Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
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...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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...
Nuclear Localization Signals and Import01:46

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Extending structural surfaceomics to identify aberrant conformations of tumor surface proteins as potential immunotherapy targets.

bioRxiv : the preprint server for biology·2026
Same author

Systematic discovery of pro- and anti-HIV host factors in primary human CD4+ T cells.

Cell·2026
Same author

The scientific legacy of Martin Karplus from the perspective of his collaborators.

Biophysical journal·2026
Same author

The filamentous ultrastructure of the PopZ condensate is required for its cellular function.

Nature structural & molecular biology·2026
Same author

ModelCIF Update: Supporting Emerging Classes of Computational Macromolecular Models.

Journal of molecular biology·2026
Same author

IHMValidation: Assessment of Integrative Structure Models Deposited to the Protein Data Bank.

Journal of molecular biology·2025
Same journal

A pan-vertebrate signaling motif controls the molecular function of intracellular AQP12.

The Journal of cell biology·2026
Same journal

Synergistic assembly, disassembly, and protection of complex forms of bundled F-actin.

The Journal of cell biology·2026
Same journal

Recruitment and release of XPG during NER is controlled by pre- and post-incision factors and EXO1.

The Journal of cell biology·2026
Same journal

Meiotic CENP-C supports centromere assembly and kinetochore recruitment in spermatogenesis.

The Journal of cell biology·2026
Same journal

Phosphatidylserine and RhoB connect PI4P and PA metabolism to maintain plasma membrane identity.

The Journal of cell biology·2026
Same journal

PIKfyve influences inter-organelle contacts with lysosomes to modulate the endoplasmic reticulum.

The Journal of cell biology·2026
See all related articles

Related Experiment Video

Updated: May 24, 2026

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
11:55

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

Structure-function mapping of a heptameric module in the nuclear pore complex.

Javier Fernandez-Martinez1, Jeremy Phillips, Matthew D Sekedat

  • 1Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10065, USA.

The Journal of Cell Biology
|February 15, 2012
PubMed
Summary
This summary is machine-generated.

Researchers determined the structure of the yeast nuclear pore complex (NPC) Nup84 complex using integrative methods. This reveals how the NPC assembles and interacts with the nuclear envelope, offering evolutionary insights.

More Related Videos

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Related Experiment Videos

Last Updated: May 24, 2026

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
11:55

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • The nuclear pore complex (NPC) is crucial for regulating transport between the nucleus and cytoplasm in eukaryotic cells.
  • Understanding the structure of NPC components is key to deciphering nucleocytoplasmic transport mechanisms.

Purpose of the Study:

  • To determine the high-resolution structure of the yeast Nup84 complex, an essential NPC component.
  • To elucidate the assembly of the Nup84 complex within the NPC and its interaction with the nuclear envelope.

Main Methods:

  • An integrative approach combining negative-stain electron microscopy and protein domain-mapping.
  • Determination of subunit configuration using spatial restraints.
  • Mapping phenotypic data onto the complex structure.

Main Results:

  • The ~600-kD heptameric Nup84 complex structure was determined to ~1.5 nm precision.
  • Identified regions responsible for NPC-nuclear envelope membrane interactions and connections within the NPC.
  • Proposed a model for Nup84 complex assembly and its evolutionary history.

Conclusions:

  • Integrative approaches using low-resolution data can yield functionally relevant intermediate-resolution structures.
  • The determined structure provides insights into NPC assembly, stability, and evolution.