Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination

@article{Bhogaraju2016PhosphoribosylationOU,
  title={Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination},
  author={Sagar Bhogaraju and Sissy Kalayil and Yaobin Liu and Florian Bonn and Thomas Colby and Ivan Matic and Ivan Dikic},
  journal={Cell},
  year={2016},
  volume={167},
  pages={1636-1649.e13}
}
Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transfer to host proteins. Here, we identify a phosphodiesterase domain in SdeA that efficiently catalyzes phosphoribosylation of ubiquitin on a specific arginine via an ADP-ribose-ubiquitin intermediate… CONTINUE READING

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