This protein may also help maintain the membrane skeleton of erythrocytes.

The last two terms come from the entropic elasticity of the membrane skeleton.

Protein 4.1 is a major structural element of the erythrocyte membrane skeleton.

This appears to be to prevent membrane surface loss, rather than being to do with membrane skeleton assembly.

Hereditary elliptocytosis is another defect in membrane skeleton proteins.

A cell membrane is simplified as lipid bilayer plus membrane skeleton.

The latter is commonly referred to as the "cytoskeleton" or "membrane skeleton" [ 4].

Physical linkage of the plasma membrane to the underlying membrane skeleton (via binding with ankyrin and protein 4.2).

Protein 4.1 (80 kD) interacts with spectrin and short actin filaments to form the erythrocyte membrane skeleton.

Inherited as an autosomal dominant, elliptocytosis results from mutation in any one of several genes encoding proteins of the red cell membrane skeleton.

Ankyrin-based macromolecular complex - proteins linking the bilayer to the membrane skeleton through the interaction of their cytoplasmic domains with Ankyrin.

In in vitro assays plectin has been found to bind subplasma membrane skeleton proteins such as alpha-spectrin and fodrin.

The movement of phospholipids, even those located in the outer leaflet of the membrane, is regulated by the actin-based membrane skeleton meshwork.

Band 3 serves as the principal binding site for the membrane skeleton, a submembrane protein network composed of ankyrin, spectrin, actin, and band 4.1.

The actin-based membrane skeleton (MSK) meshwork is directly situated on the cytoplasmic surface of the plasma membrane.

A third type of microtubules, the aster microtubules, radiates from the centrosome into the cytoplasm or contacts components of the membrane skeleton.

Beneath the lipid membrane, the membrane skeleton, a network of proteins, links with the proteins in the lipid membrane.

In erythrocytes, AnkyrinR links the membrane skeleton to the Cl/HCO anion exchanger.

Ovalocyte band 3 binds more tightly than normal band 3 to ankyrin, which connects the membrane skeleton to the band 3 anion transporter.

In this model various TM proteins are anchored to and aligned along the membrane skeleton, and effectively act as rows of pickets against the free diffusion of phospholipids.

The subpellicular network consists of a two-dimensional network of intermediate filaments located on the cytoplasmic side of the inner membrane complex and acts as a membrane skeleton.

As such, the actin-based membrane skeleton might work as a base scaffold for enhancing the interactions between the receptor and the actin-bound downstream molecules and for localized signaling.

Cytoplasmic domains collide with the actin-based membrane skeleton which induces temporary confinement or corralling of transmembrane (TM) proteins in the membrane skeleton mesh.

The proteins - the inner membrane complex proteins (IMCs) - that compose this structure are functional homologs of the articulins, the membrane skeleton proteins of free-living protists.

When a TM protein is anchored to the membrane skeleton and immobilized, the viscosity of the fluid around it becomes higher, due to hydrodynamic friction effects at the surface of the immobilized protein.