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Commun Biol. 2019 Jun 26;2:243. doi: 10.1038/s42003-019-0486-3. eCollection 2019.

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

Author information

1
1Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011 Japan.
2
2Division of Biological Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0192 Japan.
3
3Department of Agro-environmental Sciences, Kyushu University, Fukuoka, 819-0395 Japan.
4
4Division of Membrane Biology, Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe, Hyogo 657-8501 Japan.
5
5Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe, Hyogo 650-0017 Japan.
6
6Mechanobiology Laboratory, Nagoya University Graduate School of Medicine, 65 Tsurumai, Nagoya, 466-8550 Japan.
7
7School of Pharmacy and Pharmaceutical Sciences, Mukogawa Women's University, Nishinomiya, Hyogo 663-8179 Japan.

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.

KEYWORDS:

Lamellipodia; Membranes

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