Atg9 sorting from mitochondria is impaired in early secretion and VFT-complex mutants in Saccharomyces cerevisiae
| Autor: | Daniel J. Klionsky, Fulvio Reggiori |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Carrier Proteins/genetics
Saccharomyces cerevisiae Proteins Mutation/genetics Saccharomyces cerevisiae/cytology Qa-SNARE Proteins/genetics Autophagy-Related Proteins Saccharomyces cerevisiae Biology CVT pathway Models Biological Article Lysosome Mitochondria/metabolism medicine Guanine Nucleotide Exchange Factors CVT vesicle Pre-autophagosomal structure Cytoplasm-to-vacuole targeting Membrane Glycoproteins Qa-SNARE Proteins Autophagy Membrane Proteins Cell Biology Membrane Glycoproteins/genetics Actins Mitochondria Transport protein Cell biology Protein Transport medicine.anatomical_structure Biochemistry Actins/metabolism Biosynthetic process Mutation Saccharomyces cerevisiae Proteins/genetics Membrane Proteins/metabolism Carrier Proteins |
| Zdroj: | Reggiori, F & Klionsky, D J 2006, ' Atg9 sorting from mitochondria is impaired in early secretion and VFT-complex mutants in Saccharomyces cerevisiae ', Journal of Cell Science, vol. 119, no. Pt 14, pp. 2903-11 . https://doi.org/10.1242/jcs.03047 |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | In eukaryotic cells, the turnover of long-lived proteins and large cytoplasmic structures is mediated by autophagy. Components that have to be eliminated are sequestered into double-membrane vesicles called autophagosomes and delivered into the lysosome or vacuole where they are destroyed by resident hydrolases. The integral membrane protein Atg9 is essential for both autophagy and the cytoplasm-to-vacuole targeting pathway, a selective biosynthetic process in Saccharomyces cerevisiae that is mechanistically and morphologically similar to autophagy. Atg9 cycles between the pre-autophagosomal structure, the putative site of double-membrane vesicle biogenesis and mitochondria. To understand the function of Atg9, and also its trafficking mode between these two locations, we identified mutants that affect specific Atg9 transport steps. We recently reported that five Atg proteins and phosphatidylinositol-3-phosphate regulate Atg9 recycling from the pre-autophagosomal structure. Here, we describe a different category of mutants that blocks Atg9 sorting from mitochondria. All mutants have been previously shown to be required for the normal progression of both the Cvt pathway and autophagy, but their precise role in these transport routes was unknown. |
| Databáze: | OpenAIRE |
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