The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains
The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains
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DOI：
10.1016/s0014-5793(99)01335-6
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发表时间：
1999-10-22
期刊：
影响因子：
3.5
通讯作者：
Houslay, MD
中科院分区：
文献类型：
--
作者：
Beard, MB;O'Connell, JC;Houslay, MD
在五种PDE 4D同工酶中，只有PDE 4D 4 cAMP特异性磷酸二酯酶能够与SH 3结构域结合。只有PDE 4D 4和PDE 4A 5与src、林恩和fyn激酶SH 3结构域结合，而其它PDE 4A、B、C和D亚型在大鼠脑中表达，纯化的PDE 4D 4可与纯化的林恩SH 3结合。PDE 4D 4和PDE 4A 5均表现出对结合某些蛋白质的SH 3结构域的选择性。PDE 4D 4不与WW结构域结合。我们认为PDE 4D 4独特的N-末端区域的一个重要功能可能是允许与某些含SH 3结构域的蛋白质结合，（C）1999欧洲生物化学学会联合会。
Of the five PDE4D isoenzymes, only the PDE4D4 cAMP specific phosphodiesterase mas able to bind to SH3 domains. Only PDE4D4 and PDE4A5, but not any other PDE4A, B, C and D isoforms expressed in rat brain, bound to src, lyn and fyn kinase SH3 domains, Purified PDE4D4 could bind to purified lyn SH3. PDE4D4 and PDE4A5 both exhibited selectivity for binding the SH3 domains of certain proteins. PDE4D4 did not bind to WW domains. We suggest that an important function of the unique N-terminal region of PDE4D4 may be to allow for association with certain SH3 domain-containing proteins, (C) 1999 Federation of European Biochemical Societies.