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Related Concept Videos

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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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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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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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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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Updated: Jun 3, 2025

Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection
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Setdb1 and Atf7IP form a hetero-trimeric complex that blocks Setdb1 nuclear export.

Leena Kariapper1, Ila A Marathe2, Ashley B Niesman3

  • 1Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Biorxiv : the Preprint Server for Biology
|January 7, 2025
PubMed
Summary

Setdb1 and Atf7IP form a stable complex, revealing how Atf7IP regulates Setdb1

Keywords:
Setdb1chromatinhistonemethylationretrotransposon

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Area of Science:

  • Epigenetics
  • Molecular Biology
  • Structural Biology

Background:

  • Histone H3K9 methylation (H3K9me) by Setdb1 silences retrotransposons (rTEs).
  • Atf7IP is crucial for Setdb1's nuclear localization, activation, and chromatin recruitment.
  • Structural details of the Setdb1/Atf7IP interaction remain largely uncharacterized.

Purpose of the Study:

  • To elucidate the structural basis of the Setdb1/Atf7IP interaction.
  • To understand how Atf7IP regulates Setdb1's nuclear localization and activity.
  • To investigate the role of Atf7IP paralogs in Setdb1 complex formation and function.

Main Methods:

  • AlphaFold2 predictions for structural modeling.
  • Biochemical reconstitutions to validate complex formation.
  • In vitro and in cell assays to study protein interactions.

Main Results:

  • Setdb1 and Atf7IP form a stable heterotrimeric complex (1:2 stoichiometry) in vitro and in cells.
  • Atf7IP self-associates, and Setdb1 binding resolves these multimeric complexes.
  • Atf7IP binds Setdb1 via coiled-coil interactions, including Setdb1's nuclear export signals (NES), thereby preventing CRM1-mediated nuclear export.
  • Setdb1 also forms heterotrimers with Atf7IP2, and mixed heterotrimers (Setdb1/Atf7IP/Atf7IP2) are possible.

Conclusions:

  • Atf7IP directly binds Setdb1's NES motifs, inhibiting nuclear export and stabilizing Setdb1 in the nucleus.
  • The formation of heterotrimers with varying Atf7IP/Atf7IP2 ratios allows for fine-tuning of Setdb1 activity and H3K9me.
  • These findings provide structural insights into the regulation of heterochromatin formation by the Setdb1/Atf7IP complex.