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Phosphoinositides and PIPs01:42

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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.
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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...
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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...
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Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a...
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Microsporidia are a group of obligate intracellular fungi that were initially classified as protists but were later reclassified based on phylogenetic, molecular, and structural evidence linking them to the Chytridiomycota. These unicellular, non-motile organisms are highly specialized parasites that infect a wide range of animal hosts, including humans. They have evolved extensive genomic and metabolic reductions, making them highly dependent on their hosts for survival.Morphology and Genomic...
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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Updated: Nov 12, 2025

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

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Inositol polyphosphate-protein interactions: Implications for microbial pathogenicity.

Sophie Lev1,2,3, Bethany Bowring1,2,3, Desmarini Desmarini1,2,3

  • 1Centre for Infectious Diseases and Microbiology, The Westmead Institute for Medical Research, Sydney, New South Wales, Australia.

Cellular Microbiology
|March 15, 2021
PubMed
Summary
This summary is machine-generated.

Inositol polyphosphates (IPs) and pyrophosphates (PP-IPs) are vital regulators in eukaryotic cells. Their interactions with proteins impact cellular functions and pathogenicity, even with conserved binding domains.

Keywords:
fungal pathogensinositol polyphosphate kinasesinositol polyphosphatesinositol pyrophosphatesmicrobial pathogenesisprotein modification

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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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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Inositol polyphosphates (IPs) and inositol pyrophosphates (PP-IPs) are crucial regulators of diverse cellular processes in eukaryotes.
  • These molecules are highly negatively charged and interact with specific protein targets to exert their biological effects.
  • Previous research, mainly in mammalian cells and yeasts, elucidated their roles in allosteric regulation and phosphate donation.

Purpose of the Study:

  • To review the complex mechanisms of IP-mediated regulation across eukaryotes, including microbial pathogens.
  • To highlight the impact of IP and PP-IP interactions on pathogenicity.
  • To examine the conservation of IP-protein interaction outcomes despite conserved IP-binding domains.

Main Methods:

  • Literature review focusing on genetic studies and biochemical analyses of inositol polyphosphate and pyrophosphate functions.
  • Analysis of conserved domains and functional outcomes in IP-protein interactions across eukaryotic proteomes.
  • Examination of studies in microbial pathogens investigating the role of IP/PP-IP biosynthesis and interactions.

Main Results:

  • IPs and PP-IPs modulate protein function via allosteric regulation and, in the case of PP-IPs, phosphate donation.
  • Disrupting PP-IP biosynthesis and PP-IP-protein interactions significantly affects microbial pathogenicity.
  • Examples of poor conservation in the outcome of IP-protein interactions were identified, despite conserved binding domains.

Conclusions:

  • IP-mediated regulation is complex and extends to microbial pathogens, influencing their virulence.
  • Understanding these interactions is crucial for deciphering cellular processes and developing novel therapeutic strategies.
  • The variability in IP-protein interaction outcomes warrants further investigation into the nuances of these molecular interactions.