Jove
Visualize
Contact Us

Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

6.5K
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...
6.5K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.9K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.9K
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

9.0K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
9.0K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.9K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.9K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
2.1K
Delivery Pathways to the Lysosome01:36

Delivery Pathways to the Lysosome

8.7K
Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
8.7K

You might also read

Related Articles

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

Sort by
Same author

Regulation of solid tumors by the peripheral nervous system.

The Journal of experimental medicine·2026
Same author

L-type pyocins inhibit the BAM complex to kill without cell entry.

Nature communications·2026
Same author

Structural basis for independent pore function of Vpb4 from Bacillus thuringiensis.

Nature communications·2026
Same author

The Kelch-Repeat Superfamily Gene <i>SiNL4</i> Regulates the Leaf Width in Foxtail Millet.

Plants (Basel, Switzerland)·2026
Same author

Chromatin context-dependent deacetylation by the asymmetric Rpd3L.

Nucleic acids research·2026
Same author

Effects of low temperature on energy metabolism during germination of foxtail millet (Setaria italica L.) seeds.

Plant physiology and biochemistry : PPB·2026
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: Jan 13, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

2.9K

Structure of the lysosomal KICSTOR-GATOR1-SAMTOR nutrient-sensing supercomplex.

Christopher J Lupton1, Charles Bayly-Jones2, Shuqi Dong3

  • 1Cancer Program, Biomedicine Discovery Institute, Monash University, Clayton 3800, VIC, Australia.

Cell
|January 9, 2026
PubMed
Summary

Researchers elucidated the KICSTOR-GATOR1 complex structure, revealing a crescent assembly crucial for regulating mTORC1 activation. This finding explains how amino acid levels control cell growth via the Rag GTPases and lysosomal signaling.

Keywords:
GATOR1KICSTORRAG GTPaseRag-RagulatorS-adenosylmethionineSAMTORSZT2cell metabolismcryo-EMmTORC1

More Related Videos

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

7.7K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.8K

Related Experiment Videos

Last Updated: Jan 13, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

2.9K
High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

7.7K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.8K

Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • The mechanistic target of rapamycin complex 1 (mTORC1) pathway regulates cell growth and is activated by amino acid availability.
  • Rag GTPases act as a molecular switch at the lysosome, linking amino acid levels to mTORC1 activation.
  • GATOR1, a GTPase-activating protein (GAP) for Rags, inhibits mTORC1 under low amino acid conditions, but its lysosomal recruitment by KICSTOR was unclear.

Purpose of the Study:

  • To determine the structural basis of KICSTOR-GATOR1 complex formation.
  • To understand how this complex regulates GATOR1's GAP activity towards Rag GTPases.
  • To gain insights into the mechanism of amino acid sensing by the SAMTOR-KICSTOR complex.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) to resolve the KICSTOR-GATOR1 structure.
  • Biochemical assays to assess the impact of mutations on complex formation and mTORC1 regulation.
  • Structural analysis of the SAMTOR-KICSTOR interaction.

Main Results:

  • The KICSTOR-GATOR1 complex forms a large, crescent-shaped assembly (∼60 nm).
  • GATOR1 binds KICSTOR through an extensive interface, essential for regulating mTORC1.
  • SAMTOR binds KICSTOR in a way that prevents simultaneous metabolite binding, suggesting a regulatory mechanism.
  • KICSTOR and GATOR1 form a dimeric supercomplex, orienting GATOR1 for efficient Rag GTPase engagement.

Conclusions:

  • The KICSTOR-GATOR1 structure reveals a stable lysosomal docking complex essential for mTORC1 regulation.
  • The complex's architecture dictates GATOR1's GAP activity, favoring Rag GTPase engagement under specific conditions.
  • Structural insights into SAMTOR binding provide a mechanism for amino acid sensing and downstream signaling control.