Bioinformatic and image analyses of the cellular localization of the apoptotic proteins endonuclease G, AIF, and AMID during apoptosis in human cells
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Apoptosis physiology MeSH
- Cell Nucleus metabolism MeSH
- Cell Line MeSH
- Endodeoxyribonucleases isolation & purification metabolism MeSH
- Apoptosis Inducing Factor isolation & purification metabolism MeSH
- Microscopy, Fluorescence MeSH
- Golgi Apparatus metabolism MeSH
- Intracellular Membranes metabolism MeSH
- Humans MeSH
- Lysosomes metabolism MeSH
- Mitochondrial Proteins isolation & purification metabolism MeSH
- Mitochondria metabolism MeSH
- Apoptosis Regulatory Proteins isolation & purification metabolism MeSH
- Recombinant Fusion Proteins metabolism MeSH
- Computational Biology * MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- AIFM1 protein, human MeSH Browser
- Endodeoxyribonucleases MeSH
- endonuclease G MeSH Browser
- Apoptosis Inducing Factor MeSH
- ferroptosis suppressor protein 1, human MeSH Browser
- Mitochondrial Proteins MeSH
- Apoptosis Regulatory Proteins MeSH
- Recombinant Fusion Proteins MeSH
We studied the cellular localization of the apoptotic proteins endonuclease G, AIF, and AMID in silico using three prediction tools and in living cells using both single-cell colocalization image analysis and nuclear translocation analysis. We confirmed the mitochondrial localization of endonuclease G and AIF by prediction analysis and by single-cell colocalization image analysis. We found the AMID protein to be cytoplasmic, most probably incorporated into the cytoplasmic side of the membranes of various organelles. The highest concentration of AMID was observed associated with the Golgi. Colocalization of AMID with lysosomes was also indirectly confirmed by analysis of AMID-rich vesicle velocity using manual tracking analysis. Bioinformatic analysis also detected nuclear localization signals in endonuclease G and AIF, but not in AMID. A novel analysis of time-lapse fluorescence image data during staurosporine-induced apoptosis revealed nuclear translocation only for endonuclease G and AIF.
References provided by Crossref.org
Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis
Prediction of localization and interactions of apoptotic proteins
