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Related Concept Videos

Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...

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Related Experiment Video

Updated: Jul 15, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

PTEN is destabilized by phosphorylation on Thr366.

Helene Maccario1, Nevin M Perera, Lindsay Davidson

  • 1Division of Molecular Physiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.

The Biochemical Journal
|April 21, 2007
PubMed
Summary

Phosphorylation of PTEN (phosphatase and tensin homologue deleted on chromosome 10) at Thr366 by GSK3 (glycogen synthase kinase 3) destabilizes the PTEN protein. Inhibiting this phosphorylation stabilizes PTEN, offering potential therapeutic strategies for cancers with PTEN loss.

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Related Experiment Videos

Last Updated: Jul 15, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a critical tumor suppressor frequently lost in human cancers.
  • Loss of PTEN expression, beyond mutation, is observed in a significant proportion of tumors.
  • PTEN protein levels are regulated post-translationally, impacting its tumor-suppressive function.

Purpose of the Study:

  • To investigate the role of PTEN phosphorylation in regulating its protein stability.
  • To identify kinases involved in PTEN phosphorylation and their impact on PTEN levels.
  • To explore the functional consequences of modulating PTEN phosphorylation in cancer cell lines.

Main Methods:

  • In vitro kinase assays using purified PTEN and identified kinases (GSK3, CK2).
  • Site-directed mutagenesis of PTEN phosphorylation sites (Thr366, Ser370).
  • Treatment of glioblastoma cell lines with specific kinase inhibitors (GSK3 inhibitor).
  • Western blot analysis to assess PTEN protein levels and phosphorylation status.

Main Results:

  • PTEN is phosphorylated by GSK3 (glycogen synthase kinase 3) at Thr366 and CK2 (casein kinase 2) at Ser370 in vitro.
  • Mutation of phosphorylation sites did not affect PTEN phosphatase activity in vitro or in cells.
  • Inhibition of GSK3 or mutation of Thr366 led to PTEN protein stabilization in glioblastoma cells.
  • Phosphorylation of Thr366 by GSK3 was identified as a key event in PTEN protein destabilization.

Conclusions:

  • PTEN phosphorylation at Thr366 by GSK3 plays a critical role in its protein destabilization.
  • Targeting GSK3 or preventing Thr366 phosphorylation represents a potential therapeutic strategy to restore PTEN levels in cancers.
  • Understanding PTEN post-translational regulation is crucial for developing effective cancer therapies.