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

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

4.5K
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...
4.5K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

7.2K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
7.2K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.4K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
2.4K
Rab Cascades01:25

Rab Cascades

2.6K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
2.6K
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.5K
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...
4.5K
Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

3.2K
Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
3.2K

You might also read

Related Articles

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

Sort by
Same author

Crocin Targets HSP90 to Suppress NLRP3/Caspase-1-Mediated Sertoli Cell Pyroptosis.

Molecular reproduction and development·2026
Same author

Author Correction: In situ cryo-ET defines the ultrastructure of ER exit sites in human cells.

Nature cell biology·2026
Same author

EphB4 inhibition defines a druggable synthetic-lethal vulnerability in MYC-driven triple-negative breast cancer.

Cell death & disease·2026
Same author

Surface BO<sub>3</sub> Configuration in Li-Rich Cathode Materials Enabling Highly-Stable Anionic Redox Reactions.

Angewandte Chemie (International ed. in English)·2026
Same author

Reliability assessment of key equipment for coal gasification using artificial intelligence technology.

PloS one·2026
Same author

Experimental and numerical investigations on the transport mechanisms of Ti<sub>3</sub>C<sub>2</sub>T<sub>x</sub> MXene under variable flow and solution chemistry.

Journal of hazardous materials·2026

Related Experiment Video

Updated: Jun 6, 2025

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
11:05

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Published on: February 21, 2019

9.0K

Multiple roles for TFG ring complexes in neuronal cargo trafficking.

Ziheng Zhang, Molly M Lettman, Amber L Schuh

    Biorxiv : the Preprint Server for Biology
    |November 22, 2024
    PubMed
    Summary
    This summary is machine-generated.

    Pathological variants in Trk-fused gene (TFG) cause hereditary spastic paraplegia (HSP) by disrupting its octameric ring structure. These mutations destabilize TFG complexes, leading to axonopathy and neurodegeneration through distinct mechanisms.

    More Related Videos

    Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
    08:55

    Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

    Published on: December 29, 2017

    9.5K
    Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
    11:09

    Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

    Published on: October 30, 2014

    9.3K

    Related Experiment Videos

    Last Updated: Jun 6, 2025

    Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
    11:05

    Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

    Published on: February 21, 2019

    9.0K
    Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
    08:55

    Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

    Published on: December 29, 2017

    9.5K
    Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
    11:09

    Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

    Published on: October 30, 2014

    9.3K

    Area of Science:

    • Neuroscience
    • Structural Biology
    • Genetics

    Background:

    • Pathological variants in Trk-fused gene (TFG) are linked to neurodegenerative diseases.
    • Mutations in the TFG amino-terminal PB1 domain are associated with hereditary spastic paraplegia (HSP).
    • The structural basis for TFG's role in HSP remains unclear.

    Purpose of the Study:

    • To elucidate the structural mechanism of TFG octamer formation.
    • To investigate how HSP-associated mutations affect TFG structure and function.
    • To understand the molecular basis of TFG-mediated neurodegeneration.

    Main Methods:

    • X-ray crystallography
    • Cryo-electron microscopy
    • Structural modeling

    Main Results:

    • A structural model of TFG reveals its formation of octameric ring complexes.
    • A network of electrostatic and hydrophobic interactions stabilizes the TFG protomer interface.
    • HSP-associated mutations disrupt this interface, destabilizing octamers and causing axonopathy.
    • The in vivo impact of TFG variants is not uniform, suggesting diverse pathogenic mechanisms.

    Conclusions:

    • TFG forms octameric rings through specific intermolecular interactions.
    • HSP-causing mutations in TFG destabilize these octamers, leading to neurodegeneration.
    • Distinct mechanisms underlie TFG mutation-induced neurodegenerative disease.