Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers

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Item Type:	Article
Title:	Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers
Creators Name:	Neuspiel, M., Schauss, A.C., Braschi, E., Zunino, R., Rippstein, P., Rachubinski, R.A., Andrade-Navarro, M.A. and McBride, H.M.
Abstract:	Mitochondria and peroxisomes share a number of common biochemical processes, including the beta oxidation of fatty acids and the scavenging of peroxides. Here, we identify a new outer-membrane mitochondria-anchored protein ligase (MAPL) containing a really interesting new gene (RING)-finger domain. Overexpression of MAPL leads to mitochondrial fragmentation, indicating a regulatory function controlling mitochondrial morphology. In addition, confocal- and electron-microscopy studies of MAPL-YFP led to the observation that MAPL is also incorporated within unique, DRP1-independent, 70-100 nm diameter mitochondria-derived vesicles (MDVs). Importantly, vesicles containing MAPL exclude another outer-membrane marker, TOM20, and vesicles containing TOM20 exclude MAPL, indicating that MDVs selectively incorporate their cargo. We further demonstrate that MAPL-containing vesicles fuse with a subset of peroxisomes, marking the first evidence for a direct relationship between these two functionally related organelles. In contrast, a distinct vesicle population labeled with TOM20 does not fuse with peroxisomes, indicating that the incorporation of specific cargo is a primary determinant of MDV fate. These data are the first to identify MAPL, describe and characterize MDVs, and define a new intracellular transport route between mitochondria and peroxisomes.
Keywords:	Cellbio, Proteins, Animals, Monkeys
Source:	Current Biology
ISSN:	0960-9822
Publisher:	Cell Press
Volume:	18
Number:	2
Page Range:	102-108
Date:	22 January 2008
Official Publication:	https://doi.org/10.1016/j.cub.2007.12.038
PubMed:	View item in PubMed

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