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Related Concept Videos

Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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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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Regulated mRNA Transport02:22

Regulated mRNA Transport

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In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing...
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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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Nonsense-mediated mRNA Decay02:27

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The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...
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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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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mRNA Stability and Gene Expression02:51

mRNA Stability and Gene Expression

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The structure and stability of mRNA molecules regulates gene expression, as mRNAs are a key step in the pathway from gene to protein. In eukaryotes, the half-life of mRNA varies from a few minutes up to several days. mRNA stability is essential in growth and development. The absence of the proteins regulating its stability, such as tristetraprolin in mice, can cause systemic issues, including bone marrow overgrowth, inflammation, and autoimmunity.
Cis-acting Elements involved in mRNA stability
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Updated: Oct 22, 2025

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
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The mRNA decapping complex is buffered by nuclear localization.

Kiril Tishinov1, Anne Spang1

  • 1Biozentrum, University of Basel, Spitalstrasse 41, CH-4056 Basel, Switzerland.

Journal of Cell Science
|August 26, 2021
PubMed
Summary
This summary is machine-generated.

Scd6 and Edc3 proteins regulate mRNA decay by controlling the location of the Dcp1-Dcp2 decapping complex. This ensures proper P-body assembly and function in yeast cells.

Keywords:
Endoplasmic reticulumMembraneless granulesNucleo-cytoplasmic transportPhase separationProcessing bodiesmRNA

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Yeast Genetics

Background:

  • mRNA decay regulates cellular proteome, with processing bodies (P-bodies) as key sites.
  • P-body assembly into granules under stress is poorly understood.
  • The localization and regulation of mRNA decay factors are critical for cellular homeostasis.

Purpose of the Study:

  • To elucidate the regulatory mechanisms governing P-body assembly in Saccharomyces cerevisiae.
  • To identify proteins involved in controlling the localization of the Dcp1-Dcp2 decapping complex.
  • To understand the interplay between cytoplasmic and nuclear localization of Dcp1/2.

Main Methods:

  • Yeast genetics and molecular biology techniques.
  • Analysis of protein localization and interactions.
  • Investigating the role of Scd6, Edc3, and Kap95 in P-body formation.

Main Results:

  • Scd6 and Edc3 partially and redundantly sequester the Dcp1-Dcp2 complex in the cytoplasm, preventing nuclear import.
  • Dcp2 possesses a nuclear localization signal overlapping its RNA-binding site, suggesting dual regulatory control.
  • Nuclear Dcp1/2 may serve as a stored pool, indicating dynamic cytoplasmic-nuclear exchange.
  • Cytoplasmic Dcp1/2 interacts with Dhh1 via Edc3, promoting P-body formation at the endoplasmic reticulum.

Conclusions:

  • Scd6 and Edc3 are crucial regulators of P-body assembly by controlling Dcp1/2 localization.
  • Nuclear import of Dcp1/2 does not drive mRNA decay but may represent a storage mechanism.
  • P-body formation is linked to endoplasmic reticulum localization and phase separation driven by Dcp1/2, Dhh1, and Edc3 interactions.