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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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...
RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
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...
Negative Regulator Molecules01:23

Negative Regulator Molecules

Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.

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Related Experiment Video

Updated: Jul 1, 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

Understanding PTEN regulation: PIP2, polarity and protein stability.

N R Leslie1, I H Batty, H Maccario

  • 1Division of Molecular Physiology, College of Life Sciences, University of Dundee, James Black Centre, Dundee, Scotland, UK. n.r.leslie@dundee.ac.uk

Oncogene
|September 17, 2008
PubMed
Summary

The PTEN tumor suppressor enzyme acts at cell membranes, regulating cell polarity and growth. Its activity is controlled by its location, post-translational modifications, and interactions, impacting tumor suppression.

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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

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Last Updated: Jul 1, 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

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Oncology

Background:

  • PTEN (Phosphatase and tensin homolog) is a crucial tumor suppressor.
  • It dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdInsP(3)), inhibiting PI3K signaling.
  • Dysregulation of PTEN is linked to various cancers.

Purpose of the Study:

  • To explore PTEN's function as an 'interfacial enzyme'.
  • To understand how PTEN activity is regulated spatially and temporally.
  • To elucidate PTEN's role in cell polarity and tumor suppression.

Main Methods:

  • Conceptual discussion of PTEN's enzymatic mechanism.
  • Analysis of PTEN's membrane binding and substrate interactions.
  • Review of post-translational modifications affecting PTEN activity, stability, and localization.

Main Results:

  • PTEN functions as an interfacial enzyme, highly active at membrane surfaces with specific lipids.
  • This interfacial activity enables spatial control of PtdInsP(3) gradients, crucial for cell polarity.
  • PTEN activity is further regulated by oxidation, phosphorylation, and ubiquitination, impacting its tumor suppressor function.

Conclusions:

  • PTEN's interfacial mechanism is key to its role in cell polarity and development.
  • Post-translational modifications fine-tune PTEN activity, localization, and stability.
  • Understanding PTEN regulation is vital for cancer research and therapeutic strategies.