DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
Ubiquitylation had been considered limited to protein lysine residues, but other substrates have recently emerged. Here, we show that DELTEX E3 ligases specifically target the 3' hydroxyl of the adenosine diphosphate (ADP)-ribosyl moiety that can be linked to a protein, thus generating a hybrid...
Main Authors: | Zhu, K, Suskiewicz, MJ, Hloušek-Kasun, A, Meudal, H, Mikoč, A, Aucagne, V, Ahel, D, Ahel, I |
---|---|
Format: | Journal article |
Language: | English |
Published: |
American Association for the Advancement of Science
2022
|
Similar Items
-
ADP-ribosylation: new facets of an ancient modification
by: Palazzo, L, et al.
Published: (2017) -
Specificity of DNA ADP-Ribosylation Reversal by NADARs
by: Bara Cihlova, et al.
Published: (2024-04-01) -
Beyond protein modification: the rise of non-canonical ADP-ribosylation
by: Schuller, M, et al.
Published: (2022) -
Specificity of reversible ADP-ribosylation and regulation of cellular processes
by: Crawford, K, et al.
Published: (2017) -
Reversible ADP-ribosylation of RNA
by: Munnur, D, et al.
Published: (2019)