title: A differential requirement for SUMOylation in proliferating and non-proliferating cells during Drosophila development.
abstract: SUMOylation is a highly conserved post-translational modification shown to modulate target protein activity in a wide variety of cellular processes. Although the requirement for SUMO modification of specific substrates has received significant attention in vivo and in vitro, the developmental requirements for SUMOylation at the cell and tissue level remain poorly understood. Here, we show that in Drosophila melanogaster, both heterodimeric components of the SUMO E1-activating enzyme are zygotically required for mitotic progression but are dispensable for cell viability, homeostasis and DNA synthesis in non-dividing cells. Explaining the lack of more pleiotropic effects following a global block of SUMO conjugation, we further demonstrate that low levels of global substrate SUMOylation are detected in mutants lacking either or both E1 subunits. These results not only suggest that minimal SUMOylation persists in the absence of Aos1/Uba2, but also show that the process of cell division is selectively sensitive to reductions in global SUMOylation. Supporting this view, knockdown of SUMO or its E1 and E2 enzymes robustly disrupts proliferating cells in the developing eye, without any detectable effects on the development or differentiation of neighboring post-mitotic cells.
authors: Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110,  USA.
authors: Kiriaki
authors: K
authors: Kanakousaki
authors: Matthew C
authors: MC
authors: Gibson
mesh_terms: D000818:Animals; D049109:Cell Proliferation; D002470:Cell Survival; D003433:Crosses, Genetic; D029721:Drosophila Proteins / Q000378:metabolism / Q000502:physiology*; D004331:Drosophila melanogaster / Q000196:embryology*; D018507:Gene Expression Regulation, Developmental; D023281:Genomics; D006706:Homeostasis; D060227:Imaginal Discs / Q000196:embryology; D008025:Ligases / Q000378:metabolism; D008938:Mitosis; D008957:Models, Genetic; D009154:Mutation; D009687:Nuclear Proteins / Q000378:metabolism / Q000502:physiology*; D017956:Photoreceptor Cells, Invertebrate / Q000502:physiology*; D034622:RNA Interference; D012469:Salivary Glands / Q000196:embryology; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D044764:Ubiquitin-Activating Enzymes / Q000378:metabolism / Q000502:physiology*
chemical_list: D029721:Drosophila Proteins; D009687:Nuclear Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; D008025:Ligases; C542423:Uba1 protein, Drosophila; D044764:Ubiquitin-Activating Enzymes; C429037:uba2 protein, Drosophila; C404950:Aos1 protein, Drosophila