Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.07.27.223842v1?rss=1 Authors: Liu, Y., Mukherjee, R., Bonn, F., Colby, T., Matic, I., Dikic, I. Abstract: 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 induces fragmentation of the Golgi stacks due to its ubiquitin ligase activity. The Golgi tethering factors 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 fragmentation 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. Copy rights belong to original authors. Visit the link for more info