Evidence map›Paper›PMID 40443892›Full record

ArticleJACS Au2025

Examining the Role of Threonine Phosphorylation in Ubiquitin's Function Using Chemical Protein Synthesis.

Bingji Wang, Chuntong Li, Fangyu Zhao, Luyu Shi, Xu Li, Yijie Liu, Shuzhe Sun, Ligong Yuan, Maoshen Sun, Yingyue Zhang and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in JACS Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Design and Semisynthesis of Ubiquitin Extension Probes.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
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

12 authors.

Bingji WangCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.
Chuntong LiDepartment of Chemistry, Key Lab of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing 100084, China.
Fangyu ZhaoCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.
Luyu ShiCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.
Xu LiCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.
Yijie LiuCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.
Shuzhe SunDepartment of Chemistry, Key Lab of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing 100084, China.
Ligong YuanDepartment of Thoracic Surgery, the First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230001, China.
Maoshen SunDepartment of Cell Biology, Harvard Medical School, Howard Hughes Medical Institute, Boston, Massachusetts 02115-6027, United States.ORCID https://orcid.org/0000-0002-8602-4817
Yingyue ZhangCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.
Jing ShiCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.ORCID https://orcid.org/0000-0003-0180-4265
Lu-Jun LiangCenter for BioAnalytical Chemistry, Hefei National Laboratory of Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The phosphorylation of ubiquitin significantly enhances the complexity of the ubiquitin code. However, the molecular consequences of ubiquitin phosphorylation at threonine residues remain largely uncharacterized. In this study, we present an effective method for the total chemical synthesis of threonine-phosphorylated ubiquitin, producing tens of milligrams of all six in vivo-identified threonine-phosphorylated ubiquitin analogues: pUbT7, pUbT12, pUbT14, pUbT22, pUbT55, and pUbT66. The biochemical activities of phosphorylated ubiquitin analogues were examined in vitro. Our results show that threonine phosphorylation has a differential impact on E2 charging, with phosphorylation at residue Thr7 exhibiting significant inhibition. In addition, threonine phosphorylation significantly affects the E1-E2-E3-mediated assembly and deubiquitinase-mediated disassembly of polyubiquitin chains in a site-specific manner. Collectively, this work provides new insights into the effect of phosphorylation on the ubiquitin code.

Indexed as

chemical protein synthesisdeubiquitinationpolyubiquitin chainthreonine phosphorylationubiquitin phosphorylation

Identifiers

PMID40443892
PMCPMC12117390

What OpenQuestion holds

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Registered trials

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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.