Methods for Monitoring Autophagy from Yeast to Human
By D. Klionsky, A. Cuervo, Per O. Seglen. Autophagy, 2007
696 citations recorded by the source corpus.
The increasing interest in autophagy in a wide range of organisms, accompanied by an ever-growing influx of researchers into this field, necessitates a good understanding of the methodologies available to monitor this process. In this review we discuss current approaches that can be used to follow the overall process of autophagy, as well as individual steps, from yeast to human. The majority of the review considers methods that apply to macroautophagy; however, we also consider alternative types of degradation including chaperone-mediated autophagy and microautophagy. This information is meant to provide a resource for newcomers as well as a stimulus for experienced researchers who may be prompted to develop additional assays to examine autophagy-related pathways.
Subfields: Cell Biology, Epidemiology, Pharmacology
View Paper: https://www.semanticscholar.org/paper/c8c4f755bdcbf14b7acd150c6a4e6b74097e35bc
How researchers see this paper
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In Cell Biology
- D. Klionsky
- N. Mizushima
- I. Slaninová
- Beth Levine
- V. Deretic
- A. Cuervo
- Guido Kroemer
- Alec C. Kimmelman
In Epidemiology
- N. Mizushima
- D. Klionsky
- Beth Levine
- I. Slaninová
- Guido Kroemer
- V. Deretic
- Alec C. Kimmelman
- A. Cuervo
In Pharmacology
- Guido Kroemer
- N. Mizushima
- Beth Levine
- Alec C. Kimmelman
- I. Slaninová
- D. Klionsky
- Ralph A. Nixon
- M. Komatsu
Citations in the corpus
- Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes (2008, background): “91,92 However, transcriptional upregulation of Drosophila melanogaster Atg8a and Atg8b is observed in fat bodies following induction of autophagy at the end of larval development,93 and an increase in Drosophila melanogaster Atg8b is observed in cultured Drosophila melanogaster l(2)mbn cells followi”
- Autophagy: process and function. (2007, background): “Since the function of these Atg proteins has been extensively reviewed (Klionsky 2005; Klionsky et al. 2007; Suzuki and Ohsumi 2007), only some topics are highlighted here.”
- Monitoring and Measuring Autophagy (2017, background): “Released isotope-labeled amino acids can be detected in the supernatant after protein precipitation by trichloroacetic acid [10].”
- Guidelines for the use and interpretation of assays for monitoring autophagy (2012, background): “The labeling can be done with relative ease both in cultured cells, and in live animals.(3) In cells, it is also possible to measure the release of an unlabeled amino acid by chromatographic methods, thereby obviating the need for prelabeling;(490) however, it is important to keep in mind that amino”
- Autophagy mediates the mitotic senescence transition. (2009, background): “This evolutionarily conserved process is characterized by the formation of doublemembrane cytosolic vesicles, autophagosomes, which sequester cytoplasmic content and deliver it to lysosomes (Ohsumi 2001; Klionsky et al. 2007; Mizushima et al. 2008).”
- Atg8 controls phagophore expansion during autophagosome formation. (2008, background): “Although Atg8 has been widely used as a marker for recognition of autophagosomes (Klionsky et al., 2007), its exact in vivo function is still not clear.”
- Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (2012, positive): “The labeling can be done with relative ease both in cultured cells and in live animals.(3) In cells, it is also possible to measure the release of an unlabeled amino acid by chromatographic methods, thereby obviating the need for prelabeling;(678) however, it is important to keep in mind that amino ”
- Protein turnover via autophagy: implications for metabolism. (2007, methodology): “Sequestration assays include the lysosomal uptake of raffinose or long-lived enzymes such as lactate dehydrogenase (measured in the presence of a lysosomal protease inhibitor) (47).”