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Related Concept Videos

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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At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
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Cell division is essential for organismal growth and development. In animal cells, the central spindle and its associated proteins form the midbody, a structure that has an essential role in cytokinesis. In plants, the central spindle, along with the microtubules, actin, and other cell components, matures into the phragmoplast, which is necessary for cytokinesis. Unlike the stationary midbody, the phragmoplast expands centrifugally, eventually leading to the formation of the new cell wall.
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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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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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Related Experiment Video

Updated: Jul 12, 2025

"Phagosome Closure Assay" to Visualize Phagosome Formation in Three Dimensions Using Total Internal Reflection Fluorescent Microscopy TIRFM
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PHF1 compartmentalizes PRC2 via phase separation.

Genzhe Lu1,2,3, Pilong Li1,2

  • 1Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing 100084, China.

The Biochemical Journal
|October 27, 2023
PubMed
Summary
This summary is machine-generated.

Polycomb-like (PCL) proteins like PHF1 form phase-separated condensates at target sites. These condensates recruit Polycomb repressive complex 2 (PRC2) to deposit H3K27me3 marks and repress transcription.

Keywords:
PHF1PRC2phase separation

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Chemical Dimerization-Induced Protein Condensates on Telomeres
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Related Experiment Videos

Last Updated: Jul 12, 2025

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Chemical Dimerization-Induced Protein Condensates on Telomeres
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Area of Science:

  • Epigenetics and Gene Regulation
  • Molecular Biology
  • Cell Biology

Background:

  • Polycomb repressive complex 2 (PRC2) deposits histone H3 lysine 27 trimethylation (H3K27me3), a key epigenetic mark for gene silencing.
  • The recruitment mechanisms of PRC2 to specific genomic loci remain incompletely understood.
  • Polycomb-like (PCL) proteins are known accessory factors that can influence PRC2 targeting.

Purpose of the Study:

  • To investigate the role of PHF1, a PCL protein, in the recruitment and function of PRC2.
  • To elucidate the molecular mechanisms by which PHF1 mediates PRC2 targeting and activity.
  • To determine if PHF1-mediated phase separation influences transcriptional repression.

Main Methods:

  • Cellular imaging and observation techniques.
  • Biochemical reconstitution assays.
  • Luciferase reporter assays for gene expression analysis.

Main Results:

  • PHF1 forms phase-separated condensates at H3K27me3-marked loci.
  • These condensates recruit PRC2, with specific PHF1 domains mediating target recognition, PRC2 binding, and phase separation.
  • PHF1 condensates compartmentalize PRC2, DNA, and nucleosomes, promoting transcriptional repression via phase separation.

Conclusions:

  • PHF1 drives the formation of biomolecular condensates at target loci.
  • These condensates serve as platforms to recruit and concentrate PRC2, facilitating H3K27me3 deposition and gene silencing.
  • PHF1-mediated phase separation is a novel mechanism for regulating polycomb repression and gene transcription.