Evidence map›Paper›PMID 35098239›Full record

ArticleJACS Au2022

A Synthetic Multidomain Peptide That Drives a Macropinocytosis-Like Mechanism for Cytosolic Transport of Exogenous Proteins into Plants.

Takaaki Miyamoto, Kiminori Toyooka, Jo-Ann Chuah, Masaki Odahara, Mieko Higchi-Takeuchi, Yumi Goto, Yoko Motoda, Takanori Kigawa, Yutaka Kodama, Keiji Numata

Abstract read
In one paragraph

Article in JACS Au, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Review
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  5. Article
  6. Deciphering the Mechanism of Action of the Antimicrobial Peptide BP100.International journal of molecular sciences · 2024
    Review
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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

10 authors.

Takaaki MiyamotoBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.ORCID https://orcid.org/0000-0002-8192-9342
Kiminori ToyookaTechnology Platform Division, Mass Spectrometry and Microscopy Unit, RIKEN Center for Sustainable Resource Science, Yokohama 230-0045, Japan.
Jo-Ann ChuahBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.
Masaki OdaharaBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.
Mieko Higchi-TakeuchiBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.
Yumi GotoTechnology Platform Division, Mass Spectrometry and Microscopy Unit, RIKEN Center for Sustainable Resource Science, Yokohama 230-0045, Japan.
Yoko MotodaBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.
Takanori KigawaLaboratory for Cellular Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama 230-0045, Japan.ORCID https://orcid.org/0000-0003-0146-9719
Yutaka KodamaBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.
Keiji NumataBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.ORCID https://orcid.org/0000-0003-2199-7420

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Direct delivery of proteins into plants represents a promising alternative to conventional gene delivery for probing and modulating cellular functions without the risk of random integration of transgenes into the host genome. This remains challenging, however, because of the lack of a protein delivery tool applicable to diverse plant species and the limited information about the entry mechanisms of exogenous proteins in plant cells. Here, we present the synthetic multidomain peptide (named dTat-Sar-EED4) for cytosolic protein delivery in various plant species via simple peptide-protein coincubation. dTat-Sar-EED4 enabled the cytosolic delivery of an active enzyme with up to ∼20-fold greater efficiency than previously described cell-penetrating peptides in several model plant systems. Our analyses using pharmacological inhibitors and transmission electron microscopy revealed that dTat-Sar-EED4 triggered a unique endocytic mechanism for cargo protein internalization. This endocytic mechanism shares several features with macropinocytosis, including the dependency of actin polymerization, sensitivity to phosphatidylinositol-3 kinase activity, and formation of membrane protrusions and large intracellular vesicles (>200 nm in diameter), even though macropinocytosis has not been identified to date in plants. Our study thus presents a robust molecular tool that can induce a unique cellular uptake mechanism for the efficient transport of bioactive proteins into plants.

Identifiers

PMID35098239
PMCPMC8790739

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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.