The spectrin-actin junction of erythrocyte membrane skeletons.
Published
Journal Article (Review)
High-resolution electron microscopy of erythrocyte membrane skeletons has provided striking images of a regular lattice-like organization with five or six spectrin molecules attached to short actin filaments to form a sheet of five- and six-sided polygons. Visualization of the membrane skeletons has focused attention on the (spectrin)5,6-actin oligomers, which form the vertices of the polygons, as basic structural units of the lattice. Membrane skeletons and isolated junctional complexes contain four proteins that are stable components of this structure in the following ratios: 1 mol of spectrin dimer, 2-3 mol of actin, 1 mol of protein 4.1 and 0.1-0.5 mol of protein 4.9 (numbers refer to mobility on SDS gels). Additional proteins have been identified that are candidates to interact with the junction, based on in vitro assays, although they have not yet been localized to this structure and include: tropomyosin, tropomyosin-binding protein and adducin. The spectrin-actin complex with its associated proteins has a key structural role in mediating cross-linking of spectrin into the network of the membrane skeleton, and is a potential site for regulation of membrane properties. The purpose of this article is to review properties of known and potential constituent proteins of the spectrin-actin junction, regulation of their interactions, the role of junction proteins in erythrocyte membrane dysfunction, and to consider aspects of assembly of the junctions.
Full Text
Duke Authors
Cited Authors
- Bennett, V
Published Date
- January 18, 1989
Published In
Volume / Issue
- 988 / 1
Start / End Page
- 107 - 121
PubMed ID
- 2642392
Pubmed Central ID
- 2642392
International Standard Serial Number (ISSN)
- 0006-3002
Digital Object Identifier (DOI)
- 10.1016/0304-4157(89)90006-3
Language
- eng
Conference Location
- Netherlands