tetano
Editor, Senior Moderator
Commun Biol. 2019 Jun 26;2:243. doi: 10.1038/s42003-019-0486-3. eCollection 2019.
[h=1]An influenza-derived membrane tension-modulating peptide regulates cell movement and morphology via actin remodeling.[/h] Masuda T[SUP]1[/SUP], Baba K[SUP]2[/SUP], Nomura T[SUP]3[/SUP], Tsujita K[SUP]4,[/SUP][SUP]5[/SUP], Murayama T[SUP]1[/SUP], Itoh T[SUP]4,[/SUP][SUP]5[/SUP], Takatani-Nakase T[SUP]6[/SUP], Sokabe M[SUP]7[/SUP], Inagaki N[SUP]2[/SUP], Futaki S[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
[h=4]KEYWORDS:[/h] Lamellipodia; Membranes
PMID: 31263787 PMCID: PMC6594980 DOI: 10.1038/s42003-019-0486-3
Free PMC Article
[h=1]An influenza-derived membrane tension-modulating peptide regulates cell movement and morphology via actin remodeling.[/h] Masuda T[SUP]1[/SUP], Baba K[SUP]2[/SUP], Nomura T[SUP]3[/SUP], Tsujita K[SUP]4,[/SUP][SUP]5[/SUP], Murayama T[SUP]1[/SUP], Itoh T[SUP]4,[/SUP][SUP]5[/SUP], Takatani-Nakase T[SUP]6[/SUP], Sokabe M[SUP]7[/SUP], Inagaki N[SUP]2[/SUP], Futaki S[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
[h=4]KEYWORDS:[/h] Lamellipodia; Membranes
PMID: 31263787 PMCID: PMC6594980 DOI: 10.1038/s42003-019-0486-3
Free PMC Article