The Protein Neddylation Pathway in Trypanosoma brucei: FUNCTIONAL CHARACTERIZATION AND SUBSTRATE IDENTIFICATION.
作者： Shanhui Liao , Huiqing Hu , Tao Wang , Xiaoming Tu , Ziyin Li
关键词: NEDD8 、 Cullin Proteins 、 Cullin 、 Protein ubiquitination 、 Protein neddylation 、 Neddylation 、 Trypanosoma brucei 、 Flagellum 、 Biology 、 Cell biology 、 Biochemistry
摘要: Protein posttranslational modifications such as neddylation play crucial roles in regulating protein function. Only a few neddylated substrates have been validated to date, and the role of remains poorly understood. Here, using Trypanosoma brucei model organism, we investigated function TbNedd8. TbNedd8 is distributed throughout cytosol but enriched nucleus flagellum. Depletion by RNAi abolished global ubiquitination, caused DNA re-replication postmitotic cells, impaired spindle assembly, compromised flagellum attachment zone filament, leading detachment. Through affinity purification mass spectrometry, identified 70 TbNedd8-conjugated -associated proteins, including known Nedd8-conjugated putative conjugation system enzymes, proteins diverse biological functions, unknown Finally, six Cullins bona fide site three Cullins. This work lays foundation for understanding this early divergent parasitic protozoan.
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