiation.

AB - In embryonic stem cells, removal of oxidatively damaged proteins is triggered upon the first signs of cell fate specification but the underlying mechanism is not known. Here, we report that this phase of differentiation encompasses an unexpected induction of genes encoding the proteasome activator PA28aß (11S), subunits of the immunoproteasome (20Si), and the 20Si regulator TNFa. This induction is accompanied by assembly of mature PA28-20S(i) proteasomes and elevated proteasome activity. Inhibiting accumulation of PA28a using miRNA counteracted the removal of damaged proteins demonstrating that PA28aß has a hitherto unidentified role required for resetting the levels of protein damage at the transition from self-renewal to cell differentiation.

KW - Faculty of Health and Medical Sciences

KW - Embryonic Stem Cells

KW - PROTEIN QUALITY control

KW - STEM-CELL DIFFERENTIATION

KW - PROTEASOME

U2 - 10.1038/srep01381

DO - 10.1038/srep01381

M3 - Journal article

C2 - 23459332

VL - 3

SP - 1381

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

ER -

ID: 44739796