Cargando…

The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?

The proteasome is a multi-enzyme complex responsible for orchestrating protein quality control by degrading misfolded, damaged, abnormal and foreign proteins. Studies related to the association of the proteasomal system in the preservation of self-renewal in both human and mouse pluripotent cells ar...

Descripción completa

Detalles Bibliográficos
Autores principales: Schröter, Friederike, Adjaye, James
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4035846/
https://www.ncbi.nlm.nih.gov/pubmed/25127410
http://dx.doi.org/10.1186/scrt413
_version_ 1782318112545177600
author Schröter, Friederike
Adjaye, James
author_facet Schröter, Friederike
Adjaye, James
author_sort Schröter, Friederike
collection PubMed
description The proteasome is a multi-enzyme complex responsible for orchestrating protein quality control by degrading misfolded, damaged, abnormal and foreign proteins. Studies related to the association of the proteasomal system in the preservation of self-renewal in both human and mouse pluripotent cells are sparse, and therefore a clear indication of the emergence of a new and important field of research. Under specific conditions the standard proteasome switches to the newly synthesized immunoproteasome, a catalytically active protein chamber also involved in the regulation of protein homeostasis, cell signaling and gene expression. Herein we review recent data to help elucidate and highlight the pivotal role of the proteasome complex, constitutive as well as inducible, in the regulation of self-renewal, pluripotency and differentiation of both embryonic and induced pluripotent stem cells. The proteasome that is endowed with enhanced proteolytic activity maintains self-renewal by regulating gene expression. In addition to protein degradation, the proteasome activator PA28, compartments of the 19S regulatory particle and key members of the ubiquitin pathway dictate the fate of a pluripotent stem cell. We anticipate that our observations will stimulate active research in this new and emerging theme related to stem cell biology, disease and regenerative medicine.
format Online
Article
Text
id pubmed-4035846
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-40358462015-02-18 The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up? Schröter, Friederike Adjaye, James Stem Cell Res Ther Review The proteasome is a multi-enzyme complex responsible for orchestrating protein quality control by degrading misfolded, damaged, abnormal and foreign proteins. Studies related to the association of the proteasomal system in the preservation of self-renewal in both human and mouse pluripotent cells are sparse, and therefore a clear indication of the emergence of a new and important field of research. Under specific conditions the standard proteasome switches to the newly synthesized immunoproteasome, a catalytically active protein chamber also involved in the regulation of protein homeostasis, cell signaling and gene expression. Herein we review recent data to help elucidate and highlight the pivotal role of the proteasome complex, constitutive as well as inducible, in the regulation of self-renewal, pluripotency and differentiation of both embryonic and induced pluripotent stem cells. The proteasome that is endowed with enhanced proteolytic activity maintains self-renewal by regulating gene expression. In addition to protein degradation, the proteasome activator PA28, compartments of the 19S regulatory particle and key members of the ubiquitin pathway dictate the fate of a pluripotent stem cell. We anticipate that our observations will stimulate active research in this new and emerging theme related to stem cell biology, disease and regenerative medicine. BioMed Central 2014-02-18 /pmc/articles/PMC4035846/ /pubmed/25127410 http://dx.doi.org/10.1186/scrt413 Text en Copyright © 2014 Schröter et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 The licensee has exclusive rights to distribute this article, in any medium, for 12 months following its publication. After this time, the article is available under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Schröter, Friederike
Adjaye, James
The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
title The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
title_full The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
title_fullStr The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
title_full_unstemmed The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
title_short The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
title_sort proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4035846/
https://www.ncbi.nlm.nih.gov/pubmed/25127410
http://dx.doi.org/10.1186/scrt413
work_keys_str_mv AT schroterfriederike theproteasomecomplexandthemaintenanceofpluripotencysustainthefatebymoppingup
AT adjayejames theproteasomecomplexandthemaintenanceofpluripotencysustainthefatebymoppingup
AT schroterfriederike proteasomecomplexandthemaintenanceofpluripotencysustainthefatebymoppingup
AT adjayejames proteasomecomplexandthemaintenanceofpluripotencysustainthefatebymoppingup