Author: Klee, C. B.; Crouch, T. H.; Krinks, M. H.
Description: The inhibitory protein that binds calmodulin and thus prevents activation of several Ca2+-dependent enzymes by calmodulin is shown to also bind four Ca2+ per mol of protein with high affinity (Kd less than or equal to 10(-6) M). On the basis of its Ca2+- binding properties and its localization to nervous tissue, the inhibitory protein is now called calcineurin. Calcineurin is composed of two subunits: calcineurin A (61,000 Mr) which interacts with calmodulin in a Ca2+-dependent fashion, and calcineurin B (15,000 Mr) which binds Ca2+. The interaction of calcineurin A with calcineurin B is independent of Ca2+ or Mg2+. The dual interaction of calcineurin A with two different Ca2+-binding components and the high affinity of calcineurin for Ca2+ suggest a possible role for calcineurin in the regulation of free Ca2+ concentrations in the nervous system. Calcineurin may thereby modulate the release and action of neurotransmitters.
Subject headings: Animals; Brain; Calcium; Calcium-Binding Proteins; Calmodulin; Cattle; Molecular Weight; Nerve Tissue Proteins; Protein Binding; Calcineurin; Neurotransmitter
Publication year: 1979
Journal or book title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 76
Issue: 12
Pages: 6270-6273
Find the full text: https://www.pnas.org/content/pnas/76/12/6270.full.pdf
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Serial number: 3392