Evidence map›Paper›PMID 35906209›Full record

ArticleNature communications2022

Defunctionalizing intracellular organelles such as mitochondria and peroxisomes with engineered phospholipase A/acyltransferases.

Satoshi Watanabe, Yuta Nihongaki, Kie Itoh, Toru Uyama, Satoshi Toda, Shigeki Watanabe, Takanari Inoue

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. The Phospholipase AJournal of lipid and atherosclerosis · 2026
    Review
  2. Recent Progress inInternational journal of molecular sciences · 2025
    Review
  3. Synthetic Lipid Biology.Chemical reviews · 2025
    Review
  4. Article
  5. Review
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 2 countries.

Satoshi WatanabeJohns Hopkins University School of Medicine, Department of Cell Biology, Baltimore, MD, 21205, USA. s-watanabe@protein.osaka-u.ac.jp.ORCID 0000-0002-8129-6223
Yuta NihongakiJohns Hopkins University School of Medicine, Department of Cell Biology, Baltimore, MD, 21205, USA.ORCID 0000-0002-9818-9344
Kie ItohJohns Hopkins University School of Medicine, Department of Cell Biology, Baltimore, MD, 21205, USA.
Toru UyamaDepartment of Biochemistry, Kagawa University School of Medicine, 1750-1 Ikenobe, Miki, Kagawa, 761-0793, Japan.
Satoshi TodaWPI Nano Life Science Institute, Kanazawa University, Kanazawa, 920-1192, Japan.ORCID 0000-0003-4997-9558
Shigeki WatanabeJohns Hopkins University School of Medicine, Department of Cell Biology, Baltimore, MD, 21205, USA.ORCID 0000-0001-7580-8141
Takanari InoueJohns Hopkins University School of Medicine, Department of Cell Biology, Baltimore, MD, 21205, USA. jctinoue@jhmi.edu.ORCID 0000-0002-7957-7624
Johns Hopkins University · USKagawa University · JPKanazawa University · JP

Funding

Reviving electron microscopy for synaptic cell biologyDP2NS111133 · NINDS · JOHNS HOPKINS UNIVERSITY · PI WATANABE, SHIGEKI · 2018 to 2018
$2.5M
ActuAtor, a molecular tool for generating force in living cellsR01GM136858 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI INOUE, TAKANARI · 2020 to 2022
$983k
NIGMS NIH HHS R01 GM136858NINDS NIH HHS DP2 NS111133
6 · The paper itself

Abstract

Organelles vitally achieve multifaceted functions to maintain cellular homeostasis. Genetic and pharmacological approaches to manipulate individual organelles are powerful in probing their physiological roles. However, many of them are either slow in action, limited to certain organelles, or rely on toxic agents. Here, we design a generalizable molecular tool utilizing phospholipase A/acyltransferases (PLAATs) for rapid defunctionalization of organelles via remodeling of the membrane phospholipids. In particular, we identify catalytically active PLAAT truncates with minimal unfavorable characteristics. Chemically-induced translocation of the optimized PLAAT to the mitochondria surface results in their rapid deformation in a phospholipase activity dependent manner, followed by loss of luminal proteins as well as dissipated membrane potential, thus invalidating the functionality. To demonstrate wide applicability, we then adapt the molecular tool in peroxisomes, and observe leakage of matrix-resident functional proteins. The technique is compatible with optogenetic control, viral delivery and operation in primary neuronal cultures. Due to such versatility, the PLAAT strategy should prove useful in studying organelle biology of diverse contexts.

Indexed as

AcyltransferasesPeroxisomesHomeostasisMitochondriaOrganellesPhospholipasesAcyltransferasesPhospholipases

Identifiers

PMID35906209
PMCPMC9338259
OpenAlexW4288712640

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.