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Diversity in protein associations of the spectrin-based membrane skeleton of nonerythroid cells

Publication ,  Journal Article
Bennett, V; Steiner, J; Davis, J
Published in: Protoplasma
June 1, 1988

The purpose of this review is to summarize recent progress in understanding interactions of spectrin with membranes from brain and other tissues. Spectrin has at least two choices in linkages with the membrane, one through ankyrin, which in turn is associated with integral membrane proteins, and another linkage directly with integral membrane sites identified recently in brain membranes. Some of the integral membrane protein sites in brain bind preferentially with one spectrin isoform, while some can interact with both erythroid and the general isoform of spectrin. Ankyrin also has different isoforms, and these exhibit specificity in binding to spectrin isoforms and associate with distinct integral membrane proteins. The membrane binding sites for ankyrin include several integral membrane proteins, which are differentially expressed in different cells: the anion exchanger of intercalated cells of mammalian kidney, the sodium/potassium ATPase of kidney, and the voltage-dependent sodium channel of neurons. Ankyrin is present in many other cell types and it is likely that additional ankyrin-binding proteins will be identified. Each of the proteins that now are candidates for ankyrin binding proteins are ion channels or transporters and are localized in specialized cellular domains. The polarized localization of the ankyrin-associated membrane proteins is an essential aspect of their function at a physiological level. Spectrin and ankyrin thus exhibit an unsuspected diversity in protein linkages and have the potential for cell domain-specific interactions with a variety of membrane proteins. © 1988 Springer-Verlag.

Duke Scholars

Published In

Protoplasma

DOI

EISSN

1615-6102

ISSN

0033-183X

Publication Date

June 1, 1988

Volume

145

Issue

2-3

Start / End Page

89 / 94

Related Subject Headings

  • Plant Biology & Botany
  • 3108 Plant biology
  • 0607 Plant Biology
  • 0601 Biochemistry and Cell Biology
 

Citation

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Bennett, V., Steiner, J., & Davis, J. (1988). Diversity in protein associations of the spectrin-based membrane skeleton of nonerythroid cells. Protoplasma, 145(2–3), 89–94. https://doi.org/10.1007/BF01349343
Bennett, V., J. Steiner, and J. Davis. “Diversity in protein associations of the spectrin-based membrane skeleton of nonerythroid cells.” Protoplasma 145, no. 2–3 (June 1, 1988): 89–94. https://doi.org/10.1007/BF01349343.
Bennett V, Steiner J, Davis J. Diversity in protein associations of the spectrin-based membrane skeleton of nonerythroid cells. Protoplasma. 1988 Jun 1;145(2–3):89–94.
Bennett, V., et al. “Diversity in protein associations of the spectrin-based membrane skeleton of nonerythroid cells.” Protoplasma, vol. 145, no. 2–3, June 1988, pp. 89–94. Scopus, doi:10.1007/BF01349343.
Bennett V, Steiner J, Davis J. Diversity in protein associations of the spectrin-based membrane skeleton of nonerythroid cells. Protoplasma. 1988 Jun 1;145(2–3):89–94.
Journal cover image

Published In

Protoplasma

DOI

EISSN

1615-6102

ISSN

0033-183X

Publication Date

June 1, 1988

Volume

145

Issue

2-3

Start / End Page

89 / 94

Related Subject Headings

  • Plant Biology & Botany
  • 3108 Plant biology
  • 0607 Plant Biology
  • 0601 Biochemistry and Cell Biology