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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.
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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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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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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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Updated: Dec 5, 2025

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Nuclear envelope-vacuole contacts mitigate nuclear pore complex assembly stress.

Christopher L Lord1, Susan R Wente1

  • 1Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN.

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Cellular mechanisms mitigating nuclear pore complex (NPC) assembly stress involve nucleus-vacuole junctions (NVJs). These NVJs enhance NPC formation and viability in budding yeast when NPC biogenesis is compromised.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Yeast Genetics

Background:

  • Nuclear pore complex (NPC) biogenesis is crucial for nuclear transport and nuclear envelope (NE) morphology.
  • Failures in NPC assembly can lead to cellular defects, but mechanisms for alleviating this stress are poorly understood.

Purpose of the Study:

  • To investigate cellular mechanisms that mitigate stress during NPC assembly in Saccharomyces cerevisiae.
  • To elucidate the role of nucleus-vacuole junctions (NVJs) in response to compromised NPC biogenesis.

Main Methods:

  • Analysis of nup mutants in Saccharomyces cerevisiae.
  • Investigating the role of NVJs and lipid droplets in NPC assembly.
  • Studying the function of ATG1 in NE remodeling and nucleoporin degradation.

Main Results:

  • NE-vacuole contacts (NVJs) increase in nup mutants with compromised NPC assembly.
  • NVJs, along with lipid droplets, enhance NPC formation and cell viability in assembly mutants.
  • NVJs cooperate with ATG1 to remodel the NE and promote vacuole-dependent degradation of nucleoporins.

Conclusions:

  • NVJs play a critical role in mitigating cellular stress caused by disrupted NPC assembly.
  • These interorganelle contacts significantly improve the physiology of NPC assembly mutants.
  • The findings define a novel coordination mechanism between NE-vacuole contacts and cellular responses to maintain homeostasis.