4.7 Article

Assaying PTEN catalysis in vitro

期刊

METHODS
卷 77-78, 期 -, 页码 51-57

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2014.11.003

关键词

Phosphatase; Tumour suppressor; Phosphoinositide; Vesicle; Enzyme assay; Phosphate

资金

  1. Medical Research Council [G0801865]
  2. Astra Zeneca
  3. Boehringer Ingelheim
  4. GlaxoSmithKline
  5. Merck KGaA
  6. Pfizer
  7. MRC [G0801865, G9403619] Funding Source: UKRI
  8. Medical Research Council [G9403619, G0801865] Funding Source: researchfish

向作者/读者索取更多资源

PTEN is a major tumour suppressor protein and a regulator of numerous diverse biological processes. It has an evolutionarily conserved role as a phosphoinositide lipid phosphatase, regulating the PI3K signalling pathway, but also has catalytic phosphatase activity against protein substrates, although the significance of this latter activity is less well understood. Unlike many tumour suppressors, even modest changes in PTEN activity can have strong effects on phenotypes, including tumour formation. Due to this recognised functional significance, several experimental platforms have been developed to assay the catalytic activity of PTEN against different substrates and are being applied to understand this cellular substrate diversity and the regulation of PTEN. Here we present and discuss methods to assay the phosphatase activity of PTEN in vitro. (C) 2014 Elsevier Inc. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据