Non-nuclear function of sumoylated proteins

• Published in: Biochimica et biophysica acta. Molecular cell research Vol. 1843; no. 12; pp. 2878 - 2885
• Main Authors: Wasik, Urszula, Filipek, Anna
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01-12-2014
• Subjects: Autophagy; Cytoskeletal function; Enzyme activity; Exocytosis; Mitochondrial dynamics; Receptor function; Receptor function; Enzyme activity; COS-7; Mitochondrial dynamics; RhoGDI; Kv; Ubc9; Exocytosis; Autophagy; PIAS; Drp1; KAP1; KARs; Vps; TGF-β; Rac1; Cytoskeletal function; TRPM4; TβRI; hnRNPA2B1; SUMO; K2P; CASK; PKC; MAPK; SENPs; RGSZ1; FAK; PTP1B; RGSZ2; RIM; mGluRs; RGS
• ISSN: 0167-4889; 1879-2596
• DOI: 10.1016/j.bbamcr.2014.07.018

Post-translational modification by the SUMO moiety is now regarded as one of the key regulatory modifications in eukaryotic cells. Up to now, plenty of sumoylated proteins have been found to be involved in nuclear processes such as chromatin organization, transcription and DNA repair as well as in other cellular functions. Since the number of data concerning sumoylated proteins and their function outside the nucleus has grown rapidly, in this review we summarized the results describing the non-nuclear role of SUMO substrates. In particular, we focused on the role of sumoylation in the regulation of channel activity, receptor function, G-protein signaling, activity of enzymes, cytoskeletal organization, exocytosis, autophagy and mitochondrial dynamics.
•Sumoylation is an important regulatory modification in eukaryotic cells.•Besides nuclear proteins, cytosolic and membrane proteins are also sumoylated.•Sumoylation regulates the function of multiple cellular proteins.