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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.
Masuda T1, Baba K2, Nomura T3, Tsujita K4,5, Murayama T1, Itoh T4,5, Takatani-Nakase T6, Sokabe M7, Inagaki N2, Futaki S1.
Author information
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
PMID: 31263787 PMCID: PMC6594980 DOI: 10.1038/s42003-019-0486-3
Free PMC Article
An influenza-derived membrane tension-modulating peptide regulates cell movement and morphology via actin remodeling.
Masuda T1, Baba K2, Nomura T3, Tsujita K4,5, Murayama T1, Itoh T4,5, Takatani-Nakase T6, Sokabe M7, Inagaki N2, Futaki S1.
Author information
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
PMID: 31263787 PMCID: PMC6594980 DOI: 10.1038/s42003-019-0486-3
Free PMC Article