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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...
Hybridization of Atomic Orbitals II03:35

Hybridization of Atomic Orbitals II

sp3d and sp3d 2 Hybridization
π Molecular Orbitals of the Allyl Cation and Anion01:18

π Molecular Orbitals of the Allyl Cation and Anion

An allyl group is a three-carbon conjugated system where the sp³-hybridized allylic carbon is bonded to a CH=CH2 group via a single bond. Allyl anions can be obtained by treating propene with a strong base that can deprotonate methyl groups. Allyl cations are formed as intermediates during substitution reactions involving allylic halides. In both cases, the hybridization of the allylic carbon changes from sp3 to sp2, giving rise to a carbon chain with three sp2-hybridized carbons, each with an...
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...
π Molecular Orbitals of 1,3-Butadiene01:24

π Molecular Orbitals of 1,3-Butadiene

Conjugated dienes have lower heats of hydrogenation than cumulated and isolated dienes, making them more stable. The enhanced stabilization of conjugated systems can be understood from their π molecular orbitals.
The simplest conjugated diene is 1,3-butadiene: a four-carbon system where each carbon is sp2-hybridized and has an unhybridized p orbital that contains an unpaired electron. According to molecular orbital theory, atomic orbitals combine to form molecular orbitals such that the number...

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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The PI(3,5)P2 and PI(4,5)P2 interactomes.

Bruno Catimel1, Christine Schieber, Melanie Condron

  • 1Ludwig Institute for Cancer Research, Melbourne Tumour Biology Branch, Royal Melbourne Hospital, Parkville Victoria 3052, Australia. Bruno.catimel@ludwig.edu.au

Journal of Proteome Research
|April 16, 2009
PubMed
Summary

Researchers identified 388 proteins interacting with specific phosphoinositides, including novel candidates. This study advances understanding of cellular signaling by mapping 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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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

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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

Area of Science:

  • Cell Biology
  • Biochemistry
  • Cancer Research

Background:

  • Phosphoinositides are key regulators of cellular processes.
  • Understanding their interactions is crucial for cell signaling research.
  • Specific phosphoinositides like PI(3,5)P2 and PI(4,5)P2 play vital roles.

Purpose of the Study:

  • To comprehensively analyze the phosphoinositide interactome.
  • To identify proteins that specifically bind to PI(3,5)P2 and PI(4,5)P2.
  • To discover novel phosphoinositide-interacting proteins in colon cancer.

Main Methods:

  • Utilized immobilized phosphoinositide analogues (PI(3,5)P2, PI(4,5)P2) on Affi-10 beads and liposomes as affinity absorbents.
  • Employed affinity-based capture followed by Liquid Chromatography/Tandem Mass Spectrometry (LC/MS/MS).
  • Analyzed cytosolic extracts from colonic carcinoma cell lines.

Main Results:

  • Identified 388 proteins and protein complexes with specific interactions to the targeted phosphoinositides.
  • Discovered a significant number of previously unknown proteins potentially interacting with phosphoinositides.
  • Provided a detailed map of the phosphoinositide interactome in the studied cell lines.

Conclusions:

  • The study successfully mapped a substantial portion of the phosphoinositide interactome.
  • Novel protein targets interacting with PI(3,5)P2 and PI(4,5)P2 were identified, opening new avenues for research.
  • Findings contribute to understanding aberrant signaling in colonic carcinoma.