Related Experiment Video
Updated: Jul 20, 2025

14:55
Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
15.5K
[Assembly and Disassembly of the Nuclear Pore Complex: A View from the Structural Side]
A V Orlova1,2, S G Georgieva1, D V Kopytova1
1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia.
Molekuliarnaia Biologiia
|August 2, 2023
Summary
Nuclear pore complexes (NPCs) facilitate nucleocytoplasmic transport via nucleoporins. This study details NPC structure, properties, and cell cycle-dependent assembly/disassembly mechanisms.
Area of Science:
- Cell Biology
- Structural Biology
Context:
- Nucleocytoplasmic transport is essential for cellular function, mediated by nuclear pore complexes (NPCs).
- NPCs are intricate protein structures spanning the nuclear envelope, regulating molecular traffic.
- Understanding NPC architecture and dynamics is crucial for cell biology.
Purpose:
- To elucidate the structural organization and properties of nucleoporins within NPCs.
- To investigate the mechanisms governing NPC assembly and disassembly during the cell cycle.
Summary:
- This work examines the hierarchical organization of NPCs, built from nucleoporins forming octameric structures.
- It details the permeability barrier within NPCs enabling selective molecular transport.
- The study covers both the static structure and dynamic assembly/disassembly processes of NPCs.
Impact:
- Provides a comprehensive overview of nuclear pore complex structure and function.
- Offers insights into the dynamic regulation of nucleocytoplasmic transport.
- Contributes to understanding fundamental cellular processes and potential therapeutic targets.
Related Concept Videos
Nuclear Protein Sorting
4.7K
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...
4.7K
Protein Complex Assembly
10.7K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.7K
Disassembly of Intermediate Filaments
2.1K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.1K
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
Assembly of Cytoskeletal Filaments
21.1K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
21.1K
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

