Related Experiment Video
Updated: Jul 12, 2025

12:13
Single-Molecule Imaging of Nuclear Transport
Published on: June 9, 2010
13.4K
Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex
Coby Rush1, Zecheng Jiang1, Mark Tingey1
1Department of Biology, Temple University, Philadelphia, PA, United States.
Frontiers in Cell and Developmental Biology
|October 25, 2023
Summary
Nuclear pore complexes (NPCs) control transport via FG-Nups. This review explores models of FG-Nup structure and dynamics, highlighting challenges in their characterization and validation.
Area of Science:
- Cell Biology
- Biophysics
- Structural Biology
Background:
- The nuclear pore complex (NPC) is a crucial gatekeeper for nucleocytoplasmic transport.
- Intrinsically disordered regions in phenylalanine-glycine (FG) nucleoporins (Nups) pose challenges for structural studies.
Purpose of the Study:
- To provide a comprehensive overview of existing models for FG-Nup organization and behavior within the NPC.
- To comparatively analyze the dynamic and structural attributes proposed by each model.
Main Methods:
- Literature review and synthesis of existing research on FG-Nup models.
- Comparative analysis of proposed structural and dynamic characteristics.
Main Results:
- Multiple models exist for FG-Nup structure and dynamics, each with distinct proposed features.
- Technological advancements have improved understanding, but challenges remain in characterizing intrinsically disordered regions.
Conclusions:
- Existing models offer insights into FG-Nup function but lack definitive empirical validation.
- Further research is needed to unequivocally validate proposed FG-Nup models and their roles in nucleocytoplasmic transport.
Related Concept Videos
Nuclear Protein Sorting
4.6K
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...
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...
4.6K
Regulation of Nuclear Protein Sorting
2.4K
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...
2.4K
Nuclear Export of mRNA
7.7K
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...
7.7K
Nuclear Export
3.7K
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...
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
3.7K
Structure of Porins
3.0K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.0K
Nuclear Localization Signals and Import
5.7K
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...
5.7K

