Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation
Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation
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DOI：
10.1016/j.febslet.2012.04.033
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发表时间：
2012-06-04
期刊：
影响因子：
3.5
通讯作者：
Baillie, George S.
中科院分区：
文献类型：
--
作者：
Brown, Kim M.;Lee, Louisa C. Y.;Baillie, George S.
环腺苷酸特异性磷酸二酯酶PDE8在类固醇生成、T细胞粘附、心跳调节和趋化性等重要过程中起着关键作用。然而，没有关于这种酶的活性是如何调节的信息。我们表明，在升高的cAMP条件下，PKA的作用磷酸化PDE8A丝氨酸359和这种行动有助于提高酶的活性。这是PDE8活性可以通过激酶调节的第一个迹象，我们认为这种机制形成了一个反馈回路，导致基础cAMP水平的恢复。(C)2012年欧洲生物化学学会联合会。由Elsevier B出版。版权所有© 2016
The cyclic AMP-specific phosphodiesterase PDE8 has been shown to play a pivotal role in important processes such as steroidogenesis, T cell adhesion, regulation of heart beat and chemotaxis. However, no information exists on how the activity of this enzyme is regulated. We show that under elevated cAMP conditions, PKA acts to phosphorylate PDE8A on serine 359 and this action serves to enhance the activity of the enzyme. This is the first indication that PDE8 activity can be modulated by a kinase, and we propose that this mechanism forms a feedback loop that results in the restoration of basal cAMP levels. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.