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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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 Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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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Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

PI(3,4,5)P3 Interactome.

Bruno Catimel1, Meng-Xin Yin, Christine Schieber

  • 1Ludwig Institute for Cancer Research, Melbourne Tumour Biology Branch, Royal Melbourne Hospital, and School of Chemistry, Bio21 Institute, University of Melbourne, Parkville, Victoria 3010, Australia. Bruno.catimel@ludwig.edu.au

Journal of Proteome Research
|May 26, 2009
PubMed
Summary

Researchers identified 282 proteins interacting with phosphatidylinositol (3,4,5)-trisphosphate (PI(3,4,5)P3) using novel affinity absorbents. This advance aids in understanding the phosphoinositide interactome in colon cancer cells.

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Mapping Dysfunctional Protein-Protein Interactions in Disease

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

  • Biochemistry
  • Cell Biology
  • Proteomics

Background:

  • Phosphoinositides, such as phosphatidylinositol (3,4,5)-trisphosphate (PI(3,4,5)P3), play critical roles in cellular signaling pathways.
  • Understanding the proteins that interact with PI(3,4,5)P3 is crucial for elucidating cellular functions and disease mechanisms, particularly in cancer.

Purpose of the Study:

  • To develop and utilize novel affinity absorbents for the comprehensive analysis of the PI(3,4,5)P3 interactome.
  • To identify proteins that directly or indirectly bind to PI(3,4,5)P3 in colon cancer cell extracts.

Main Methods:

  • Chemically synthesized analogues of PI(3,4,5)P3 were immobilized onto Affi-10 beads and incorporated into liposomes.
  • These affinity absorbents were used with cytosolic cell extracts from the LIM1215 colon cancer cell line.
  • Protein identification was performed using affinity-based capture followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS).

Main Results:

  • The study successfully identified 282 proteins associated with PI(3,4,5)P3.
  • These proteins include direct PI(3,4,5)P3 binding partners and proteins captured indirectly within larger complexes.
  • The methodology provided a comprehensive view of the phosphoinositide interactome in the context of colon cancer.

Conclusions:

  • The developed affinity-based approach is effective for analyzing the phosphoinositide interactome.
  • The identified protein set offers new insights into PI(3,4,5)P3-mediated cellular processes in colon cancer.
  • This work lays the foundation for further investigation into the roles of these protein interactions in cancer biology.