Evidence map›Paper›PMID 31263787›Full record

ArticleCommunications biology2019

An influenza-derived membrane tension-modulating peptide regulates cell movement and morphology via actin remodeling.

Toshihiro Masuda, Kentarou Baba, Takeshi Nomura, Kazuya Tsujita, Tomo Murayama, Toshiki Itoh, Tomoka Takatani-Nakase, Masahiro Sokabe, Naoyuki Inagaki, Shiroh Futaki

Abstract read
In one paragraph

Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Review
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  6. External-field-induced Assembly for Biological Analytical Chemistry.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry
    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

10 authors.

Toshihiro Masuda1Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011 Japan.ORCID 0000-0003-2177-7735
Kentarou Baba2Division of Biological Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0192 Japan.ORCID 0000-0002-3002-3129
Takeshi Nomura3Department of Agro-environmental Sciences, Kyushu University, Fukuoka, 819-0395 Japan.ORCID 0000-0001-8955-3426
Kazuya Tsujita4Division of Membrane Biology, Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe, Hyogo 657-8501 Japan.ORCID 0000-0002-1860-6831
Tomo Murayama1Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011 Japan.
Toshiki Itoh4Division of Membrane Biology, Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe, Hyogo 657-8501 Japan.
Tomoka Takatani-Nakase6Mechanobiology Laboratory, Nagoya University Graduate School of Medicine, 65 Tsurumai, Nagoya, 466-8550 Japan.ORCID 0000-0001-7510-7943
Masahiro Sokabe7School of Pharmacy and Pharmaceutical Sciences, Mukogawa Women's University, Nishinomiya, Hyogo 663-8179 Japan.ORCID 0000-0001-7791-0166
Naoyuki Inagaki2Division of Biological Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0192 Japan.ORCID 0000-0002-2664-9196
Shiroh Futaki1Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011 Japan.ORCID 0000-0002-0124-4002

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tension in cell membranes is closely related to various cellular events, including cell movement and morphogenesis. Therefore, modulation of membrane tension can be a new approach for manipulating cellular events. Here, we show that an amphipathic peptide derived from the influenza M2 protein (M2[45-62]) yields lamellipodia at multiple sites in the cell. Effect of M2[45-62] on cell membrane tension was evaluated by optical tweezer. The membrane tension sensor protein FBP17 was involved in M2[45-62]-driven lamellipodium formation. Lysine-to-arginine substitution in M2[45-62] further enhanced its activity of lamellipodium formation. M2[45-62] had an ability to reduce cell motility, evaluated by scratch wound migration and transwell migration assays. An increase in neurite outgrowth was also observed after treatment with M2[45-62]. The above results suggest the potential of M2[45-62] to modulate cell movement and morphology by modulating cell membrane tension.

Indexed as

ActinsAnimalsArginineCell MembraneCell MovementCell SurvivalChlorocebus aethiopsCOS CellsElectrophysiologyGreen Fluorescent ProteinsHeLa CellsHippocampusHumansInfluenza, HumanLysineMembrane ProteinsActinsArginineGreen Fluorescent ProteinsLysineM2 protein, Influenza A virusMembrane ProteinsPeptidesViral Matrix ProteinsViroporin ProteinsLamellipodiaMembranes

Identifiers

PMID31263787
PMCPMC6594980

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.