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Nuclear Export of mRNA

Nuclear Export of mRNA

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...

Overview of Protein Sorting and Transport

Overview of Protein Sorting and Transport

Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation. In gated transport, folded...

Nuclear Protein Sorting

Nuclear Protein Sorting

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...

Nuclear Localization Signals and Import

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of 2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...

Nuclear Export

Nuclear Export

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.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...

Directionality of Nuclear Transport

Directionality of Nuclear Transport

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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Related Experiment Video

Updated: Jul 19, 2026

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Published on: March 11, 2011

Nucleocytoplasmic transport: Ran, beta and beyond.

S Kuersten¹, M Ohno, I W Mattaj

¹Gene Expression Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117, Heidelberg, Germany.

Trends in Cell Biology

|November 24, 2001

Summary

Nucleocytoplasmic transport moves molecules rapidly and selectively. This review explores known mechanisms and novel functions of nuclear transport, even in cells lacking a nucleus.

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Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells

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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Published on: February 21, 2019

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Nucleocytoplasmic transport is essential for cellular function, involving the movement of proteins, RNAs, and macromolecular complexes between the nucleus and cytoplasm.
The importin beta family and Ran GTPase are key regulators of this transport, ensuring efficiency and selectivity.
However, some transport processes do not align with the established importin/Ran model, suggesting alternative mechanisms.

Purpose of the Study:

To review current understanding of diverse nucleocytoplasmic transport mechanisms.
To evaluate cellular functions mediated by nucleocytoplasmic transport machinery in non-eukaryotic systems or anucleated cells.

Main Methods:

Literature review and synthesis of existing research on nucleocytoplasmic transport.
Analysis of case studies demonstrating transport mechanisms outside the canonical importin/Ran pathway.
Evaluation of functional roles of transport components in nuclear and non-nuclear contexts.

Main Results:

Established models involving importin beta and Ran GTPase explain many, but not all, nucleocytoplasmic transport events.
Alternative and less understood mechanisms contribute to the specificity and rapidity of transport.
Nucleocytoplasmic transport molecules and pathways are repurposed for critical cellular functions in the absence of a nucleus.

Conclusions:

Nucleocytoplasmic transport is more complex than initially understood, involving multiple pathways.
The study of these transport systems offers insights into fundamental cellular processes, including those in anucleated cells.
Further research is needed to fully elucidate the diversity and function of nucleocytoplasmic transport.