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d-serine is naturally present throughout the human body. It is also used as add-on therapy for treatment-refractory schizophrenia. d-Serine interacts with the strychnine-insensitive glycine binding site of NMDA receptor, and this interaction could lead to potentially toxic activity (i.e., excitotoxi...
ORGANISM(S): Rattus norvegicus 
Here we show that Legionella SidE effectors mediate phosphoribosyl-linked serine ubiquitination (PR-Ub) of the autophagic SNARE proteins STX17 and SNAP29. On the one hand, PR-Ub modification of STX17 enhances its interaction with ATG14L, which drives the recruitment of ER membranes to the bacterial ...
ORGANISM(S): Homo sapiens (Human) 
2025-05-14 | PXD058184 | Pride
Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C-terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transf...
ORGANISM(S): Homo sapiens (Human) 
2016-12-07 | PXD005240 | Pride
The mitochondrial kinase PINK1 and the cytosolic ubiquitin ligase (E3) Parkin is involved in mitochondrial quality control. PINK1, which phosphorylates ubiquitin at serine 65 residue and the ubiquitin-like (Ubl) domain of Parkin at serine 65 residue, promotes the Parkin activation and translocation ...
ORGANISM(S): Homo Sapiens (human) 
Previously, analysis of EGF-induced EGFR ubiquitination by mass spectrometry revealed that ubiquitinated lysine residues were located in the TKD of EGFR. However, the specific lysine residues for the CBL-mediated polyubiquitination have not been identified. To investigate the differences in EGFR ubi...
ORGANISM(S): Homo sapiens (Human) 
2021-09-10 | PXD024279 | Pride
Previous study reported that eIF4A1 protein stability is subject to control by the ubiquitin-proteasome pathway, and deubiquitinase USP9X elevated eIF4A1 protein level by promoting eIF4A1 deubiquitination. However, the E3 ubiquitin ligases responsible for eIF4A1 proteolysis is not determined. Our re...
ORGANISM(S): Homo sapiens (Human) 
2024-05-10 | PXD039031 | Pride
Our previous studies have implicated CHIP as a co-chaperone/ubiquitin ligase, whose activities yield protection against stress-induced apoptotic events. In this report, we demonstrate a stress-dependent interaction between CHIP (carboxyl terminus of Hsp70-interacting protein) and Daxx, death domain-...
ORGANISM(S): Mus musculus 
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