Evidence map›Paper›PMID 35309941›Full record

ArticleFrontiers in cell and developmental biology2022

Phosphorylation of MAD2 at Ser195 Promotes Spindle Checkpoint Defects and Sensitizes Cancer Cells to Radiotherapy in ATM Deficient Cells.

Yang Wang, Tianyu Yu, Yi Han, Yazhi He, Yiran Song, Leiming Guo, Liwei An, Chunying Yang, Feng Wang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in cell and developmental biology, 2022. 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
0.5field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

9 authors at 2 institutions in 1 country.

Yang WangDepartment of Gastroenterology, Shanghai 10th People's Hospital, Tongji University School of Medicine, Shanghai, China.
Tianyu YuDepartment of General Surgery, Pudong New Area Gongli Hospital Affiliated to Naval Military Medical University, Naval Military Medical University, Shanghai, China.
Yi HanDepartment of Gastroenterology, Shanghai 10th People's Hospital, Tongji University School of Medicine, Shanghai, China.
Yazhi HeDepartment of Gastroenterology, Shanghai 10th People's Hospital, Tongji University School of Medicine, Shanghai, China.
Yiran SongDepartment of Gastroenterology, Shanghai 10th People's Hospital, Tongji University School of Medicine, Shanghai, China.
Leiming GuoDepartment of R&D, Shanghai Creative Immune Therapeutics Co., Ltd, Shanghai, China.
Liwei AnDepartment of Gastroenterology, Shanghai 10th People's Hospital, Tongji University School of Medicine, Shanghai, China.
Chunying YangCentral Laboratory, Shanghai Putuo District People's Hospital, Tongji University School of Medicine, Shanghai, China.
Feng WangDepartment of Gastroenterology, Shanghai 10th People's Hospital, Tongji University School of Medicine, Shanghai, China.
Tongji University · CNSecond Military Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spindle assembly checkpoint (SAC) is a critical monitoring device in mitosis for the maintenance of genomic stability. Specifically, the SAC complex comprises several factors, including Mad1, Mad2, and Bub1. Ataxia-telangiectasia mutated (ATM) kinase, the crucial regulator in DNA damage response (DDR), also plays a critical role in mitosis by regulating Mad1 dimerization and SAC. Here, we further demonstrated that ATM negatively regulates the phosphorylation of Mad2, another critical component of the SAC, which is also involved in DDR. Mechanistically, we found that phosphorylation of Mad2 is aberrantly increased in ATM-deficient cells. Point-mutation analysis further revealed that Serine 195 mainly mediated Mad2 phosphorylation upon ATM ablation. Functionally, the phosphorylation of Mad2 causes decreased DNA damage repair capacity and is related to the resistance to cancer cell radiotherapy. Altogether, this study unveils the key regulatory role of Mad2 phosphorylation in checkpoint defects and DNA damage repair in ATM-deficient cells.

Indexed as

ATM kinasecheckpoint defectDNA damage repairmad2phosphorylation

Identifiers

PMID35309941
PMCPMC8924061
OpenAlexW4214909694

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.