Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, Équipe Labellisée "Ligue Nationale Contre le Cancer", CNRS UMR 5237, 1919 Route de Mende, CEDEX 5, 34293 Montpellier, France.
Biomolecules. 2020 Nov 22;10(11):1586. doi: 10.3390/biom10111586.
Protein phosphorylation is a post-translational modification essential for the control of the activity of most enzymes in the cell. This protein modification results from a fine-tuned balance between kinases and phosphatases. PP2A is one of the major serine/threonine phosphatases that is involved in the control of a myriad of different signaling cascades. This enzyme, often misregulated in cancer, is considered a tumor suppressor. In this review, we will focus on PP2A-B55, a particular holoenzyme of the family of the PP2A phosphatases whose specific role in cancer development and progression has only recently been highlighted. The discovery of the Greatwall (Gwl)/Arpp19-ENSA cascade, a new pathway specifically controlling PP2A-B55 activity, has been shown to be frequently altered in cancer. Herein, we will review the current knowledge about the mechanisms controlling the formation and the regulation of the activity of this phosphatase and its misregulation in cancer.
蛋白质磷酸化是一种翻译后修饰，对于控制细胞中大多数酶的活性至关重要。这种蛋白质修饰源于激酶和磷酸酶之间的精细平衡。PP2A 是一种主要的丝氨酸/苏氨酸磷酸酶，参与控制无数不同的信号级联。这种酶在癌症中经常失调，被认为是一种肿瘤抑制因子。在这篇综述中，我们将重点介绍 PP2A-B55，这是 PP2A 磷酸酶家族中的一种特殊全酶，其在癌症发展和进展中的特定作用最近才被强调。最近发现，一个专门控制 PP2A-B55 活性的新通路——Gwl/Arpp19-ENSA 级联，在癌症中经常发生改变。在此，我们将回顾目前关于控制该磷酸酶形成和活性调节的机制及其在癌症中的失调的知识。
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