Evidence for ESCRT- and clathrin-dependent microautophagy
Autor: | Yoko Kagohashi, Takeshi Kondo, Masahide Oku, Yuichiro Maeda, Yasuyoshi Sakai, Mai Yamada, Toyoshi Fujimoto |
---|---|
Jazyk: | angličtina |
Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Endosome Saccharomyces cerevisiae Vacuole Clathrin Microbiology ESCRT Article 03 medical and health sciences Lipid droplet Autophagy Microautophagy Research Articles Organelles biology Endosomal Sorting Complexes Required for Transport Cell Biology biology.organism_classification Alkaline Phosphatase Transmembrane protein Cell biology 030104 developmental biology Metabolism biology.protein |
Zdroj: | The Journal of Cell Biology |
ISSN: | 0021-9525 |
Popis: | Microautophagy is a mode of autophagy in which the lysosomal or vacuolar membrane invaginates and engulfs target components. Oku et al. show that, upon a diauxic shift, yeast microautophagy involves recruitment of ESCRT proteins to the vacuolar membrane, including clathrin-interacting Vps27, and uptake of lipid droplets by the vacuole. Microautophagy refers to a mode of autophagy in which the lysosomal or vacuolar membrane invaginates and directly engulfs target components. The molecular machinery of membrane dynamics driving microautophagy is still elusive. Using immunochemical monitoring of yeast vacuolar transmembrane proteins, Vph1 and Pho8, fused to fluorescent proteins, we obtained evidence showing an induction of microautophagy after a diauxic shift in the yeast Saccharomyces cerevisiae. Components of the endosomal sorting complex required for transport machinery were found to be required for this process, and the gateway protein of the machinery, Vps27, was observed to change its localization onto the vacuolar membrane after a diauxic shift. We revealed the functional importance of Vps27’s interaction with clathrin in this microautophagy that also contributed to uptake of lipid droplets into the vacuole. This study sheds light on the molecular mechanism of microautophagy, which does not require the core Atg proteins. |
Databáze: | OpenAIRE |
Externí odkaz: |