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Calcineurin: a calcium- and calmodulin-binding protein of the nervous system.

Klee, C B, Crouch, T H, Krinks, M H·1979·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.76.12.6270
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Abstract

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.

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Crossref · 10.1073/pnas.76.12.6270

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Figures

FIG. 1 Effect of Ca2+ and EGTA on the electrophoretic mobilities of Ca2+-binding proteins. Protein samples (2 μg in 20 μl) in 50 mM Tris-HCl (pH 8.0) containing 1 mM Ca2+ or 1 mM EGTA were subjected to electrophoresis in the presence of sodium dodecyl sulfate in 7.5–15% gradients of acrylamide. Additions of Ca2+ or EGTA were as indicated. The M markers were bovine serum albumin, catalase, fumarase, lactate dehydrogenase, β-lactoglobulin, α-lactalbumin, and lysozyme. Columns: 1, calcineurin A (M 61,000) and calcineurin B (Mr 16,500 or 15,500 in the presence of EGTA or Ca2+, respectively); 2, calmodulin (Mr 19,000 in EGTA or 17,000 in Ca2+; 3, troponin C (Mr 19,500 in EGTA or 18,500 in Ca2+; 4, β-lactoglobulin (Mr 17,500); 5, lysozyme (M 14,200).
FIG. 1 Effect of Ca2+ and EGTA on the electrophoretic mobilities of Ca2+-binding proteins. Protein samples (2 μg in 20 μl) in 50 mM Tris-HCl (pH 8.0) containing 1 mM Ca2+ or 1 mM EGTA were subjected to electrophoresis in the presence of sodium dodecyl sulfate in 7.5–15% gradients of acrylamide. Additions of Ca2+ or EGTA were as indicated. The M markers were bovine serum albumin, catalase, fumarase, lactate dehydrogenase, β-lactoglobulin, α-lactalbumin, and lysozyme. Columns: 1, calcineurin A (M 61,000) and calcineurin B (Mr 16,500 or 15,500 in the presence of EGTA or Ca2+, respectively); 2, calmodulin (Mr 19,000 in EGTA or 17,000 in Ca2+; 3, troponin C (Mr 19,500 in EGTA or 18,500 in Ca2+; 4, β-lactoglobulin (Mr 17,500); 5, lysozyme (M 14,200).From the PDF
FIG. 2 Calcium binding to calcineurin. Gel filtration of calcineurin was performed in the presence of 5.4 μM 4⁵CaCl2 (specific activity, 10 Ci/mol). CaCl2 concentration was measured directly in tubes 1, 11, 24, and 33.
FIG. 2 Calcium binding to calcineurin. Gel filtration of calcineurin was performed in the presence of 5.4 μM 4⁵CaCl2 (specific activity, 10 Ci/mol). CaCl2 concentration was measured directly in tubes 1, 11, 24, and 33.From the PDF
FIG. 3 Subunit composition of calcineurin and calcineurincalmodulin complexes. Calcineurin (10 μg in a final volume of 20 μl) was incubated at 23°C for various times in the presence of dimethylsuberimidate (1 mg/ml, gels 1–6; 5 mg/ml, gels 7 and 8). When present, MgCl2 was 1 mM, CaCl2 was 0.5 mM, and EGTA was 1 mM. EDTA (gel 5) was 2 mM; calmodulin (gels 7 and 8) was 3 μg in 20 μl. Electrophoresis was for 10 hr to maximize the band resolution. Under these conditions, calmodulin and calcineurin B migrated out of the gels. The Mr markers were the products of crosslinking of lactate dehydrogenase and fumarase. The identity of the A-B-calmodulin complex (CaM-A-B) was confirmed by using [14C]guanidinated calmodulin; radioactivity was recovered in the M 76,000 and 92,000 bands (gel 7). In the presence of EGTA (gel 8), no radioactivity was found in the M 76,000 band.
FIG. 3 Subunit composition of calcineurin and calcineurincalmodulin complexes. Calcineurin (10 μg in a final volume of 20 μl) was incubated at 23°C for various times in the presence of dimethylsuberimidate (1 mg/ml, gels 1–6; 5 mg/ml, gels 7 and 8). When present, MgCl2 was 1 mM, CaCl2 was 0.5 mM, and EGTA was 1 mM. EDTA (gel 5) was 2 mM; calmodulin (gels 7 and 8) was 3 μg in 20 μl. Electrophoresis was for 10 hr to maximize the band resolution. Under these conditions, calmodulin and calcineurin B migrated out of the gels. The Mr markers were the products of crosslinking of lactate dehydrogenase and fumarase. The identity of the A-B-calmodulin complex (CaM-A-B) was confirmed by using [14C]guanidinated calmodulin; radioactivity was recovered in the M 76,000 and 92,000 bands (gel 7). In the presence of EGTA (gel 8), no radioactivity was found in the M 76,000 band.From the PDF
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Cites

Research works printed but not linked: 5

  1. [8]Cheung, W. Y. (1979) Science, in press.
  2. [12]: Davies, G. E. & Stark, G. R. (1970) Proc. Natl. Acad. Sci. USA 66, 651–656.
  3. [28]Schulman, H. & Greengard, P. (1978) Proc. Natl. Acad. Sci. USA 75, 5432–5436.
  4. [27]Greengard, P. (1978) Cyclic Nucleotides, Phosphorylated Proteins and Neuronal Function (Raven, New York), Vol. 1.
  5. [29]Wood, J. G., Wallace, R. W., Whitaker, J. N. & Cheung, W. Y. J. Cell. Biol., in press.

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Metadata

Authors
Klee, C. B., Crouch, T. H., & Krinks, M. H.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1979-12
Volume
76
Issue
12
Pages
6270-6273
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.76.12.6270
Cited by
579
References
1
Language
en

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