PKA-phosphorylation of PDE4D3 facilitates recruitment of the mAKAP signalling complex

被引：61

作者：

Michel, JJC

Dodge, KL

Wong, W

Mayer, NC

Langeberg, LK

Scott, JD

机构：

[1] Oregon Hlth & Sci Univ, Howard Hughes Med Inst, Portland, OR 97239 USA

[2] Oregon Hlth & Sci Univ, Vollum Inst, Portland, OR 97239 USA

来源：

BIOCHEMICAL JOURNAL | 2004年 / 381卷

关键词：

A-kinase-anchoring protein (AKAP); cAMP-dependent protein kinase (PKA); increased affinity; phosphodiesterase; serine-13; signalling;

D O I：

10.1042/BJ20040846

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

mAKAP (muscle-selective A-kinase-anchoring protein) co-ordinates a cAMP-sensitive negative-feedback loop comprising PKA (cAMP-dependent protein kinase) and the cAMP-selective PDE4D3 (phosphodiesterase 4D3). In vitro and cellular experiments demonstrate that PKA-phosphorylation of PDE4D3 on Ser-13 increases the affinity of PDE4D3 for mAKAP. Our data suggest that activation of mAKAP-anchored PKA enhances the recruitment of PDE4D3, allowing for quicker signal termination.

引用

页码：587 / 592

页数：6

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