Evidence map›Paper›PMID 34452999›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Ssu72 phosphatase directly binds to ZAP-70, thereby providing fine-tuning of TCR signaling and preventing spontaneous inflammation.

Jae Sung Ko, Dongjin Jeong, Jaemoon Koh, Hyeryeon Jung, Kyeong Cheon Jung, Yoon Kyung Jeon, Hye Young Kim, Eugene C Yi, Ho Lee, Chang-Woo Lee and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

6 citing papers in PubMed, 7 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

11 authors at 2 institutions in 1 country.

Jae Sung KoLaboratory of Immune Regulation, Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Korea.ORCID 0000-0003-3195-5910
Dongjin JeongLaboratory of Immune Regulation, Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Korea.
Jaemoon KohDepartment of Pathology, Seoul National University College of Medicine, Seoul 03080, Korea.ORCID 0000-0002-2824-5080
Hyeryeon JungDepartment of Molecular Medicine and Biopharmaceutical Sciences, School of Convergence Science and Technology, Seoul National University, Seoul 08826, Korea.ORCID 0000-0001-5179-8604
Kyeong Cheon JungDepartment of Pathology, Seoul National University College of Medicine, Seoul 03080, Korea.
Yoon Kyung JeonDepartment of Pathology, Seoul National University College of Medicine, Seoul 03080, Korea.
Hye Young KimLaboratory of Immune Regulation, Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Korea.ORCID 0000-0001-5978-512X
Eugene C YiDepartment of Molecular Medicine and Biopharmaceutical Sciences, School of Convergence Science and Technology, Seoul National University, Seoul 08826, Korea.
Ho LeeGraduate School of Cancer Science and Policy, National Cancer Center, Goyang 10408, Korea.
Chang-Woo LeeDepartment of Pathology, Seoul National University College of Medicine, Seoul 03080, Korea; doohyun@snu.ac.kr cwlee1234@skku.edu.
Doo Hyun ChungLaboratory of Immune Regulation, Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Korea; doohyun@snu.ac.kr cwlee1234@skku.edu.ORCID 0000-0002-9948-8485
Seoul National University · KRNational Cancer Center · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ZAP-70 is required for the initiation of T cell receptor (TCR) signaling, and Ssu72 is a phosphatase that regulates RNA polymerase II activity in the nucleus. However, the mechanism by which ZAP-70 regulates the fine-tuning of TCR signaling remains elusive. Here, we found that Ssu72 contributed to the fine-tuning of TCR signaling by acting as tyrosine phosphatase for ZAP-70. Affinity purification-mass spectrometry and an in vitro assay demonstrated specific interaction between Ssu72 and ZAP-70 in T cells. Upon TCR stimulation, Ssu72-deficient T cells increased the phosphorylation of ZAP-70 and downstream molecules and exhibited hyperresponsiveness, which was restored by reducing ZAP-70 phosphorylation. In vitro assay demonstrated that recombinant Ssu72 reduced tyrosine phosphorylation of ZAP-70 via phosphatase activity.

Indexed as

AnimalsCD8-Positive T-LymphocytesCell CommunicationInflammationMemory T CellsMiceMice, Inbred C57BLMice, KnockoutPhosphoprotein PhosphatasesPhosphorylationReceptors, Antigen, T-CellZAP-70 Protein-Tyrosine KinasePhosphoprotein PhosphatasesReceptors, Antigen, T-Cellssu72 protein, mouseZap70 protein, mouseZAP-70 Protein-Tyrosine Kinaseautoimmunityfine-tuningphosphatase Ssu72tyrosine phosphorylationZAP-70

Identifiers

PMID34452999
PMCPMC8536320
OpenAlexW3193791071

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.