TY  - JOUR
A1  - Liu, Yaobin
A1  - Mukherjee, Rukmini
A1  - Bonn, Florian
A1  - Colby, Thomas
A1  - Matić, Ivan
A1  - Glogger, Marius
A1  - Heilemann, Mike
A1  - Đikić, Ivan
T1  - Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
T2  - Cell death and differentiation
N2  - 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 host secretory pathway. Taken together, our study sheds light on the Golgi manipulation strategy by which Legionella hijacks the secretory pathway and promotes bacterial infection.
KW  - Biochemistry
KW  - Cell biology
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/62803
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-628034
SN  - 1476-5403
N1  - This project was funded by European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (ID, grant agreement No 742720), and LOEWE Main Research Focus DynaMem of the German Federal State of Hesse (III L6-519/03/03.001-(O006), to ID). Work in Ivan Matic’s laboratory was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy-CECAD, EXC 2030-390661388 (to IM), and the EMBO Young Investigator Programme (to IM). MH and MG acknowledge funding by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)—Project-ID 253130777—SFB 1177. Open Access funding enabled and organized by Projekt DEAL
VL  - 28
IS  - 10
SP  - 2957
EP  - 2969
PB  - Macmillan
CY  - London
ER  -