ArticleMolecules and cells2017
The Roles of the SNARE Protein Sed5 in Autophagy in Saccharomyces cerevisiae.
Article in Molecules and cells, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Atg23 Interacts With Both the N- and C-termini of Atg9 Via a Hydrophobic Binding Pocket.bioRxiv : the preprint server for biology · 2025Article
- The TRAPPIII complex regulates development and virulence of Fusarium graminearum by coordinating autophagy and intracellular transport.PLoS pathogens · 2025Article
- Article
- The Golgin Protein RUD3 Regulates Fusarium graminearum Growth and Virulence.Applied and environmental microbiology · 2021Article
- Acetyl-CoA carboxylase 1-dependent lipogenesis promotes autophagy downstream of AMPK.The Journal of biological chemistry · 2019Article
- Autophagy requires Tip20 inJournal of biosciences · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autophagy is a degradation pathway in eukaryotic cells in which aging proteins and organelles are sequestered into double-membrane vesicles, termed autophagosomes, which fuse with vacuoles to hydrolyze cargo. The key step in autophagy is the formation of autophagosomes, which requires different kinds of vesicles, including COPII vesicles and Atg9-containing vesicles, to transport lipid double-membranes to the phagophore assembly site (PAS). In yeast, the cis-Golgi localized t-SNARE protein Sed5 plays a role in endoplasmic reticulum (ER)-Golgi and intra-Golgi vesicular transport. We report that during autophagy, sed5-1 mutant cells could not properly transport Atg8 to the PAS, resulting in multiple Atg8 dots being dispersed into the cytoplasm. Some dots were trapped in the Golgi apparatus. Sed5 regulates the antero-grade trafficking of Atg9-containing vesicles to the PAS by participating in the localization of Atg23 and Atg27 to the Golgi apparatus. Furthermore, we found that overexpression of SFT1 or SFT2 (suppressor of sed5 ts) rescued the autophagy defects in sed5-1 mutant cells. Our data suggest that Sed5 plays a novel role in autophagy, by regulating the formation of Atg9-containing vesicles in the Golgi apparatus, and the genetic interaction between Sft1/2 and Sed5 is essential for autophagy.
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