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Related Concept Videos

Nuclear Protein Sorting01:34

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...
Structure of Porins01:21

Structure of Porins

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 precursors...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Nuclear Export of mRNA02:31

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...

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Related Experiment Video

Updated: Jun 4, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Perspective on the metazoan nuclear pore complex.

Tal Maimon1, Ohad Medalia

  • 1Department of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University, Beer-Sheva, Israel.

Nucleus (Austin, Tex.)
|February 18, 2011
PubMed
Summary

The nuclear pore complex (NPC) acts as the nucleus gateway, controlling molecule transport. Recent cryo-electron tomography reveals new details of the Xenopus NPC structure.

Keywords:
cryo-electron tomographynuclear envelopenuclear pore complexxenopus oocytes

Related Experiment Videos

Last Updated: Jun 4, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Area of Science:

  • Cell Biology
  • Structural Biology
  • Biophysics

Background:

  • The nuclear pore complex (NPC) is a large protein assembly embedded in the nuclear envelope.
  • It regulates the transport of molecules between the nucleus and cytoplasm.
  • Understanding NPC structure is crucial for comprehending nuclear function and cellular processes.

Purpose of the Study:

  • To present novel structural insights into the metazoan nuclear pore complex (NPC).
  • To discuss recent advancements in determining NPC structure using advanced imaging techniques.
  • To outline future directions for high-resolution structural and functional analysis of NPCs.

Main Methods:

  • X-ray crystallography for individual nucleoporin (Nup) structures.
  • Cryo-electron tomography (cryo-ET) for overall NPC assembly analysis.
  • Advanced image processing techniques applied to cryo-ET data.

Main Results:

  • Medium-resolution structure of the Xenopus oocyte metazoan NPC was resolved.
  • Novel structural features of the Xenopus NPC were identified.
  • Integration of crystallographic and tomographic data provided new details.

Conclusions:

  • Recent structural studies have significantly advanced our understanding of NPC architecture.
  • The Xenopus NPC exhibits unique features that warrant further investigation.
  • Future research aims to achieve high-resolution structural and functional characterization of NPCs.