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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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Nuclear Export

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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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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Updated: May 29, 2025

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Nucleoporin PNET1 coordinates mitotic nuclear pore complex dynamics for rapid cell division.

Yiling Fang1, Yu Tang1, Peiqiao Xie1

  • 1Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA, USA.

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|January 31, 2025
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Summary

Plant Nuclear Envelope Transmembrane 1 (PNET1) facilitates rapid cell division by regulating nuclear pore complex (NPC) assembly and disassembly. Its phosphorylation controls NPC dynamics during mitosis, crucial for cell proliferation in plants and cancer.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Plant Biology

Background:

  • The nuclear pore complex (NPC) regulates macromolecule transport between the nucleus and cytoplasm.
  • Understanding NPC dynamics during cell division is crucial for cell cycle control.

Purpose of the Study:

  • To investigate the role of Plant Nuclear Envelope Transmembrane 1 (PNET1) in nuclear pore complex (NPC) function during cell division.
  • To elucidate the mechanism by which PNET1 regulates NPC assembly and disassembly.

Main Methods:

  • Arabidopsis thaliana cell culture and genetic analysis.
  • Phosphorylation site mapping and interaction studies.
  • Microscopy to observe NPC dynamics during mitosis.

Main Results:

  • PNET1 is a transmembrane nucleoporin predominantly expressed in actively dividing cells.
  • PNET1's cell cycle-dependent phosphorylation regulates NPC disassembly during mitosis and reassembly in daughter cells.
  • PNET1 is essential for rapid cell growth in Arabidopsis meristem and callus tissues.

Conclusions:

  • PNET1 plays a conserved role in facilitating rapid cell division in highly proliferative tissues.
  • PNET1's phosphorylation acts as a key switch for NPC dynamics during the cell cycle.
  • The human PNET1 homologue is upregulated in cancer, suggesting a role in cancer cell proliferation.