Related Experiment Video
Updated: May 10, 2025

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Modifying the modifiers: ubiquitination of ADP-ribosylation in human cells
Karla L H Feijs-Žaja1, Jonas Siefert1, Roko Žaja1
1Institute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.
Abstract:
Ubiquitination and ADP-ribosylation are protein post-translational modifications (PTMs) which influence diverse protein properties. In vitro work has indicated that ubiquitin can be ADP-ribosylated and vice versa, ADP-ribose ubiquitinated. An exciting new study by Bejan et al. now demonstrates that ubiquitination of ADP-ribosylated proteins, termed MARUbylation, occurs in human cells.
Related Concept Videos
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Regulation of Expression at Multiple Steps
RNA Editing
Export of Misfolded Proteins out of the ER

