IRSp53 senses negative membrane curvature and phase separates along membrane tubules

• Published in: Nature communications Vol. 6; no. 1; p. 8529
• Main Authors: Prévost, Coline, Zhao, Hongxia, Manzi, John, Lemichez, Emmanuel, Lappalainen, Pekka, Callan-Jones, Andrew, Bassereau, Patricia
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 15.10.2015; Nature Publishing Group; Nature Pub. Group
• Subjects: 14/19; 631/45/612/1237; 631/80/313/2375; 631/80/84/1757; Bacteriology; Cell Behavior; Cell Line, Tumor; Cell Membrane - physiology; Cellular Biology; Humanities and Social Sciences; Humans; Life Sciences; Membranes; Microbiology and Parasitology; multidisciplinary; Nanotechnology; Nerve Tissue Proteins - metabolism; Pseudopodia - physiology; Science; Science (multidisciplinary); Subcellular Processes; Tension; Membrane curvature; Filopodia; Membrane proteins

BAR domain proteins contribute to membrane deformation in diverse cellular processes. The inverted-BAR (I-BAR) protein IRSp53, for instance, is found on the inner leaflet of the tubular membrane of filopodia; however its role in the formation of these structures is incompletely understood. Here we d...