Related Experiment Video

Updated: Oct 15, 2025

Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

9.3K

Rabaptin5 targets autophagy to damaged endosomes and Salmonella vacuoles via FIP200 and ATG16L1

Valentina Millarte1, Simon Schlienger1, Simone Kälin1

  • 1Biozentrum, University of Basel, Basel, Switzerland.

EMBO Reports
|October 27, 2021
PubMed

Insights

Rabaptin5 targets damaged early endosomes for selective autophagy, crucial for cellular homeostasis. This process involves interactions with FIP200 and ATG16L1, aiding in pathogen clearance and organelle quality control.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Selective autophagy maintains cellular homeostasis by removing damaged organelles.
  • Mechanisms for autophagic target selection are not fully understood.
  • Rabaptin5 is a known regulator of early endosome identity and maturation.

Purpose of the Study:

  • To investigate the role of Rabaptin5 in selective autophagy.
  • To identify novel Rabaptin5 interactors involved in autophagy.
  • To elucidate the mechanism of Rabaptin5-mediated autophagic targeting of early endosomes.

Main Methods:

  • Co-immunoprecipitation to identify Rabaptin5 interactors.
  • Cell-based assays to study autophagy of damaged early endosomes.
  • Analysis of bacterial infection models.

Main Results:

  • FIP200 and ATG16L1 were identified as novel Rabaptin5 interactors.
  • Rabaptin5 and its interaction motif with ATG16L1 are required for autophagy of damaged early endosomes.
  • Rabaptin5 facilitates the autophagic elimination of Salmonella during early infection.

Conclusions:

  • Rabaptin5 plays a novel role in the quality control of early endosomes.
  • Rabaptin5 mediates selective autophagy targeting of damaged early endosomes and phagosomes.
  • This pathway is important for cellular homeostasis and pathogen clearance.
Keywords:
ATG16L1Rabaptin5Salmonella-containing vacuolesautophagyearly endosomes

More Related Videos

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein07:20

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

2.4K
Author Spotlight: A Selective Luciferase-Based Assay for Monitoring ATG4B 27 Activity in Cells09:51

Author Spotlight: A Selective Luciferase-Based Assay for Monitoring ATG4B 27 Activity in Cells

Published on: June 30, 2023

1.1K

Related Concept Videos

Autophagic Cell Death01:18

Autophagic Cell Death

Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and...
3.6K
Autophagy01:27

Autophagy

Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
4.8K
Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...
2.9K
Delivery Pathways to the Lysosome01:36

Delivery Pathways to the Lysosome

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...
8.1K
Rab Cascades01:25

Rab Cascades

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.
2.8K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
4.1K