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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...
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...
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...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

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Related Experiment Video

Updated: Jul 8, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

PTEN phosphatase selectively binds phosphoinositides and undergoes structural changes.

Roberta E Redfern1, Duane Redfern, Melonnie L M Furgason

  • 1Chemistry Department, Kent State University, Kent, Ohio 44242, USA.

Biochemistry
|January 29, 2008
PubMed
Summary
This summary is machine-generated.

Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) activity is regulated by membrane binding. Specifically, PI(4,5)P2 binding to PTEN

More Related Videos

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

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

Related Experiment Videos

Last Updated: Jul 8, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

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
  • Molecular Biology
  • Cancer Research

Background:

  • PTEN is a critical tumor suppressor gene.
  • PTEN mutations are common in human cancers.
  • PTEN regulates cell growth and survival.
  • The precise mechanisms regulating PTEN activity are not fully understood.

Purpose of the Study:

  • To investigate the molecular mechanisms by which PI(4,5)P2 enhances PTEN phosphatase activity.
  • To determine the role of membrane binding in PTEN conformational changes.
  • To identify the specific lipid interactions that modulate PTEN function.

Main Methods:

  • Spectroscopic analysis (circular dichroism) to detect conformational changes.
  • Binding assays using PTEN protein and N-terminal peptides with various phospholipids.
  • Experiments with mutant PTEN proteins to map lipid-binding sites.

Main Results:

  • PI(4,5)P2 binding induces a conformational change in PTEN, increasing alpha-helicity.
  • This conformational change is specific to PI(4,5)P2 and not observed with other phosphoinositides like PI(3,5)P2 or PI(3,4,5)P3.
  • PI(4,5)P2 interacts with the N-terminal domain of PTEN.
  • PTEN also binds to phosphatidylserine, and these lipids bind synergistically.
  • Membrane binding involves multiple sites, but PI(4,5)P2 binding to the N-terminus is key for conformational change.

Conclusions:

  • PI(4,5)P2 binding to the PTEN N-terminus triggers a significant conformational change, enhancing its activity.
  • PTEN utilizes multiple membrane interaction sites, with PI(4,5)P2 playing a crucial role in regulating its conformation and function.
  • Understanding these lipid-protein interactions provides insights into PTEN's role in tumor suppression and potential therapeutic strategies.