环腺苷酸特异性磷酸二酯酶，PDE8A1，可被蛋白激酶 A 介导的磷酸化作用激活。

Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation.

机构信息

Institute of Cardiovascular and Medical Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.

出版信息

FEBS Lett. 2012 Jun 4;586(11):1631-7. doi: 10.1016/j.febslet.2012.04.033. Epub 2012 May 3.

DOI:10.1016/j.febslet.2012.04.033

PMID:22673573

Abstract

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.

摘要

环腺苷酸（cAMP）特异性磷酸二酯酶 PDE8 已被证明在类固醇生成、T 细胞黏附、心率调节和趋化性等重要过程中发挥关键作用。然而，目前尚不清楚该酶的活性是如何调节的。我们发现，在 cAMP 水平升高的情况下，蛋白激酶 A（PKA）会使 PDE8A 上的丝氨酸 359 发生磷酸化，从而增强酶的活性。这是 PDE8 活性可以被激酶调节的首个证据，我们提出，这种机制形成了一个反馈回路，导致 cAMP 水平恢复到基础水平。