title: Spectrins: a structural platform for stabilization and activation of membrane channels, receptors and transporters.
abstract: This review focuses on structure and functions of spectrin as a major component of the membrane skeleton. Recent advances on spectrin function as an interface for signal transduction mediation and a number of data concerning interaction of spectrin with membrane channels, adhesion molecules, receptors and transporters draw a picture of multifaceted protein. Here, we attempted to show the current depiction of multitask role of spectrin in cell physiology. This article is part of a Special Issue entitled: Reciprocal influences between cell cytoskeleton and membrane channels, receptors and transporters. Guest Editor: Jean Claude Hervé.
authors.affiliation: University of Zielona Góra, Faculty of Biological Sciences, Poland.
authors.forename: Beata
authors.initials: B
authors.lastname: Machnicka
authors.affiliation: University of Wrocław, Biotechnology Faculty, Poland.
authors.forename: Aleksander
authors.initials: A
authors.lastname: Czogalla
authors.affiliation: University of Wrocław, Biotechnology Faculty, Poland.
authors.forename: Anita
authors.initials: A
authors.lastname: Hryniewicz-Jankowska
authors.affiliation: University of Zielona Góra, Faculty of Biological Sciences, Poland.
authors.forename: Dżamila M
authors.initials: DM
authors.lastname: Bogusławska
authors.affiliation: University of Zielona Góra, Faculty of Biological Sciences, Poland.
authors.forename: Renata
authors.initials: R
authors.lastname: Grochowalska
authors.affiliation: University of Zielona Góra, Faculty of Biological Sciences, Poland.
authors.forename: Elżbieta
authors.initials: E
authors.lastname: Heger
authors.affiliation: University of Wrocław, Biotechnology Faculty, Poland. Electronic address: afsikorski@gmail.com.
authors.forename: Aleksander F
authors.initials: AF
authors.lastname: Sikorski
mesh_terms: D000818:Animals; D006801:Humans; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*; D013049:Spectrin / Q000378:metabolism*
chemical_list: D007473:Ion Channels; D026901:Membrane Transport Proteins; D011956:Receptors, Cell Surface; D013049:Spectrin
keywords: (N-methyl-d-aspartate) receptor; (after Landsteiner and Wiener) blood group antigen glycoprotein; 3′-5′-cyclic adenosine monophosphate; ABD; AE1; Anion exchange protein 1 and Band 3 anion transport protein; Arp1; CD47; CH1; CHL1; DRM; EAAT4; EF-hand domain; ERM; EVL; Enabled/VASP (vasodilator-stimulated phosphoprotein)-like protein; FA; Fanconi anemia; GABA; GLUT1; GPB; GPC; LW; Lu/B-CAM; Lutheran blood group and basal cell adhesion molecule; MPP1; NMDA; Neural cell adhesion molecule L1-like protein; Neuron-Glia Cell Adhesion Molecule)-Related Cell Adhesion Molecule; Neuronal cell adhesion molecule; NgCAM; NrCAM; PH; PIP2; PKA; PKCβ(2); PSDs; Phosphatidylinositol 4,5-bisphosphate; Plasma membrane domain; Protein Kinase-A; Rh; Rh-associated glycoprotein; RhAG; Rhesus protein; SCA5; SH3; SRC homology 3 domain; Spectrin; Spectrin-based membrane skeleton; Spinocerebellar Ataxia Type 5; T cell receptor; TCR; TGFβ; Transforming growth factor beta; VASP; VGSC; Vasodilator-stimulated phosphoprotein; actin binding domain; actin-related protein 1; cAMP; calcium-binding domain; calponin homology domain; detergent-resistant membrane; excitatory amino acid transporters 4; ezrin–radixin–moesin family; glucose transporter protein 1; glycophorin B; glycophorin C; integrin-associated protein; membrane protein, palmitoylated 1; perforated postsynaptic densities; pleckstrin homology domain; protein kinase C β2; voltage-gated sodium channels; γ-Aminobutyric acid