Evidence map›Paper›PMID 26306039›Full record

ArticleThe Journal of biological chemistry2015

Death-associated Protein 3 Regulates Mitochondrial-encoded Protein Synthesis and Mitochondrial Dynamics.

Lin Xiao, Hongxu Xian, Kit Yee Lee, Bin Xiao, Hongyan Wang, Fengwei Yu, Han-Ming Shen, Yih-Cherng Liou

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

33 citing papers in PubMed, 47 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

8 authors at 2 institutions in 1 country.

Lin XiaoFrom the Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543.
Hongxu XianFrom the Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543.
Kit Yee LeeFrom the Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543.
Bin XiaoFrom the Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543.
Hongyan Wangthe Neuroscience and Behavioural Disorders Program, Duke-NUS Graduate Medical School, Singapore 169857, the NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, Singapore 117573.
Fengwei Yuthe NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, Singapore 117573, the Temasek Life Sciences Laboratory and Department of Biological Sciences, National University of Singapore, 1 Research Link, Singapore 117604, and.
Han-Ming Shenthe Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore.
Yih-Cherng LiouFrom the Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543, the NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, Singapore 117573, dbslyc@nus.edu.sg.
National University of Singapore · SGDuke-NUS Medical School · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial morphologies change over time and are tightly regulated by dynamic machinery proteins such as dynamin-related protein 1 (Drp1), mitofusion 1/2, and optic atrophy 1 (OPA1). However, the detailed mechanisms of how these molecules cooperate to mediate fission and fusion remain elusive. DAP3 is a mitochondrial ribosomal protein that involves in apoptosis, but its biological function has not been well characterized. Here, we demonstrate that DAP3 specifically localizes in the mitochondrial matrix. Knockdown of DAP3 in mitochondria leads to defects in mitochondrial-encoded protein synthesis and abnormal mitochondrial dynamics. Moreover, depletion of DAP3 dramatically decreases the phosphorylation of Drp1 at Ser-637 on mitochondria, enhancing the retention time of Drp1 puncta on mitochondria during the fission process. Furthermore, autophagy is inhibited in the DAP3-depleted cells, which sensitizes cells to different types of death stimuli. Together, our results suggest that DAP3 plays important roles in mitochondrial function and dynamics, providing new insights into the mechanism of a mitochondrial ribosomal protein function in cell death.

Indexed as

Mitochondrial DynamicsProtein BiosynthesisAnimalsApoptosis Regulatory ProteinsAutophagyCell LineDynaminsGene Knockdown TechniquesGene Knockout TechniquesHomeostasisHumansMembrane ProteinsMiceMitochondriaMitochondrial ProteinsPhosphorylationApoptosis Regulatory ProteinsDAP3 protein, humanDnm1l protein, mouseDynaminsMembrane ProteinsMff protein, humanMitochondrial ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA, Small InterferingSerineautophagycell deathcell signalingDrp1, DAP3metabolismmitochondria

Identifiers

PMID26306039
PMCPMC4599003
OpenAlexW1902911958

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.