RT Journal Article
SR Electronic
T1 Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.07.27.223842
DO 10.1101/2020.07.27.223842
A1 Yaobin Liu
A1 Rukmini Mukherjee
A1 Florian Bonn
A1 Thomas Colby
A1 Ivan Matic
A1 Marius Glogger
A1 Mike Heilemann
A1 Ivan Dikic
YR 2020
UL http://biorxiv.org/content/early/2020/11/19/2020.07.27.223842.abstract
AB SidE family of Legionella effectors catalyze non-canonical phosphoribosyl-linked ubiquitination (PR-ubiquitination) of host proteins during bacterial infection. SdeA localizes predominantly to ER and partially to the Golgi apparatus, and mediates serine ubiquitination of multiple ER and Golgi proteins. Here we show that SdeA causes disruption of Golgi integrity due to its ubiquitin ligase activity. The Golgi linking proteins GRASP55 and GRASP65 are PR-ubiquitinated on multiple serine residues, thus preventing their ability to cluster and form oligomeric structures. In addition, we found that the functional consequence of Golgi disruption is not linked to the recruitment of Golgi membranes to the growing Legionella-containing vacuoles. Instead, it affects the secretory pathway, including cytokine release in cells. Taken together, our study sheds light on the Golgi manipulation strategy by which Legionella hijacks the secretory pathway and promotes bacterial infection.Competing Interest StatementThe authors have declared no competing interest.