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The Ubiquitin-Like SUMO System and Heart Function: From Development to Disease.

Mendler L, Braun T, Müller S
Circulation research 2016; 11812016Jan08: 132-44


SUMOylation is a ubiquitin-related transient posttranslational modification pathway catalyzing the conjugation of small ubiquitin-like modifier (SUMO) proteins (SUMO1, SUMO2, and SUMO3) to lysine residues of proteins. SUMOylation targets a wide variety of cellular regulators and thereby affects a multitude of different cellular processes. SUMO/sentrin-specific proteases are able to remove SUMOs from targets, contributing to a tight control of SUMOylated proteins. Genetic and cell biological experiments indicate a critical role of balanced SUMOylation/deSUMOylation for proper cardiac development, metabolism, and stress adaptation. Here, we review the current knowledge about SUMOylation/deSUMOylation in the heart and provide an integrated picture of cardiac functions of the SUMO system under physiologic or pathologic conditions. We also describe potential therapeutic approaches targeting the SUMO machinery to combat heart disease.

Zugehörigkeit: From the Institute of Biochemistry II, Goethe University, Medical School, Frankfurt, Germany (L.M., S.M.); Institute of Biochemistry, Faculty of General Medicine, University of Szeged, Szeged, Hungary (L.M.); and Department I - Cardiac Development and Remodelling, Max Planck Institute for Heart and Lung Research, Bad Nauheim, Germany (T.B.).

Aritkel auf PubMed

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