Membrane cytoskeleton

The membrane cytoskeleton (inclusive of the submembranous actin-spec-trin network) may function in the establishment and maintenance of restricted domains of specific proteins on the plasma membrane of polarized epithelial cells (Rodriguez-Boulan and Nelson, 1989 Mays et al., 1994). 

Machesky, L.M. Pollard, T.D. (1993). Profilin as a potential mediator of membrane-cytoskeleton communication. Trends Cell Biol. 3, 381-385. 

Actin microfilaments and the membrane cytoskeleton play critical roles in neuronal growth and secretion 129... 

Cross-link MFs in membrane cytoskeleton Links MF/spectrin to membrane proteins... 

Throughout neurons and glia, enriched in growth cones and in membrane cytoskeleton Co-distributed with most MFs Enriched in membrane cytoskeleton Membrane cytoskeleton, distinct forms in axon, dendrite and nodes of Ranvier Growing neurites... 

Ilsley.J. L., Sudol, M., and Winder, S. J. (2002). The WW domain Linking cell signaling to the membrane cytoskeleton. Cell. Signal. 14, 183-189. 

Spectrin is a common component of the submembranous cytoskeleton. It was first identified as a major constituent of the erythrocyte membrane cytoskeleton, but has since been found in many other vertebrate tissues as well as in the nonvertebrates Drosophila, Acanthamoeba, Dictyostelium, and echinoderms (Bennett and Condeelis, 1988 Byers et al., 1992 Dubreuil et al., 1989 Pollard, 1984 Wessel and Chen., 1993). The ease with which spectrin could be isolated from erythrocyte ghosts made it an ideal candidate for the study of the biochemical processes involved in the assembly and organization of the cytoskeleton (Gratzer, 1985). 

Winder, S. J. (1997). The membrane-cytoskeleton interface The role of dystrophin and utrophin./. Muscle Res. Cell Motil. 18, 617-629. 

Myelin/oligodendrocyte specific protein (MOSP) MOSP is a novel surface protein which is exclusively expressed in CNS myehn. It also plays an important role in membrane/cytoskeleton interactions during the formation and maintenance of CNS myelin. 

Lipid domains and rafts in biological membranes are stabilized by several different interactions, including membrane-cytoskeleton, lipid-protein, and lipid-lipid interactions, and the organization can be both equilibrium and non-equilibrium in nature [27]. Lipid-domain formation caused by cooperative phenomena in the lipid bilayers is particularly important for the activation of SPLA2 [32-35]. The cooperative phenomena in lipid bilayers are caused by the fundamental interactions between the lipid molecules and are a consequence of the many-particle character of the supramolecular aggregate. The cooperativity leads to phase transitions and phase equilibria. The key cooperative event in many liposomal membranes is the so-called main phase transition, which takes the bilayer from a solid (gel) phase with conformationally ordered acyl chains to a fluid phase with conformationally disordered chains. The main transition in lipid bilayers is often accompanied by strong lateral density and compositional fluctuations. These fluctuations are manifested as dynamic lipid domains characterized by certain time and length scales that are determined by the thermodynamic conditions and the actual lipid species in question. 

Marfatia SM, Cabral JH, Lin L, Hough C, Bryant PJ et al. (1996) Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton. J Cell Biol 735 753-766. 

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