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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.
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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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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.
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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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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.
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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 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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p14ARF forms meso-scale assemblies upon phase separation with NPM1.

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

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Nucleophosmin (NPM1) sequesters the tumor suppressor p14 Alternative Reading Frame (p14ARF) in nucleoli via phase separation. This interaction stabilizes p14ARF, impacting cell viability and tumor suppression.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • NPM1 is a nucleolar chaperone involved in ribosome biogenesis, stress responses, and tumor suppression.
  • NPM1 regulates the p14ARF tumor suppressor protein, crucial for cell cycle arrest.
  • The structural basis for NPM1 regulation of p14ARF has been unclear.

Approach:

  • Investigated the structural features of the p14ARF-NPM1 complex.
  • Utilized structural modeling to elucidate the mechanisms of p14ARF regulation by NPM1.
  • Examined the role of phase separation in p14ARF-NPM1 interactions within nucleoli.

Key Points:

  • NPM1 sequesters p14ARF within phase-separated condensates, forming a gel-like network.
  • Hydrophobic interactions involving p14ARF's N-terminal domain mediate phase separation with NPM1.
  • This process enhances nucleolar localization, restricts diffusion, and reduces cell viability.

Conclusions:

  • NPM1's chaperone function involves phase separation and meso-scale assembly of p14ARF.
  • Mechanistically links nucleolar p14ARF localization to partial folding and phase separation with NPM1.
  • Provides novel insights into NPM1's role in nucleolar stress responses and tumor suppression.