Atg2: A novel phospholipid transfer protein that mediates de novo autophagosome biogenesis.

Authors:
Takuo Osawa
Takuo Osawa
National Institute of Advanced Industrial Science and Technology (AIST)
Japan
Nobuo N Noda
Nobuo N Noda
Hokkaido University
Japan

Protein Sci 2019 Jun 29;28(6):1005-1012. Epub 2019 Apr 29.

Institute of Microbial Chemistry (BIKAKEN), Tokyo 141-0021, Japan.

The degradation of cytoplasmic components via autophagy is crucial for intracellular homeostasis. In the process of autophagy, a newly synthesized isolation membrane (IM) is developed to sequester degradation targets and eventually the IM seals, forming an autophagosome. One of the most poorly understood autophagy-related proteins is Atg2, which is known to localize to a contact site between the edge of the expanding IM and the exit site of the endoplasmic reticulum (ERES). Recent advances in structural and biochemical analyses have been applied to Atg2 and have revealed it to be a novel multifunctional protein that tethers membranes and transfers phospholipids between them. Considering that Atg2 is essential for the expansion of the IM that requires phospholipids as building blocks, it is suggested that Atg2 transfers phospholipids from the ERES to the IM during the process of autophagosome formation, suggesting that lipid transfer proteins can mediate de novo organelle biogenesis.

Download full-text PDF

Source
https://onlinelibrary.wiley.com/doi/abs/10.1002/pro.3623
Publisher Site
http://dx.doi.org/10.1002/pro.3623DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6511744PMC
June 2019
6 Reads

Publication Analysis

Top Keywords

transfers phospholipids
8
atg2
5
localize contact
4
atg2 localize
4
blocks suggested
4
contact site
4
proteins atg2
4
building blocks
4
edge expanding
4
site edge
4
autophagy-related proteins
4
expanding exit
4
understood autophagy-related
4
eventually seals
4
eres process
4
targets eventually
4
process autophagosome
4
seals forming
4
forming autophagosome
4
suggested atg2
4

References

(Supplied by CrossRef)

Similar Publications