Evidence map›Paper›PMID 27956554›Full record

ArticleThe Journal of biological chemistry2017

The Protein Neddylation Pathway in Trypanosoma brucei: FUNCTIONAL CHARACTERIZATION AND SUBSTRATE IDENTIFICATION.

Shanhui Liao, Huiqing Hu, Tao Wang, Xiaoming Tu, Ziyin Li

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 27 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Shanhui LiaoFrom the Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China and.
Huiqing Huthe Department of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center, Houston, Texas 77030.
Tao Wangthe Department of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center, Houston, Texas 77030.
Xiaoming TuFrom the Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China and xmtu@ustc.edu.cn.
Ziyin Lithe Department of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center, Houston, Texas 77030 ziyin.li@uth.tmc.edu.
The University of Texas Health Science Center at Houston · USUniversity of Science and Technology of China · CN

Funding

Mechanisms Of The Unusual Cytokinesis In TrypanosomesR01AI101437 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, ZIYIN · 2013 to 2025
$6.4M
Regulation of cell cycle transitions by cyclin-dependent kinase in trypanosomesR01AI118736 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, ZIYIN · 2016 to 2025
$3.8M
NIAID NIH HHS R01 AI101437NIAID NIH HHS R01 AI118736
6 · The paper itself

Abstract

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 neddylation remains poorly understood. Here, using Trypanosoma brucei as the model organism, we investigated the function and substrates of TbNedd8. TbNedd8 is distributed throughout the cytosol but enriched in the nucleus and the flagellum. Depletion of TbNedd8 by RNAi abolished global protein ubiquitination, caused DNA re-replication in postmitotic cells, impaired spindle assembly, and compromised the flagellum attachment zone filament, leading to flagellum detachment. Through affinity purification and mass spectrometry, we identified 70 TbNedd8-conjugated and -associated proteins, including known Nedd8-conjugated and -associated proteins, putative TbNedd8 conjugation system enzymes, proteins of diverse biological functions, and proteins of unknown function. Finally, we validated six Cullins as bona fide TbNedd8 substrates and identified the TbNedd8 conjugation site in three Cullins. This work lays the foundation for understanding the roles of protein neddylation in this early divergent parasitic protozoan.

Indexed as

Cullin ProteinsFlagellaProtozoan ProteinsTrypanosoma brucei bruceiUbiquitinationUbiquitinsCullin ProteinsProtozoan ProteinsUbiquitinsCullinDNA replicationflagellummitosismitotic spindleNedd8neddylationparasitologyTrypanosoma brucei

Identifiers

PMID27956554
PMCPMC5247642
OpenAlexW2567184184

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.