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

• Published in: Communications biology Vol. 2; no. 1; p. 243
• Main Authors: Masuda, Toshihiro, Baba, Kentarou, Nomura, Takeshi, Tsujita, Kazuya, Murayama, Tomo, Itoh, Toshiki, Takatani-Nakase, Tomoka, Sokabe, Masahiro, Inagaki, Naoyuki, Futaki, Shiroh
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 26.06.2019; Nature Publishing Group
• Subjects: 14/19; 631/80/84/1756; 631/92/314; 82/75; 9/74; 96/35; Actin; Actins - chemistry; Animals; Arginine; Arginine - chemistry; Axonogenesis; Biology; Biomedical and Life Sciences; Cell Membrane - chemistry; Cell membranes; Cell morphology; Cell Movement; Cell Survival; Chlorocebus aethiops; COS Cells; Cytology; Electrophysiology; Green Fluorescent Proteins - chemistry; HeLa Cells; Hippocampus; Hippocampus - metabolism; Humans; Influenza; Influenza, Human - virology; Lamellipodia; Life Sciences; Lysine; Lysine - chemistry; Membrane proteins; Membrane Proteins - chemistry; Morphogenesis; Morphology; Optical Tweezers; Peptides; Peptides - chemistry; Polymerization; Proteins; Pseudopodia; Pseudopodia - chemistry; Rats; RNA Interference; Viral Matrix Proteins - chemistry; Wound Healing; Lamellipodia; Membranes
• ISSN: 2399-3642; 2399-3642
• DOI: 10.1038/s42003-019-0486-3

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. Toshihiro Masuda et al. find an amphiphilic peptide derived from the influenza M2 protein, M2[45–62], which causes small actin-rich lamellipodia at multiple sites in the cell, inhibiting cell movement by decreasing membrane tension. They show that M2[45–62] stimulates actin polymerization in rat hippocampal neurons.