4.5 Article

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

期刊

BIOCHEMICAL JOURNAL
卷 381, 期 -, 页码 587-592

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BJ20040846

关键词

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

资金

  1. NHLBI NIH HHS [F32HL68480, F32 HL068480] Funding Source: Medline
  2. NIDDK NIH HHS [P01 DK054441, DK54441] Funding Source: Medline

向作者/读者索取更多资源

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.

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