SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease

SUMOylation is a transient posttranslational modification with small-ubiquitin like modifiers (SUMO1, SUMO2 and SUMO3) covalently attached to their target-proteins via a multi-step enzymatic cascade. SUMOylation modifies protein-protein interactions, enzymatic-activity or chromatin binding in a mult...

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Autores principales:	Paul W. Hotz, Stefan Müller, Luca Mendler
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	SUMO SENP heart failure heart ischemia reperfusion (I/R) injury Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/7b7ed21fdeb5415085ef9e84f16dcc99
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spelling	oai:doaj.org-article:7b7ed21fdeb5415085ef9e84f16dcc992021-11-19T06:15:42ZSUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease2296-889X10.3389/fmolb.2021.786136https://doaj.org/article/7b7ed21fdeb5415085ef9e84f16dcc992021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fmolb.2021.786136/fullhttps://doaj.org/toc/2296-889XSUMOylation is a transient posttranslational modification with small-ubiquitin like modifiers (SUMO1, SUMO2 and SUMO3) covalently attached to their target-proteins via a multi-step enzymatic cascade. SUMOylation modifies protein-protein interactions, enzymatic-activity or chromatin binding in a multitude of key cellular processes, acting as a highly dynamic molecular switch. To guarantee the rapid kinetics, SUMO target-proteins are kept in a tightly controlled equilibrium of SUMOylation and deSUMOylation. DeSUMOylation is maintained by the SUMO-specific proteases, predominantly of the SENP family. SENP1 and SENP2 represent family members tuning SUMOylation status of all three SUMO isoforms, while SENP3 and SENP5 are dedicated to detach mainly SUMO2/3 from its substrates. SENP6 and SENP7 cleave polySUMO2/3 chains thereby countering the SUMO-targeted-Ubiquitin-Ligase (StUbL) pathway. Several biochemical studies pinpoint towards the SENPs as critical enzymes to control balanced SUMOylation/deSUMOylation in cardiovascular health and disease. This study aims to review the current knowledge about the SUMO-specific proteases in the heart and provides an integrated view of cardiac functions of the deSUMOylating enzymes under physiological and pathological conditions.Paul W. HotzStefan MüllerLuca MendlerFrontiers Media S.A.articleSUMOSENPheart failureheartischemia reperfusion (I/R) injuryBiology (General)QH301-705.5ENFrontiers in Molecular Biosciences, Vol 8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	SUMO SENP heart failure heart ischemia reperfusion (I/R) injury Biology (General) QH301-705.5
spellingShingle	SUMO SENP heart failure heart ischemia reperfusion (I/R) injury Biology (General) QH301-705.5 Paul W. Hotz Stefan Müller Luca Mendler SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease
description	SUMOylation is a transient posttranslational modification with small-ubiquitin like modifiers (SUMO1, SUMO2 and SUMO3) covalently attached to their target-proteins via a multi-step enzymatic cascade. SUMOylation modifies protein-protein interactions, enzymatic-activity or chromatin binding in a multitude of key cellular processes, acting as a highly dynamic molecular switch. To guarantee the rapid kinetics, SUMO target-proteins are kept in a tightly controlled equilibrium of SUMOylation and deSUMOylation. DeSUMOylation is maintained by the SUMO-specific proteases, predominantly of the SENP family. SENP1 and SENP2 represent family members tuning SUMOylation status of all three SUMO isoforms, while SENP3 and SENP5 are dedicated to detach mainly SUMO2/3 from its substrates. SENP6 and SENP7 cleave polySUMO2/3 chains thereby countering the SUMO-targeted-Ubiquitin-Ligase (StUbL) pathway. Several biochemical studies pinpoint towards the SENPs as critical enzymes to control balanced SUMOylation/deSUMOylation in cardiovascular health and disease. This study aims to review the current knowledge about the SUMO-specific proteases in the heart and provides an integrated view of cardiac functions of the deSUMOylating enzymes under physiological and pathological conditions.
format	article
author	Paul W. Hotz Stefan Müller Luca Mendler
author_facet	Paul W. Hotz Stefan Müller Luca Mendler
author_sort	Paul W. Hotz
title	SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease
title_short	SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease
title_full	SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease
title_fullStr	SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease
title_full_unstemmed	SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease
title_sort	sumo-specific isopeptidases tuning cardiac sumoylation in health and disease
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/7b7ed21fdeb5415085ef9e84f16dcc99
work_keys_str_mv	AT paulwhotz sumospecificisopeptidasestuningcardiacsumoylationinhealthanddisease AT stefanmuller sumospecificisopeptidasestuningcardiacsumoylationinhealthanddisease AT lucamendler sumospecificisopeptidasestuningcardiacsumoylationinhealthanddisease
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SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease

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