Evidence map›Paper›PMID 34462553›Full record

ArticleCell death and differentiation2022

Non-canonical phosphorylation of Bmf by p38 MAPK promotes its apoptotic activity in anoikis.

Zhe Zhi, Zhenlin Ouyang, Yibo Ren, Ying Cheng, Peijun Liu, Yurong Wen, Yongping Shao

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 38 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

7 authors at 3 institutions in 1 country.

Zhe ZhiFrontier Institute of Science and Technology, Xi'an Jiaotong University, Xi'an, China.
Zhenlin OuyangDepartment of Talent Highland, The First Affiliated Hospital, Xi'an Jiaotong University, Xi'an, China.
Yibo RenFrontier Institute of Science and Technology, Xi'an Jiaotong University, Xi'an, China.
Ying ChengThe Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an, China.
Peijun LiuCenter for Translational Medicine, The First Affiliated Hospital, Xi'an Jiaotong University, Xi'an, China.ORCID http://orcid.org/0000-0003-0529-387X
Yurong WenDepartment of Talent Highland, The First Affiliated Hospital, Xi'an Jiaotong University, Xi'an, China.
Yongping ShaoFrontier Institute of Science and Technology, Xi'an Jiaotong University, Xi'an, China. yongping.shao@mail.xjtu.edu.cn.ORCID http://orcid.org/0000-0002-2400-1070
First Affiliated Hospital of Xi'an Jiaotong University · CNXi'an Jiaotong University · CNSecond Affiliated Hospital of Xi'an Jiaotong University · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31771557National Natural Science Foundation of China (National Science Foundation of China) 31870132National Natural Science Foundation of China (National Science Foundation of China) 31970724National Natural Science Foundation of China (National Science Foundation of China) 82072237
6 · The paper itself

Abstract

Bmf contributes to the onset of anoikis by translocating from cytoskeleton to mitochondria when cells lose attachment to the extracellular matrix. However, the structural details of Bmf cytoskeleton tethering and the control of Bmf release upon loss of anchorage remained unknown. Here we showed that cell detachment induced rapid and sustained activation of p38 MAPK in mammary epithelial cell lines. Inhibition of p38 signaling or Bmf knockdown rescued anoikis. Activated p38 MAPK could directly phosphorylate Bmf at multiple sites including a non-proline-directed site threonine 72 (T72). Crystallographic studies revealed that Bmf T72 directly participated in DLC2 binding and its phosphorylation would block Bmf/DLC2 interaction through steric hindrance. Finally, we showed that phosphomimetic mutation of T72 enhanced Bmf apoptotic activity in vitro and in a knock-in mouse model. This work unraveled a novel regulatory mechanism of Bmf activity during anoikis and provided structural basis for Bmf cytoskeleton tethering and dissociation.

Indexed as

Anoikisp38 Mitogen-Activated Protein KinasesAdaptor Proteins, Signal TransducingAnimalsEpithelial CellsMicePhosphorylationSignal TransductionAdaptor Proteins, Signal TransducingBmf protein, mousep38 Mitogen-Activated Protein Kinases

Identifiers

PMID34462553
PMCPMC8817011
OpenAlexW3197841292

What Socratic 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 Socratic graph.