Lateral segregation within plasma membranes
“Plasma membranes require high levels of plasticity to modulate perception and transduction of extra- and intracellular signals. Lateral assembly of protein complexes combined with an independent compositional lipid patterning of the bilayer in both membrane leaflets, provide the opportunity to decorate this interface with specific proteins in an organized and dynamic manner. This ability to reorganize the protein composition of the plasma membrane is essential for the regulation of processes such as polarity of transport, development and microbial infection. Accumulating evidence indicating dynamic compartmentalization of plasma membrane proteins in response to environmental cues has evoked increasing interest in its compositional heterogeneity. Functional membrane domains (‘membrane rafts’) host a number of signalling proteins but also serve as key cellular entry points for pathogenic microbes and viruses. It will be a challenge to understand and modulate these sites to engeneer pathogen resistance or abiotic stress tolerance in the future.” (modified from: Urbanus and Ott (2012), Frontiers in Plant Science, 3: 181).
The discovery of intrinsic disorder (ID) in proteins about 10 years ago led to a paradigm shift in protein science as these regions in proteins have no ordered secondary structure under physiological conditions. However, upon interaction with other proteins, post-translational modifications and/or protein-ligand interactions, ID regions can undergo conformational changes to bind the targets with high specificity but low affinity. We investigate these structural dynamics and the functional relevance of ID segments in remorin proteins.