Lateral Organization of Host Heterogeneous Raft‐like Membranes Altered by the Myristoyl Modification of Tyrosine Kinase c‐Src

• DOI: 10.1002/ange.201706233
• Publication Date: 2017-06-30T06:55:16Z
• Authors: Mridula Dwivedi; Tom Mejuch; Herbert Waldmann; Roland Winter
• Keywords: Fluorescence Correlation Spectroscopy; Raft; Lipid raft; Membrane Curvature; Lipid microdomain

Abstract Membrane‐bound c‐Src non‐receptor tyrosine kinase, unlike other acyl‐modified lipid‐anchored proteins, anchors to the membrane by a myristoyl chain along with polybasic residue stretch, which is shorter in length than its host membrane. The packing defect arising from this mismatched of and lipid anchor significantly affects lateral organization heterogeneous membranes. We reveal mixing phase domains formation novel nanoscale‐clusters upon binding Myr‐Src (2–9) peptide. Fluorescence cross correlation spectroscopy was used explore nature these clusters. show that able oligomerize, peptide clusters are embedded platform generated sorting. Further, using confocal fluorescence microscopy FRET assays we localized charge enrichment curvature shift partition coefficient towards more ordered phase.