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...
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 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...
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...
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...
Nuclear Export01:42

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...

You might also read

Related Articles

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

Sort by
Same author

Structural and Mechanistic Basis of F227C-Mediated Hypersusceptibility to Islatravir in HIV-1 Reverse Transcriptase.

bioRxiv : the preprint server for biology·2026
Same author

Unraveling the Mechanism of HIV-1 Hypersusceptibility to Tenofovir Imparted by Islatravir Resistance Mutations.

bioRxiv : the preprint server for biology·2026
Same author

Catching our breath: development of interventions and therapies for respiratory syncytial virus.

Microbiology and molecular biology reviews : MMBR·2026
Same author

Structural Basis of Polypurine Track Strand Displacement by HIV-1 Reverse Transcriptase.

bioRxiv : the preprint server for biology·2026
Same author

Damaging the conical morphology of HIV-1 capsid by targeting the FG-binding pocket and disfavoring pentameric subunits needed for core closure.

bioRxiv : the preprint server for biology·2026
Same author

Lenacapavir prevents production of infectious HIV-1 by abrogating immature virus assembly.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jul 9, 2026

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

HIV-1 capsid interactions with Nuclear Pore Complex components support nuclear entry via affinity gradient.

Ivo Melčák1,2, Ryan L Slack1,2, Zachary C Lorson1,2

  • 1Center for ViroScience and Cure, Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322.

Proceedings of the National Academy of Sciences of the United States of America
|July 7, 2026
PubMed
Summary

HIV capsid (CA) proteins interact with nuclear pore complex (NPC) phenylalanine-glycine (FG) repeats. Specific FG motifs and enhancers create an affinity gradient, facilitating HIV capsid translocation into the nucleus.

Keywords:
HIVcapsid corenuclear importthe Nuclear Pore Complextranslocation

More Related Videos

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)
10:16

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)

Published on: May 5, 2012

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
11:45

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

Related Experiment Videos

Last Updated: Jul 9, 2026

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)
10:16

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)

Published on: May 5, 2012

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
11:45

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

Area of Science:

  • Cell Biology
  • Virology
  • Structural Biology

Background:

  • HIV capsid (CA) proteins must traverse the Nuclear Pore Complex (NPC) to enter the nucleus.
  • This translocation depends on interactions between CA proteins and phenylalanine-glycine (FG) repeats within nucleoporins (NUPs).
  • FG repeats are categorized into FG, GLFG, and FxFG motifs, distributed differently across the NPC.

Purpose of the Study:

  • To investigate the differential binding affinities of HIV CA to various FG repeat motifs and their associated enhancers within the NPC.
  • To elucidate the mechanism by which these interactions facilitate HIV capsid nuclear import.

Main Methods:

  • Quantitative analysis of binding affinities between HIV capsid proteins and different nucleoporin FG repeat motifs.
  • Characterization of novel FG repeat structures and their interaction enhancers using biophysical techniques.
  • Mapping the distribution and functional role of FG motifs and enhancers within the NPC.

Main Results:

  • HIV CA exhibits varying affinities for different FG motifs; GLFG motifs in the central NPC channel show higher affinity than canonical FG/FxFG motifs.
  • NUP153 contains an atypical FxFG motif, termed an "FG super-motif," which, along with basic residues, enhances CA binding ~1,000-fold.
  • Binding enhancers in NUP58, POM121, and NUP153 contribute to an affinity gradient that increases with proximity to the nuclear basket.

Conclusions:

  • The diverse FG repeats and their binding enhancers within the NPC establish an affinity gradient.
  • This gradient is crucial for potentiating the efficient translocation of the HIV capsid through the NPC.
  • Understanding these interactions may reveal new therapeutic targets for HIV infection.