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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
1988-10-13
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pubmed:abstractText |
The Ca2+/calmodulin (CaM)-dependent protein phosphatase calcineurin is rapidly phosphorylated (0.8 mol of 32PO4 per mol of 60-kDa subunit of calcineurin) by brain Ca2+/CaM-dependent protein kinase II (CaM-kinase II). This reaction requires the autophosphorylated, Ca2+-independent form of CaM-kinase II since Ca2+/CaM binding to calcineurin inhibits phosphorylation. However, the phosphorylation reaction does require Ca2+, presumably acting through the 19-kDa subunit of calcineurin. Calcineurin is a good substrate for CaM-kinase II, with a Km of 19 microM and Vmax of 2.4 mumol/min per mg. Phosphorylation of calcineurin changed its phosphatase activity with either a 2-fold increase in Km (32P-labeled myosin light chain as substrate) or a 50% decrease in Vmax (p-nitrophenyl phosphate as substrate). The phosphorylated calcineurin exhibited very slow autodephosphorylation (0.09 nmol/min per mg) but was effectively dephosphorylated by brain protein phosphatase IIA. Dephosphorylation, like phosphorylation, was blocked by high concentrations of Ca2+/CaM and stimulated by Ca2+ alone. Thus calcineurin has a regulatory phosphorylation site that is phosphorylated by the Ca2+-independent form of CaM-kinase II and blocked by high concentrations of Ca2+/CaM.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-13538948,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-188646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-208844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-2411213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-2822712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-2833910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-293720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-2983609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-2987415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-2997154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3001727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3006921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3007513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3012560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3013868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3017338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3028265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3037704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3110142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3160694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3470758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3475713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-35231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3611055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3722161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3855553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-3931554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-4078628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-4349654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6086614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6190810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6259152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6273157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6290479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6306765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6316077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6316096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6324861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6328493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6547441,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6583689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6591208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-6803791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842800-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7001-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
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pubmed:year |
1988
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pubmed:articleTitle |
Regulatory interactions of calmodulin-binding proteins: phosphorylation of calcineurin by autophosphorylated Ca2+/calmodulin-dependent protein kinase II.
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pubmed:affiliation |
Howard Hughes Medical Institute, Vanderbilt University, Nashville, TN 37232.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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