Issue 7, 2014

Peroxisomes are juxtaposed to strategic sites on mitochondria

Abstract

Peroxisomes are ubiquitous and dynamic organelles that house many important pathways of cellular metabolism. In recent years it has been demonstrated that mitochondria are tightly connected with peroxisomes and are defective in several peroxisomal diseases. Indeed, these two organelles share metabolic routes as well as resident proteins and, at least in mammals, are connected via a vesicular transport pathway. However the exact extent of cross-talk between peroxisomes and mitochondria remains unclear. Here we used a combination of high throughput genetic manipulations of yeast libraries alongside high content screens to systematically unravel proteins that affect the transport of peroxisomal proteins and peroxisome biogenesis. Follow up work on the effector proteins that were identified revealed that peroxisomes are not randomly distributed in cells but are rather localized to specific mitochondrial subdomains such as mitochondria–ER junctions and sites of acetyl-CoA synthesis. Our approach highlights the intricate geography of the cell and suggests an additional layer of organization as a possible way to enable efficient metabolism. Our findings pave the way for further studying the machinery aligning mitochondria and peroxisomes, the role of the juxtaposition, as well as its regulation during various metabolic conditions. More broadly, the approaches used here can be easily applied to study any organelle of choice, facilitating the discovery of new aspects in cell biology.

Graphical abstract: Peroxisomes are juxtaposed to strategic sites on mitochondria

Supplementary files

Article information

Article type
Paper
Submitted
01 Jan 2014
Accepted
25 Mar 2014
First published
25 Mar 2014

Mol. BioSyst., 2014,10, 1742-1748

Author version available

Peroxisomes are juxtaposed to strategic sites on mitochondria

Y. Cohen, Y. A. Klug, L. Dimitrov, Z. Erez, S. G. Chuartzman, D. Elinger, I. Yofe, K. Soliman, J. Gärtner, S. Thoms, R. Schekman, Y. Elbaz-Alon, E. Zalckvar and M. Schuldiner, Mol. BioSyst., 2014, 10, 1742 DOI: 10.1039/C4MB00001C

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