Coupling of lysosomal and mitochondrial membrane permeabilization in trypanolysis by APOL1

Autor: Laurence Lecordier, Anneke Kremer, Isabel Roditi, Gabriela Schumann Burkard, Yoshiki Yamaryo-Botté, Kristoffer Klewe, Frédéric Fontaine, Derek P. Nolan, David Perez-Morga, Gilles Vanwalleghem, Joachim Rassow, Patricia Tebabi, Cyrille Y. Botté, Etienne Pays
Jazyk: angličtina
Rok vydání: 2015
Předmět:
Trypanosoma brucei rhodesiense
Programmed cell death
VACUOLES
Trypanosoma brucei gambiense
Trypanosoma brucei brucei
Protozoan Proteins
Kinesins
General Physics and Astronomy
Apoptosis
Vacuole
Mitochondrion
Trypanosoma brucei
Endocytosis
Permeability
Article
General Biochemistry
Genetics and Molecular Biology

PROGRAMMED CELL-DEATH
Lysosome
Medicine and Health Sciences
medicine
Humans
YEAST
Inner mitochondrial membrane
AFRICAN TRYPANOSOMES
Multidisciplinary
biology
Biological Transport
Intracellular Membranes
General Chemistry
FISSION
Apolipoprotein L1
biology.organism_classification
3. Good health
Cell biology
Apolipoproteins
medicine.anatomical_structure
BAX
ENDONUCLEASE-G
Mitochondrial Membranes
TRYPANOSOMA-BRUCEI
Kinesin
570 Life sciences
Biologie cellulaire
HUMAN SERUM
Lipoproteins
HDL

Lysosomes
RESISTANCE
Zdroj: Nature communications
Vanwalleghem, G; Fontaine, F; Lecordier, L; Tebabi, P; Klewe, K; Nolan, DP; Yamaryo-Botté, Y; Botté, C; Schumann-Burkard, Gabriela; Rassow, J; Roditi, Isabel; Perez-Morga, D; Pays, E (2015). Coupling of lysosomal and mitochondrial membrane permeabilization in trypanolysis by APOL1. Nature communications, 6(8078), p. 8078. Nature Publishing Group 10.1038/ncomms9078
Nature Communications
NATURE COMMUNICATIONS
ISSN: 2041-1723
Popis: Humans resist infection by the African parasite Trypanosoma brucei owing to the trypanolytic activity of the serum apolipoprotein L1 (APOL1). Following uptake by endocytosis in the parasite, APOL1 forms pores in endolysosomal membranes and triggers lysosome swelling. Here we show that APOL1 induces both lysosomal and mitochondrial membrane permeabilization (LMP and MMP). Trypanolysis coincides with MMP and consecutive release of the mitochondrial TbEndoG endonuclease to the nucleus. APOL1 is associated with the kinesin TbKIFC1, of which both the motor and vesicular trafficking VHS domains are required for MMP, but not for LMP. The presence of APOL1 in the mitochondrion is accompanied by mitochondrial membrane fenestration, which can be mimicked by knockdown of a mitochondrial mitofusin-like protein (TbMFNL). The BH3-like peptide of APOL1 is required for LMP, MMP and trypanolysis. Thus, trypanolysis by APOL1 is linked to apoptosis-like MMP occurring together with TbKIFC1-mediated transport of APOL1 from endolysosomal membranes to the mitochondrion.
SCOPUS: ar.j
info:eu-repo/semantics/published
Databáze: OpenAIRE