Related Experiment Video
Updated: Oct 29, 2025
07:20
Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
Published on: June 16, 2023
2.4K
ATG9A protects the plasma membrane from programmed and incidental permeabilization
Aurore Claude-Taupin1,2, Jingyue Jia1,2, Zambarlal Bhujabal3
1Autophagy, Inflammation and Metabolic (AIM) Center of Biochemical Research Excellence, University of New Mexico Health Sciences Center, Albuquerque, NM, USA.
Nature Cell Biology
|July 14, 2021
Summary
The integral membrane protein ATG9A, working with IQGAP1 and ESCRT components, protects the plasma membrane from damage. ATG9A is crucial for maintaining plasma membrane integrity against various harmful agents.
Area of Science:
- Cell Biology
- Molecular Biology
- Autophagy Research
Background:
- ATG9A is an integral membrane protein vital for autophagy.
- ATG9A is found in various cellular compartments, including the plasma membrane (PM).
- The specific functions of ATG9A at the PM remain unclear.
Purpose of the Study:
- To investigate the role of ATG9A at the plasma membrane.
- To explore the interaction of ATG9A with IQGAP1 and the ESCRT system.
- To determine the contribution of ATG9A to plasma membrane integrity.
Main Methods:
- Investigated ATG9A localization and function at the plasma membrane.
- Utilized knockout models to assess ATG9A's role in PM protection.
- Examined the interplay between ATG9A, IQGAP1, and ESCRT components.
Main Results:
- ATG9A collaborates with IQGAP1 and ESCRT components to safeguard the PM.
- ATG9A and ESCRTs exhibit similar protective effects against PM injury.
- ATG9A deficiency increases PM susceptibility to permeabilization by diverse agents.
Conclusions:
- ATG9A, IQGAP1, and the ESCRT system cooperate to maintain plasma membrane integrity.
- ATG9A plays a significant role in cellular defense against plasma membrane damage.
Related Concept Videos
01:19Translocation of Proteins into the Mitochondria
9.3K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
9.3K
01:06Carrier-Mediated Transport
689
Carrier-mediated transport is a pivotal process in drug absorption, particularly for lipid-insoluble drugs, and encompasses facilitated diffusion and active transport. Facilitated diffusion allows drugs to move along their concentration gradient without energy expenditure, while active transport utilizes ATP to drive drug movement against this gradient.
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...
689
01:19Membrane Asymmetry Regulating Transporters
6.2K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
6.2K
02:37DNA Damage can Stall the Cell Cycle
9.6K
In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
9.6K
01:32Export of Misfolded Proteins out of the ER
4.4K
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...
4.4K
01:11Protein Transport to the Outer Chloroplast Membrane
2.1K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
2.1K