Human apolipoprotein L1 interferes with mitochondrial function in Saccharomyces cerevisiae

Chidiac,Mounia; Daher,Jalil; Boeckstaens,Mélanie; Poelvoorde,Philippe; Badran,Bassam; Marini,Anna Maria; Khalaf,Roy; Vanhamme,Luc

doi:10.3892/mmr.2020.11271

Human apolipoprotein L1 interferes with mitochondrial function in Saccharomyces cerevisiae

Authors:
- Mounia Chidiac
- Jalil Daher
- Mélanie Boeckstaens
- Philippe Poelvoorde
- Bassam Badran
- Anna Maria Marini
- Roy Khalaf
- Luc Vanhamme
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Affiliations: Laboratory of Molecular Parasitology, Laboratory of Gene Molecular Biology, IBMM, Université Libre de Bruxelles, 6041 Gosselies, Belgium, Department of Biology, University of Balamand, P.O. Box 100, Tripoli, Lebanon, Laboratory of Membrane Transport Biology, IBMM, Faculty of Sciences, Université Libre de Bruxelles, 6041 Gosselies, Belgium, Department of Biochemistry, Laboratory of Immunology, Lebanese University, Faculty of Sciences, P.O. Box 6573, Hadath‑Beirut, Lebanon, Department of Natural Sciences, Lebanese American University, P.O. Box 36, Byblos, Lebanon
Published online on: June 24, 2020 https://doi.org/10.3892/mmr.2020.11271
Pages: 1910-1920
Copyright: © Chidiac et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

To the best of our knowledge, the vertebrate apolipoprotein L (APOL) family has not previously been ascribed to any definite pathophysiological function, although the conserved BH3 protein domain suggests a role in programmed cell death or an interference with mitochondrial processes. In the present study, the human APOL1 was expressed in the yeast Saccharomyces cerevisiae in order to determine the molecular action of APOL1. APOL1 inhibited cell proliferation in a non‑fermentable carbon source, such as glycerol, while it had no effect on proliferation in fermentable carbon sources, such as galactose. APOL1, expressed in yeast, is localized in the mitochondrial fraction, as determined via western blotting. APOL1 induced a loss of mitochondrial function, demonstrated by a loss of respiratory index, and mitochondrial membrane potential. Green fluorescent protein tagging of mitochondrial protein revealed that APOL1 was associated with abnormal mitochondrial and lysosomal morphologies, observed by a loss of the normal mitochondrial tubular network. Thus, the results of the present study suggest that APOL1 could be a physiological regulator of mitochondrial function.

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