ArticleMethods in enzymology2017
Assays to Monitor Pexophagy in Yeast.
Article in Methods in enzymology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- A subcellular proteome atlas of the yeast Komagataella phaffii.FEMS yeast research · 2020Article
- Chemical Biology Strategies to Study Autophagy.Frontiers in cell and developmental biology · 2018Review
- TRIM37, a novel E3 ligase for PEX5-mediated peroxisomal matrix protein import.The Journal of cell biology · 2017Article
- Role of PEX5 ubiquitination in maintaining peroxisome dynamics and homeostasis.Cell cycle (Georgetown, Tex.) · 2017Review
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Pexophagy is a selective autophagy process that degrades damaged and/or superfluous peroxisomes in the yeast vacuole or in mammalian lysosomes. The molecular mechanisms of pexophagy are well studied in yeast. Peroxisomes can be rapidly induced by oleate in the budding yeast, Saccharomyces cerevisiae, and by oleate or methanol in the methylotrophic yeast, Pichia pastoris. A number of peroxisomal matrix enzymes, such as 3-ketoacyl CoA thiolase (thiolase) and alcohol oxidase (AOX), are upregulated correspondingly to meet metabolic demands of the cells. Removal of these peroxisome-inducing carbon sources creates conditions wherein peroxisomes are superfluous and results in pexophagy and the degradation of these peroxisomal matrix enzymes. In this chapter, we discuss different assays to monitor pexophagy in yeast. These assays rely on tracking the localization of the BFP-SKL protein (a peroxisomally targeted version of the blue fluorescent protein) by microscopy, biochemical analysis of the degradation of peroxisomal matrix proteins, thiolase and AOX, and/or measuring the reduction of AOX activity during pexophagy.
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