title: Dynamic, yet structured: The cell membrane three decades after the Singer-Nicolson model.
abstract: The fluid mosaic membrane model proved to be a very useful hypothesis in explaining many, but certainly not all, phenomena taking place in biological membranes. New experimental data show that the compartmentalization of membrane components can be as important for effective signal transduction as is the fluidity of the membrane. In this work, we pay tribute to the Singer-Nicolson model, which is near its 30th anniversary, honoring its basic features, "mosaicism" and "diffusion," which predict the interspersion of proteins and lipids and their ability to undergo dynamic rearrangement via Brownian motion. At the same time, modifications based on quantitative data are proposed, highlighting the often genetically predestined, yet flexible, multilevel structure implementing a vast complexity of cellular functions. This new "dynamically structured mosaic model" bears the following characteristics: emphasis is shifted from fluidity to mosaicism, which, in our interpretation, means nonrandom codistribution patterns of specific kinds of membrane proteins forming small-scale clusters at the molecular level and large-scale clusters (groups of clusters, islands) at the submicrometer level. The cohesive forces, which maintain these assemblies as principal elements of the membranes, originate from within a microdomain structure, where lipid-lipid, protein-protein, and protein-lipid interactions, as well as sub- and supramembrane (cytoskeletal, extracellular matrix, other cell) effectors, many of them genetically predestined, play equally important roles. The concept of fluidity in the original model now is interpreted as permissiveness of the architecture to continuous, dynamic restructuring of the molecular- and higher-level clusters according to the needs of the cell and as evoked by the environment.
authors.affiliation: Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, H-4012, Debrecen, Hungary.
authors.forename: G
authors.initials: G
authors.lastname: Vereb
authors.forename: J
authors.initials: J
authors.lastname: Szöllosi
authors.forename: J
authors.initials: J
authors.lastname: Matkó
authors.forename: P
authors.initials: P
authors.lastname: Nagy
authors.forename: T
authors.initials: T
authors.lastname: Farkas
authors.forename: L
authors.initials: L
authors.lastname: Vigh
authors.forename: L
authors.initials: L
authors.lastname: Mátyus
authors.forename: T A
authors.initials: TA
authors.lastname: Waldmann
authors.forename: S
authors.initials: S
authors.lastname: Damjanovich
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000502:physiology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004058:Diffusion; D031541:Fluorescence Resonance Energy Transfer; D008051:Lipid Bilayers; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000502:physiology; D021962:Membrane Microdomains / Q000502:physiology; D008565:Membrane Proteins / Q000502:physiology; D008854:Microscopy, Electron; D008954:Models, Biological; D015398:Signal Transduction
chemical_list: D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins