The hexagonal arrangements are formed by tetramers of spectrin subunits associating with short actin filaments at either end of the tetramer.
22.
It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction.
23.
Protein 4.1 ( 80 kD ) interacts with spectrin and short actin filaments to form the erythrocyte membrane skeleton.
24.
It also interacts with multiple proteins including calmodulin, SEC14 domain and spectrin repeat-containing protein 1 ( SESTD1 ).
25.
This 4.1 band domain binds to the cytoplasmic region of transmembrane proteins including glycophorin C, actin and spectrin.
26.
"' Spectrin "'is a cytoskeletal protein that lines the intracellular side of the plasma membrane in eukaryotic cells.
27.
The encoded protein contains an N-terminal actin-binding domain, and 17 spectrin repeats that are involved in dimer formation.
28.
Spectrin forms pentagonal or hexagonal arrangements, forming a scaffolding and playing an important role in maintenance of plasma membrane integrity and cytoskeletal structure.
29.
Alpha II-spectrin gene expression has been shown to be upregulated in cardiac fibroblasts in response to Angiotensin II-induced cardiac remodeling.
30.
Localization of alpha-II spectrin in green under the plasma membrane of rat neurons in tissue culture as shown with confocal microscopy and immunofluorescence.
