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Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity
AMP-activated protein kinase (AMPK) is a sensor of cellular energy status. It is a heterotrimer composed of a catalytic α and two regulatory subunits (β and γ). AMPK activity is regulated allosterically by AMP and by the phosphorylation of residue Thr-172 within the catalytic domain of the AMPKα sub...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3667731/ https://www.ncbi.nlm.nih.gov/pubmed/23552691 http://dx.doi.org/10.1091/mbc.E12-11-0806 |
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author | Rubio, Teresa Vernia, Santiago Sanz, Pascual |
author_facet | Rubio, Teresa Vernia, Santiago Sanz, Pascual |
author_sort | Rubio, Teresa |
collection | PubMed |
description | AMP-activated protein kinase (AMPK) is a sensor of cellular energy status. It is a heterotrimer composed of a catalytic α and two regulatory subunits (β and γ). AMPK activity is regulated allosterically by AMP and by the phosphorylation of residue Thr-172 within the catalytic domain of the AMPKα subunit by upstream kinases. We present evidence that the AMPKβ2 subunit may be posttranslationally modified by sumoylation. This process is carried out by the E3-small ubiquitin-like modifier (SUMO) ligase protein inhibitor of activated STAT PIASy, which modifies the AMPKβ2 subunit by the attachment of SUMO2 but not SUMO1 moieties. Of interest, AMPKβ1 is not a substrate for this modification. We also demonstrate that sumoylation of AMPKβ2 enhances the activity of the trimeric α2β2γ1 AMPK complex. In addition, our results indicate that sumoylation is antagonist and competes with the ubiquitination of the AMPKβ2 subunit. This adds a new layer of complexity to the regulation of the activity of the AMPK complex, since conditions that promote ubiquitination result in inactivation, whereas those that promote sumoylation result in the activation of the AMPK complex. |
format | Online Article Text |
id | pubmed-3667731 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-36677312013-08-16 Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity Rubio, Teresa Vernia, Santiago Sanz, Pascual Mol Biol Cell Articles AMP-activated protein kinase (AMPK) is a sensor of cellular energy status. It is a heterotrimer composed of a catalytic α and two regulatory subunits (β and γ). AMPK activity is regulated allosterically by AMP and by the phosphorylation of residue Thr-172 within the catalytic domain of the AMPKα subunit by upstream kinases. We present evidence that the AMPKβ2 subunit may be posttranslationally modified by sumoylation. This process is carried out by the E3-small ubiquitin-like modifier (SUMO) ligase protein inhibitor of activated STAT PIASy, which modifies the AMPKβ2 subunit by the attachment of SUMO2 but not SUMO1 moieties. Of interest, AMPKβ1 is not a substrate for this modification. We also demonstrate that sumoylation of AMPKβ2 enhances the activity of the trimeric α2β2γ1 AMPK complex. In addition, our results indicate that sumoylation is antagonist and competes with the ubiquitination of the AMPKβ2 subunit. This adds a new layer of complexity to the regulation of the activity of the AMPK complex, since conditions that promote ubiquitination result in inactivation, whereas those that promote sumoylation result in the activation of the AMPK complex. The American Society for Cell Biology 2013-06-01 /pmc/articles/PMC3667731/ /pubmed/23552691 http://dx.doi.org/10.1091/mbc.E12-11-0806 Text en © 2013 Rubio et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Rubio, Teresa Vernia, Santiago Sanz, Pascual Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity |
title | Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity |
title_full | Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity |
title_fullStr | Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity |
title_full_unstemmed | Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity |
title_short | Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity |
title_sort | sumoylation of ampkβ2 subunit enhances amp-activated protein kinase activity |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3667731/ https://www.ncbi.nlm.nih.gov/pubmed/23552691 http://dx.doi.org/10.1091/mbc.E12-11-0806 |
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