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| Item Type: | Dataset |
|---|---|
| Title: | Functional landscape of ubiquitin linkages connects K29-linked ubiquitylation to epigenome integrity |
| Creators Name: | Arroyo-Gomez, J., Murray, M.J., Guérillon, C., Wang, J., Isaakova, E., Reveron-Gome, N., Koutrouli, M., Rahmanto, A.S., Mitrofanov, K., Ingham, A., Schovsbo, S., Weischenfeldt, K., Coscia, F., Typas, D., Völker-Albert, M., Solis, V., Jensen, L.J., Groth, A., Mund, A., Beli, P., Shearer, R.F. and Mailand, N. |
| Abstract: | Ubiquitin chains with distinct linkages govern the outcome of numerous critical ubiquitin-dependent signaling processes, but their particular targets and functional impacts remain incompletely understood due to a paucity of tools for their specific detection and manipulation. Here, we applied a cell-based ubiquitin replacement strategy, which allows targeted conditional abrogation of each of the seven lysine-based ubiquitin linkages in human cells, to profile system-wide impacts of disabling formation of individual chain types. This revealed proteins and processes regulated by each of these poly-ubiquitin topologies, as well as indispensable roles of K48-, K63- and K27-linkages in cell proliferation. We show that K29-linked ubiquitylation is strongly associated with chromosome biology, and that the H3K9me3 methyltransferase SUV39H1 is a prominent cellular target of this modification. K29-linked ubiquitylation catalyzed by TRIP12 and reversed by TRABID constitutes the essential degradation signal for SUV39H1 and is primed and extended by Cullin-RING ubiquitin ligase activity. Preventing K29-linkage-dependent SUV39H1 turnover deregulates H3K9me3 homeostasis but not other histone modifications. Collectively, these data resources illuminate cellular functions of linkage-specific ubiquitin chains and establish a key role of K29-linked ubiquitylation in epigenome integrity. |
| Source: | BioStudies |
| Publisher: | EMBL-EBI |
| Date: | 17 October 2025 |
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