Journal
CELL REPORTS
Volume 37, Issue 7, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2021.109937
Keywords
-
Categories
Funding
- National Key R&D Program of China [2017YFA0506300]
- National Natural Science Foundation [31770820]
- Non-profit Central Research Institute Fund of Chinese Academy of Medical Sciences [2019-RC-HL-022]
Ask authors/readers for more resources
The study found that Nat3 plays a crucial role in autophagy by regulating multiple steps in the process through N-terminal acetylation of proteins like Act1 and Vps1, promoting the transport of Atg9 vesicles and the formation of autophagosomes.
Acetyl ligation to the amino acids in a protein is an important posttranslational modification. However, in contrast to lysine acetylation, N-terminal acetylation is elusive in terms of its cellular functions. Here, we identify Nat3 as an N-terminal acetyltransferase essential for autophagy, a catabolic pathway for bulk transport and degradation of cytoplasmic components. We identify the actin cytoskeleton constituent Act1 and dynamin-like GTPase Vps1 (vacuolar protein sorting 1) as substrates for Nat3-mediated N-terminal acetylation of the first methionine. Acetylated Act1 forms actin filaments and therefore promotes the transport of Atg9 vesicles for autophagosome formation; acetylated Vps1 recruits and facilitates bundling of the SNARE (soluble N-ethylmaleimide-sensitive factor activating protein receptor) complex for autophagosome fusion with vacuoles. Abolishment of the N-terminal acetylation of Act1 and Vps1 is associated with blockage of upstream and downstream steps of the autophagy process. Therefore, our work shows that protein N-terminal acetylation plays a critical role in controlling autophagy by fine-tuning multiple steps in the process.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available