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Acetylation and sumoylation control STAT5 activation antagonistically

STAT5 proteins are activated by tyrosine phosphorylation, but recently further post-translation modifications such as serine/threonine phosphorylation, acetylation at lysine residues or sumoylation in close vicinity of the critical tyrosine residue have been reported. Here, we discuss new findings o...

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Detalles Bibliográficos
Autores principales: Krämer, Oliver H., Moriggl, Richard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670247/
https://www.ncbi.nlm.nih.gov/pubmed/24058773
http://dx.doi.org/10.4161/jkst.21232
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author Krämer, Oliver H.
Moriggl, Richard
author_facet Krämer, Oliver H.
Moriggl, Richard
author_sort Krämer, Oliver H.
collection PubMed
description STAT5 proteins are activated by tyrosine phosphorylation, but recently further post-translation modifications such as serine/threonine phosphorylation, acetylation at lysine residues or sumoylation in close vicinity of the critical tyrosine residue have been reported. Here, we discuss new findings on impaired STAT5 signaling in lymphocytes isolated from a SUMO-specific protease knockout mouse (SENP1(−/−)), which results in sumoylated STAT5 and abolishes tyrosine phosphorylation. Van Nguyen and colleagues examined acetylation and sumoylation of STAT5 and found that both modifications act antagonistically to control tyrosine phosphorylation of STAT5.
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spelling pubmed-36702472013-09-19 Acetylation and sumoylation control STAT5 activation antagonistically Krämer, Oliver H. Moriggl, Richard JAKSTAT Commentary STAT5 proteins are activated by tyrosine phosphorylation, but recently further post-translation modifications such as serine/threonine phosphorylation, acetylation at lysine residues or sumoylation in close vicinity of the critical tyrosine residue have been reported. Here, we discuss new findings on impaired STAT5 signaling in lymphocytes isolated from a SUMO-specific protease knockout mouse (SENP1(−/−)), which results in sumoylated STAT5 and abolishes tyrosine phosphorylation. Van Nguyen and colleagues examined acetylation and sumoylation of STAT5 and found that both modifications act antagonistically to control tyrosine phosphorylation of STAT5. Landes Bioscience 2012-07-01 2012-07-01 /pmc/articles/PMC3670247/ /pubmed/24058773 http://dx.doi.org/10.4161/jkst.21232 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Commentary
Krämer, Oliver H.
Moriggl, Richard
Acetylation and sumoylation control STAT5 activation antagonistically
title Acetylation and sumoylation control STAT5 activation antagonistically
title_full Acetylation and sumoylation control STAT5 activation antagonistically
title_fullStr Acetylation and sumoylation control STAT5 activation antagonistically
title_full_unstemmed Acetylation and sumoylation control STAT5 activation antagonistically
title_short Acetylation and sumoylation control STAT5 activation antagonistically
title_sort acetylation and sumoylation control stat5 activation antagonistically
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670247/
https://www.ncbi.nlm.nih.gov/pubmed/24058773
http://dx.doi.org/10.4161/jkst.21232
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