Protein phosphatases come of age.
Protein phosphatases come of age.
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发表时间：
1989-12
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影响因子：
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通讯作者：
P. Cohen;P. Cohen
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文献类型：
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作者：
P. Cohen;P. Cohen
任何蛋白质的磷酸化水平都取决于蛋白激酶和蛋白磷酸酶的相对活性（I），但后者受到的关注要少得多，这可能是因为在研究它们之前很难获得明确的底物。尽管如此，在过去的几年里，关于蛋白质丝氨酸/苏氨酸磷酸酶的信息已经大量增加，读者可以参考详细的综述（2）了解背景信息和许多主要参考文献。这篇小综述将集中于最近的进展，这些进展已经证明了这些酶在肿瘤抑制和细胞分裂中的关键作用，并确定了新的磷酸酶催化亚基。我们目前的理解的结构，底物特异性，和调节蛋白磷酸酶也将讨论的重点是“靶向亚基的作用。”参考文献3中回顾了某些膜结合糖蛋白是蛋白质酪氨酸磷酸酶的发现。
The level of phosphorylation of any protein depends on the relative activities of protein kinases and protein phosphatases (I), but the latter enzymes have received far less attention, perhaps because of the difficulty in obtaining a well defined substrate before they can be studied. Nevertheless, information about, protein serine/threonine phosphatases has increased enormously over the past few years, and readers are referred to a detailed review (2) for background information and for many of the primary references. This Minireview will concentrate on recent progress that has demonstrated key roles for these enzymes in tumor suppression and in cell division and identified novel phosphatase catalytic subunits. Our current understanding of the structure, substrate specificity, and regulation of protein phosphatases will also be discussed with emphasis on the role of “targeting subunits.” The discovery that certain membrane-bound glycoproteins are protein tyrosine phosphatases is reviewed in Ref. 3.