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USP32 regulates late endosomal transport and recycling through deubiquitylation of Rab7
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10.1038.s41467-019-09437-x.pdf
Date
2019-03-29
Author
Sapmaz, Aysegul
Berlin, Ilana
Bos, Erik
Wijdeven, Ruud H.
Janssen, Hans
Konietzny, Rebecca
Akkermans, Jimmy J.
Erson Bensan, Ayşe Elif
Koning, Roman
Kessler, Benedikt M.
Neefjes, Jacques
Ovaa, Huib
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Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
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The endosomal system is a highly dynamic multifunctional organelle, whose complexity is regulated in part by reversible ubiquitylation. Despite the wide-ranging influence of ubiquitin in endosomal processes, relatively few enzymes utilizing ubiquitin have been described to control endosome integrity and function. Here we reveal the deubiquitylating enzyme (DUB) ubiquitin-specific protease 32 (USP32) as a powerful player in this context. Loss of USP32 inhibits late endosome (LE) transport and recycling of LE cargos, resulting in dispersion and swelling of the late compartment. Using SILAC-based ubiquitome profiling we identify the small GTPase Rab7-the logistical centerpiece of LE biology-as a substrate of USP32. Mechanistic studies reveal that LE transport effector RILP prefers ubiquitylation-deficient Rab7, while retromer-mediated LE recycling benefits from an intact cycle of Rab7 ubiquity-lation. Collectively, our observations suggest that reversible ubiquitylation helps switch Rab7 between its various functions, thereby maintaining global spatiotemporal order in the endosomal system.
Subject Keywords
General Biochemistry, Genetics and Molecular Biology
,
General Physics and Astronomy
,
General Chemistry
URI
https://hdl.handle.net/11511/40211
Journal
NATURE COMMUNICATIONS
DOI
https://doi.org/10.1038/s41467-019-09437-x
Collections
Department of Biology, Article
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A. Sapmaz et al., “USP32 regulates late endosomal transport and recycling through deubiquitylation of Rab7,”
NATURE COMMUNICATIONS
, pp. 0–0, 2019, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/40211.