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Repair or Lysophagy: Dealing with Damaged Lysosomes

Papadopoulos, Chrisovalantis, Kravic, Bojana, Meyer, Hemmo·2020·Journal of Molecular Biology
DOI 10.1016/j.jmb.2019.08.010
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Abstract

Lysosomal membrane permeabilization or full rupture of lysosomes is a common and severe stress condition that is relevant for degenerative disease, infection and cancer. If damage is limited, cells can repair lysosomes by means of the endosomal sorting complex required for transport (ESCRT) machinery. Presumably, if repair fails, lysosomes are tagged with ubiquitin to initiate clearance by selective macroautophagy, termed lysophagy. Accumulating evidence suggests damage-induced exposure of luminal glycans to the cytosol as the key trigger for ubiquitination. In this review, we discuss recent data on cellular damage sensing, the underlying ubiquitination and autophagy machinery as well as additional layers of regulation such as processing of ubiquitinated proteins by the AAA-ATPase VCP/p97. We conclude with thoughts on how these mechanisms may regulate decision making between lysosome repair and lysophagy.

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Metadata

Authors
Papadopoulos, C., Kravic, B., & Meyer, H.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2020-01
Volume
432
Issue
1
Pages
231-239
ISSN
0022-2836
DOI
10.1016/j.jmb.2019.08.010
Cited by
212
References
10
Language
en
Licence
Funders
Deutsche Forschungsgemeinschaft

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