Yaobin Liu
Goethe University Frankfurt
5 Papers
15 Citations
Yaobin Liu is an academic researcher from Goethe University Frankfurt. The author has contributed to research in topics: Ubiquitin & Vacuole. The author has an hindex of 3, co-authored 5 publications.
Chat about Author
Papers
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
Sagar Bhogaraju,Sissy Kalayil,Yaobin Liu,Florian Bonn,Thomas Colby,Ivan Matic,Ivan Dikic,Ivan Dikic +7 more
TL;DR: A phosphodiesterase domain in SdeA is identified that efficiently catalyzes phosphoribosylation of ubiquitin on a specific arginine via an ADP-ribose-ubiquitin intermediate and it is proposed that phosphorIBosylations of ubiqu itin potently modulates ubiquit in mammalian cells.
280
Regulation of Phosphoribosyl-Linked Serine Ubiquitination by Deubiquitinases DupA and DupB.
Donghyuk Shin,Donghyuk Shin,Rukmini Mukherjee,Yaobin Liu,Alexis Gonzalez,Florian Bonn,Yan Liu,Vladimir V. Rogov,Marcel Heinz,Marcel Heinz,Alexandra Stolz,Gerhard Hummer,Gerhard Hummer,Volker Dötsch,Zhao-Qing Luo,Sagar Bhogaraju,Ivan Dikic,Ivan Dikic +17 more
TL;DR: The deubiquitinases for PR ubiquitination (DUPs; DupA and DupB) were identified in Legionella pneumophila infection as mentioned in this paper, and they were used to identify host proteins involved in endoplasmic reticulum fragmentation and membrane recruitment to Legionella-containing vacuoles.
122
Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
TL;DR: Light is shed on the Golgi manipulation strategy by which Legionella hijacks the secretory pathway and promotes bacterial infection by showing that SdeA causes disruption of Golgi integrity due to its ubiquitin ligase activity.
27
Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection.
Yaobin Liu,Rukmini Mukherjee,Florian Bonn,Thomas Colby,Ivan Matic,Ivan Matic,Marius Glogger,Mike Heilemann,Ivan Dikic +8 more
TL;DR: In this paper, it was shown that SdeA causes disruption of Golgi integrity due to its ubiquitin ligase activity, which is not linked to the recruitment of the Golgi membranes to the growing Legionella-containing vacuoles.
Insights into catalysis and function of phosphoribosyl-linked serine ubiquitination.
Sissy Kalayil,Sagar Bhogaraju,Florian Bonn,Donghyuk Shin,Yaobin Liu,Ninghai Gan,Jérôme Basquin,Paolo Grumati,Zhao-Qing Luo,Ivan Dikic +9 more
TL;DR: The structure of the catalytic core of SdeA, comprising mono-ADP-ribosyltransferase (mART) and phosphodiesterase (PDE) domains, is described and light is shed on the activity of two distinct catalytic sites for serine ubiquitination.