Jove
Visualize
Contact Us

Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.8K
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...
4.8K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

7.6K
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...
7.6K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

5.9K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
5.9K
Nuclear Export01:42

Nuclear Export

3.7K
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...
3.7K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

4.9K
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...
4.9K
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

12.1K
Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
12.1K

You might also read

Related Articles

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

Sort by
Same author

Single-molecule dissection of CFTR folding defects and pharmacological rescue.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Structurally diverse viral inhibitors converge on a shared mechanism to stall the antigen transporter TAP.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Structure of CFTR bound to (R)-BPO-27 unveils a pore-blockage mechanism.

Nature communications·2025
Same author

A Structural Atlas of TAP Inhibition by Herpesviruses and Poxviruses.

bioRxiv : the preprint server for biology·2025
Same author

Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2.

Nature communications·2025
Same author

The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.

Proceedings of the National Academy of Sciences of the United States of America·2024
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 Experiment Video

Updated: Sep 15, 2025

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
12:48

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

Published on: August 21, 2017

8.3K

Nucleotide-dependent conformational changes direct peptide export by the transporter associated with antigen

James Lee1, Victor Manon1,2, Jue Chen1,3,4

  • 1Laboratory of Membrane Biophysics and Biology, The Rockefeller University, New York, NY 10065.

Biorxiv : the Preprint Server for Biology
|July 16, 2025
PubMed
Summary

The transporter associated with antigen processing (TAP) moves peptides into the endoplasmic reticulum for adaptive immunity. Cryo-EM structures reveal its transport cycle, showing how it binds, transports, and releases peptides.

Keywords:
ABC transporterMHC-Iadaptive immunityantigen presentationnucleotide binding domaintransporter associated with antigen processing

More Related Videos

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
07:55

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

11.9K
Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

12.6K

Related Experiment Videos

Last Updated: Sep 15, 2025

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
12:48

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

Published on: August 21, 2017

8.3K
Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
07:55

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

11.9K
Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

12.6K

Area of Science:

  • Structural Biology
  • Immunology
  • Molecular Biology

Background:

  • The transporter associated with antigen processing (TAP) is crucial for adaptive immunity by transporting peptides to the endoplasmic reticulum for MHC-I loading.
  • While TAP's peptide-binding selectivity is known, its transport and release mechanisms remain unclear.

Purpose of the Study:

  • To elucidate the structural mechanisms of peptide transport by human TAP.
  • To visualize TAP in multiple functional states throughout its transport cycle.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine high-resolution structures of human TAP.
  • Structures were captured in various functional states, including inward-facing and outward-facing conformations.

Main Results:

  • ATP binding stabilizes the inward-facing conformation of TAP.
  • A temperature-dependent transition to the outward-facing state reconfigures the peptide-binding site for release.
  • ATP hydrolysis and nucleotide-binding domain (NBD) separation reset the transport cycle.

Conclusions:

  • These structures provide a comprehensive framework for understanding TAP's peptide transport mechanism.
  • The findings offer insights into vanadate trapping and trans-inhibition mechanisms.
  • This work clarifies how TAP facilitates peptide loading onto MHC-I molecules.