CYCLIC AMP-DEPENDENT PHOSPHORYLATION OF A BRAIN INOSITOL TRISPHOSPHATE RECEPTOR DECREASES ITS RELEASE OF CALCIUM
CYCLIC AMP-DEPENDENT PHOSPHORYLATION OF A BRAIN INOSITOL TRISPHOSPHATE RECEPTOR DECREASES ITS RELEASE OF CALCIUM
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DOI：
10.1073/pnas.85.22.8747
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发表时间：
1988-11-01
影响因子：
11.1
通讯作者：
SNYDER, SH
中科院分区：
文献类型：
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作者：
SUPATTAPONE, S;DANOFF, SK;SNYDER, SH
我们报告的化学计量磷酸化肌醇1，4，5-三磷酸受体结合蛋白从大鼠脑cAMP依赖性蛋白激酶，但不是由蛋白激酶C或Ca 2 +/钙调蛋白依赖性蛋白激酶。这种磷酸化事件不会显著改变[3 H]肌醇1，4，5-三磷酸结合特性。然而，肌醇1，4，5-三磷酸是只有10%的潜力，释放45钙+磷酸化，相比，天然的，小脑微粒体。 cAMP依赖性蛋白激酶对肌醇1，4，5-三磷酸结合蛋白的磷酸化可能为第二信使串扰提供生化底物。
We report the stoichiometric phosphorylation of an inositol 1,4,5-trisphosphate receptor-binding protein from rat brain by the cAMP-dependent protein kinase but not by protein kinase C or Ca2+/calmodulin-dependent protein kinase. This phosphorylation event does not markedly alter [3H]inositol 1,4,5-trisphosphate-binding characteristics. However, inositol 1,4,5-trisphosphate is only 10% as potent in releasing 45Ca2+ from phosphorylated, as compared with native, cerebellar microsomes. Phosphorylation of the inositol 1,4,5-trisphosphate-binding protein by the cAMP-dependent protein kinase may provide a biochemical substrate for second-messenger cross talk.