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Related Concept Videos

¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Spindle Assembly02:50

Spindle Assembly

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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Updated: Jun 7, 2025

Origami Inspired Self-assembly of Patterned and Reconfigurable Particles
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p14ARF forms meso-scale assemblies upon phase separation with NPM1.

Eric Gibbs1, Qi Miao1, Mylene Ferrolino1

  • 1Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.

Nature Communications
|November 11, 2024
PubMed
Summary
This summary is machine-generated.

Nuclear protein NPM1 stabilizes the tumor suppressor p14ARF by forming a gel-like network. This NPM1-p14ARF interaction regulates nucleolar stress responses and reduces cell proliferation, offering insights into cancer suppression mechanisms.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Nuclear protein NPM1 is a nucleolar chaperone involved in ribosome biogenesis, nucleolar stress responses, and tumor suppression.
  • NPM1 regulates the p14 Alternative Reading Frame (p14ARF) tumor suppressor protein, which inhibits MDM2, stabilizes p53, and arrests the cell cycle under oncogenic stress.
  • Under normal conditions, NPM1 stabilizes p14ARF in nucleoli, preventing p53 activation.

Purpose of the Study:

  • To elucidate the structural mechanisms by which NPM1 regulates p14ARF.
  • To understand how NPM1-mediated regulation of p14ARF impacts nucleolar function and cellular processes.

Main Methods:

  • Structural analysis of the p14ARF-NPM1 complex.
  • Investigating the role of intermolecular contacts and hydrophobic interactions in complex formation.
  • Assessing the impact of NPM1-p14ARF assembly on nucleolar partitioning and cellular proliferation.

Main Results:

  • p14ARF forms a gel-like, meso-scale network through phase separation with NPM1.
  • Intermolecular hydrophobic contacts within a partially folded N-terminal region of p14ARF mediate this assembly.
  • This phase separation enhances p14ARF nucleolar localization, restricts NPM1 diffusion, and reduces cellular proliferation.

Conclusions:

  • NPM1 acts as a chaperone by promoting p14ARF phase separation and assembly into a meso-scale network.
  • This mechanism links p14ARF's partial folding and nucleolar localization to its function in regulating cellular proliferation and stress responses.
  • The findings provide structural insights into NPM1's multifaceted role in nucleolar biology and tumor suppression.