title: Control of nuclear activities by substrate-selective and protein-group SUMOylation.
abstract: Reversible modification of proteins by SUMO (small ubiquitin-like modifier) affects a large number of cellular processes. In striking contrast to the related ubiquitin pathway, only a few enzymes participate in the SUMO system, although this pathway has numerous substrates as well. Emerging evidence suggests that SUMOylation frequently targets entire groups of physically interacting proteins rather than individual proteins. Protein-group SUMOylation appears to be triggered by recruitment of SUMO ligases to preassembled protein complexes. Because SUMOylation typically affects groups of proteins that bear SUMO-interaction motifs (SIMs), protein-group SUMOylation may foster physical interactions between proteins through multiple SUMO-SIM interactions. Individual SUMO modifications may act redundantly or additively, yet they may mediate dedicated functions as well. In this review, we focus on the unorthodox principles of this pathway and give examples for SUMO-controlled nuclear activities. We propose that collective SUMOylation is typical for nuclear assemblies and argue that SUMO serves as a distinguishing mark for functionally engaged protein fractions.
authors.affiliation: Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; email: jentsch@biochem.mpg.de.
authors.forename: Stefan
authors.initials: S
authors.lastname: Jentsch
authors.forename: Ivan
authors.initials: I
authors.lastname: Psakhye
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D020816:Amino Acid Motifs; D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism* / Q000648:ultrastructure; D004260:DNA Repair / Q000502:physiology; D004798:Enzymes / Q000378:metabolism; D006801:Humans; D008239:Lysine / Q000378:metabolism; D008954:Models, Biological; D046912:Multiprotein Complexes; D009687:Nuclear Proteins / Q000378:metabolism; D018809:Proliferating Cell Nuclear Antigen / Q000378:metabolism; D025941:Protein Interaction Mapping; D011506:Proteins / Q000378:metabolism*; D040901:Proteomics; D012270:Ribosomes / Q000378:metabolism; D013379:Substrate Specificity; D058207:Sumoylation / Q000235:genetics / Q000502:physiology*; D016615:Telomere / Q000378:metabolism; D059505:Telomere Homeostasis / Q000502:physiology; D044763:Ubiquitin-Conjugating Enzymes / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism; D054875:Ubiquitination; D000074405:Valosin Containing Protein; D000098843:Ubiquitin-Conjugating Enzyme UBC9
chemical_list: D018797:Cell Cycle Proteins; D004798:Enzymes; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D018809:Proliferating Cell Nuclear Antigen; D011506:Proteins; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases; D000251:Adenosine Triphosphatases; D000074405:Valosin Containing Protein; D000098843:Ubiquitin-Conjugating Enzyme UBC9; D008239:Lysine