TY  - JOUR
A1  - Tolay, Nazife
A1  - Buchberger, Alexander
T1  - Role of the ubiquitin system in stress granule metabolism
JF  - International Journal of Molecular Sciences
N2  - Eukaryotic cells react to various stress conditions with the rapid formation of membrane-less organelles called stress granules (SGs). SGs form by multivalent interactions between RNAs and RNA-binding proteins and are believed to protect stalled translation initiation complexes from stress-induced degradation. SGs contain hundreds of different mRNAs and proteins, and their assembly and disassembly are tightly controlled by post-translational modifications. The ubiquitin system, which mediates the covalent modification of target proteins with the small protein ubiquitin (‘ubiquitylation’), has been implicated in different aspects of SG metabolism, but specific functions in SG turnover have only recently emerged. Here, we summarize the evidence for the presence of ubiquitylated proteins at SGs, review the functions of different components of the ubiquitin system in SG formation and clearance, and discuss the link between perturbed SG clearance and the pathogenesis of neurodegenerative disorders. We conclude that the ubiquitin system plays an important, medically relevant role in SG biology.
KW  - 26S proteasome
KW  - p97/VCP
KW  - Cdc48
KW  - DUB
KW  - G3BP
KW  - granulostasis
KW  - granulophagy
KW  - ALS
Y1  - 2022
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-284061
SN  - 1422-0067
VL  - 23
IS  - 7
ER  - 
TY  - JOUR
A1  - Auer, Daniela
A1  - Hügelschäffer, Sophie D.
A1  - Fischer, Annette B.
A1  - Rudel, Thomas
T1  - The chlamydial deubiquitinase Cdu1 supports recruitment of Golgi vesicles to the inclusion
JF  - Cellular Microbiology
N2  - Chlamydia trachomatis is the main cause of sexually transmitted diseases worldwide. As obligate intracellular bacteria Chlamydia replicate in a membrane bound vacuole called inclusion and acquire nutrients for growth and replication from their host cells. However, like all intracellular bacteria, Chlamydia have to prevent eradication by the host's cell autonomous system. The chlamydial deubiquitinase Cdu1 is secreted into the inclusion membrane, facing the host cell cytosol where it deubiquitinates cellular proteins. Here we show that inactivation of Cdu1 causes a growth defect of C. trachomatis in primary cells. Moreover, ubiquitin and several autophagy receptors are recruited to the inclusion membrane of Cdu1‐deficient Chlamydia . Interestingly, the growth defect of cdu1 mutants is not rescued when autophagy is prevented. We find reduced recruitment of Golgi vesicles to the inclusion of Cdu1 mutants indicating that vesicular trafficking is altered in bacteria without active deubiquitinase (DUB). Our work elucidates an important role of Cdu1 in the functional preservation of the chlamydial inclusion surface.
KW  - autophagy
KW  - Cdu1
KW  - ChlaDUB1
KW  - Chlamydia trachomatis
KW  - DUB
KW  - Golgi
KW  - xenophagy
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-208675
VL  - 22
IS  - 5
ER  -