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Published on: July 17, 2020
Kinases, tails and more: regulation of PTEN function by phosphorylation
1Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal.
Abstract:
Phosphorylation regulates the conformation, stability, homo- and heterotypic protein interactions, localization, and activity of the tumor suppressor PTEN. From a simple picture, at the beginning of this millennium, recognizing that CK2 phosphorylated PTEN at the C-terminus and thereby impacted on PTEN stability and activity, research has led to a significantly more complex scenario today, where for instance GSK3, Plk3, ATM, ROCK or Src-family kinases are also gaining the spotlight in this evolving play. Here, we review the current knowledge on the kinases that phosphorylate PTEN, and on the impact that specific phosphorylation events have on PTEN function.
Insights
Phosphorylation by various kinases impacts tumor suppressor PTEN
Area of Science:
- Biochemistry
- Molecular Biology
- Cancer Research
Background:
- Phosphorylation is a key regulatory mechanism for proteins.
- The tumor suppressor PTEN's function is known to be modulated by phosphorylation.
- Early research identified CK2 as a kinase phosphorylating PTEN.
Purpose of the Study:
- To review current knowledge on kinases phosphorylating PTEN.
- To elucidate the impact of specific PTEN phosphorylation events on its function.
Main Methods:
- Literature review of scientific studies on PTEN phosphorylation.
- Analysis of kinase-PTEN interactions and functional consequences.
Main Results:
- PTEN phosphorylation is regulated by a growing number of kinases beyond CK2.
- Kinases like GSK3, Plk3, ATM, ROCK, and Src-family kinases are involved.
- Specific phosphorylation sites influence PTEN's conformation, stability, interactions, localization, and activity.
Conclusions:
- PTEN phosphorylation is a complex regulatory network.
- Understanding these phosphorylation events is crucial for comprehending PTEN's role in tumor suppression.
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