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The spectrin-actin junction of erythrocyte membrane skeletons.

Publication ,  Journal Article
Bennett, V
Published in: Biochim Biophys Acta
January 18, 1989

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.

Duke Scholars

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

January 18, 1989

Volume

988

Issue

1

Start / End Page

107 / 121

Location

Netherlands

Related Subject Headings

  • Spectrin
  • Membrane Proteins
  • Macromolecular Substances
  • Humans
  • Erythrocyte Membrane
  • Blood Proteins
  • Anemia, Hemolytic, Congenital
  • Actins
  • 51 Physical sciences
  • 31 Biological sciences
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Bennett, V. (1989). The spectrin-actin junction of erythrocyte membrane skeletons. Biochim Biophys Acta, 988(1), 107–121. https://doi.org/10.1016/0304-4157(89)90006-3
Bennett, V. “The spectrin-actin junction of erythrocyte membrane skeletons.Biochim Biophys Acta 988, no. 1 (January 18, 1989): 107–21. https://doi.org/10.1016/0304-4157(89)90006-3.
Bennett V. The spectrin-actin junction of erythrocyte membrane skeletons. Biochim Biophys Acta. 1989 Jan 18;988(1):107–21.
Bennett, V. “The spectrin-actin junction of erythrocyte membrane skeletons.Biochim Biophys Acta, vol. 988, no. 1, Jan. 1989, pp. 107–21. Pubmed, doi:10.1016/0304-4157(89)90006-3.
Bennett V. The spectrin-actin junction of erythrocyte membrane skeletons. Biochim Biophys Acta. 1989 Jan 18;988(1):107–121.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

January 18, 1989

Volume

988

Issue

1

Start / End Page

107 / 121

Location

Netherlands

Related Subject Headings

  • Spectrin
  • Membrane Proteins
  • Macromolecular Substances
  • Humans
  • Erythrocyte Membrane
  • Blood Proteins
  • Anemia, Hemolytic, Congenital
  • Actins
  • 51 Physical sciences
  • 31 Biological sciences