CoChat
Sign Up
Cited by 7

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Methods for Studying Mitophagy in Yeast

Kolitsida, Panagiota, Abeliovich, Hagai·2019·Methods in Molecular Biology
DOI 10.1007/978-1-4939-8873-0_44
Open this paper in CoChat — free account

Abstract

Under some experimental conditions, eukaryotic cells, from yeast to man, will digest a portion of their mitochondrial cohort through an autophagic process termed mitophagy. In humans, defects in mitophagy have been proposed to play a causative role in a number of late-onset degenerative diseases such as Parkinson's disease and type II diabetes. As a consequence the study of mitophagy, as a quality control process in eukaryotic cells, has become an increasingly important focus in contemporary cell biology. When faced with the task of assaying mitophagy in yeast, the experimentalist has at his or her disposal a variety of induction conditions and assay systems to choose from. Here, we survey several well-established protocols for inducing and monitoring mitophagy in the yeast Saccharomyces cerevisiae and discuss their relative merits, limitations, and potential pitfalls.

Overview

Integrity signals

Registry

Crossref · 10.1007/978-1-4939-8873-0_44

Cites

5 of 5 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Flagged first, then by citations

Show all 5 references

Research works printed but not linked: 16

  1. Ashford TP, Porter KR (1962) Cytoplasmic components in hepatic cell lysosomes. J Cell Biol 12:198–202 · DOI
  2. Lemasters JJ (2005) Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res 8(1):3–5 · DOI
  3. Braell WA, Balch WE, Dobbertin DC, Rothman JE (1984) The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae. Cell 39(3 Pt 2):511–524 · DOI
  4. Okamoto K, Kondo-Okamoto N, Ohsumi Y (2009) Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev Cell 17(1):87–97 · DOI · Paper page
  5. Kanki T et al (2009) A genomic screen for yeast mutants defective in selective mitochondria autophagy. Mol Biol Cell 20(22):4730–4738 · DOI · Paper page
  6. De Deken RH (1966) The Crabtree effect: a regulatory system in yeast. J Gen Microbiol 44(2):149–156 · DOI
  7. Hagman A, Säll T, Piškur J (2014) Analysis of the yeast short-term Crabtree effect and its origin. FEBS J 281(21):4805–4814 · DOI
  8. Heo JM et al (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465–480 · DOI · Paper page
  9. Vida TA, Emr SD (1995) A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J Cell Biol 128(5):779–792 · DOI
  10. Kanki T, Kang D, Klionsky DJ (2009) Monitoring mitophagy in yeast: the Om45-GFP processing assay. Autophagy 5(8):1186–1189 · DOI
  11. Kissova I, Deffieu M, Manon S, Camougrand N (2004) Uth1p is involved in the autophagic degradation of mitochondria. J Biol Chem 279(37):39068–39074 · DOI
  12. Noda T, Matsuura A, Wada Y, Ohsumi Y (1995) Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun 210(1):126–132 · DOI
  13. Klionsky DJ, Emr SD (1990) A new class of lysosomal/vacuolar protein sorting signals. J Biol Chem 265(10):5349–5352 · DOI
  14. Abeliovich H, Zarei M, Rigbolt KT, Youle RJ, Dengjel J (2013) Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy. Nat Commun 4:2789 · DOI · Paper page
  15. Marangoni AG (2003) Enzyme kinetics: a modern approach. John Wiley & Sons, Hoboken, NJ
  16. Kaneko Y, Toh-e A, Banno I, Oshima Y (1989) Molecular characterization of a specific p-nitrophenylphosphatase gene, PHO13, and its mapping by chromosome fragmentation in Saccharomyces cerevisiae. Mol Gen Genet 220(1):133–139 · DOI

Cited by

Sorted by citations

See all 7

Metadata

Authors
Kolitsida, P., & Abeliovich, H.
Venue
Methods in Molecular Biology
Publisher
Springer New York
Published
2019
Pages
669-678
ISSN
  • 1064-3745
  • 1940-6029
DOI
10.1007/978-1-4939-8873-0_44
Cited by
7
References
5
Licence
www.springer.com/tdm (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review