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PMID: 2492524 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Calcium/calmodulin inhibits direct binding of spectrin to synaptosomal membranes.

The Journal of biological chemistry ·Vol. 264 ·No. 5 ·1989-02-15 ·Pages 2783-91

Steiner JP, Walke HT, Bennett V

Abstract

Brain spectrin, through its beta subunit, binds with high affinity to protein-binding sites on brain membranes quantitatively depleted of ankyrin (Steiner, J., and Bennett, V. (1988) J. Biol. Chem. 263, 14417-14425). In this study, calmodulin is demonstrated to inhibit binding of brain spectrin to synaptosomal membranes. Submicromolar concentrations of calcium are required for inhibition of binding, with half-maximal effects at pCa = 6.5. Calmodulin competitively inhibits binding of spectrin to protein(s) in stripped synaptosomal membranes, with Ki = 1.3 microM in the presence of 10 microM calcium. A reversible receptor-mediated process, and not proteolysis, is responsible for inhibition since the effect of calcium/calmodulin is reversed by the calmodulin antagonist trifluoperazine and by chelation of calcium with sodium [ethylenebis(oxyethylenenitrilo)]tetraacetic acid. The target of calmodulin is most likely the spectrin attachment protein(s) rather than spectrin itself since: (a) membrane binding of the brain spectrin beta subunit, which does not associate with calmodulin, is inhibited by calcium/calmodulin, and (b) red cell spectrin which binds calmodulin very weakly, is inhibited from interacting with membrane receptors in the presence of calcium/calmodulin. Ca2+/calmodulin inhibited association of erythrocyte spectrin with synaptosomal membranes but had no effect on binding of erythrocyte or brain spectrin to ankyrin in erythrocyte membranes. These experiments demonstrate the potential for differential regulation of spectrin-membrane protein interactions, with the consequence that Ca2+/calmodulin can dissociate direct spectrin-membrane interactions locally or regionally without disassembly of the areas of the membrane skeleton stabilized by linkage of spectrin to ankyrin. A membrane protein of Mr = 88,000 has been identified that is dissociated from spectrin affinity columns by calcium/calmodulin and is a candidate for the calmodulin-sensitive spectrin-binding site in brain.

MeSH Terms
Animals Brain/metabolism Calcium/pharmacology Calmodulin/pharmacology Carrier Proteins/isolation & purification,metabolism Cattle Chromatography, Affinity Egtazic Acid/pharmacology Intracellular Membranes/metabolism Kinetics Macromolecular Substances Spectrin/metabolism Synaptosomes/metabolism
Chemicals
Calmodulin Carrier Proteins Macromolecular Substances spectrin-binding proteins Spectrin Egtazic Acid Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Steiner J P
Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710.
Walke H T
Bennett V
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1989-02-15
Pages
2783-91
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIADDK NIH HHS · AM 19808 · United States
NIGMS NIH HHS · GM33996 · United States
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