The human phosphatase interactome: An intricate family portrait.

The human phosphatase interactome: An intricate family portrait.
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DOI:
10.1016/j.febslet.2012.05.008
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发表时间:
2012-08-14
期刊:
影响因子:
3.5
通讯作者:
Cesareni G
Cesareni G
中科院分区:
生物学3区
文献类型:
--
作者:
Sacco F;Perfetto L;Castagnoli L;Cesareni G

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真核细胞中激酶和磷酸酶的协同活动调节着蛋白质、脂质和碳水化合物的磷酸化水平。尽管付出了相当大的努力,我们仍然缺乏一个整体的画面,在蛋白质组水平上,代表激酶,磷酸酶和它们的底物之间的功能关系。在这里,我们专注于磷酸酶,我们回顾和整合现有的信息,有助于将蛋白质磷酸酶超家族的成员纳入人类蛋白质相互作用网络。此外,我们还展示了蛋白质相互作用结构域和基序,无论是与磷酸酶结构域共价连接还是在调控/接头亚基中,在底物选择中如何发挥突出作用。
The concerted activities of kinases and phosphatases modulate the phosphorylation levels of proteins, lipids and carbohydrates in eukaryotic cells. Despite considerable effort, we are still missing a holistic picture representing, at a proteome level, the functional relationships between kinases, phosphatases and their substrates. Here we focus on phosphatases and we review and integrate the available information that helps to place the members of the protein phosphatase superfamilies into the human protein interaction network. In addition we show how protein interaction domains and motifs, either covalently linked to the phosphatase domain or in regulatory/adaptor subunits, play a prominent role in substrate selection.
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