Annexin A7 mediates lysosome repair independently of ESCRT-III.

Autor:	Ebstrup ML; Membrane Integrity, Danish Cancer Institute, Copenhagen, Denmark., Sønder SL; Membrane Integrity, Danish Cancer Institute, Copenhagen, Denmark., Fogde DL; Cell Death and Metabolism, Danish Cancer Institute, Copenhagen, Denmark., Heitmann ASB; Membrane Integrity, Danish Cancer Institute, Copenhagen, Denmark., Dietrich TN; Bioimaging Core Facility, Danish Cancer Institute, Copenhagen, Denmark., Dias C; Membrane Integrity, Danish Cancer Institute, Copenhagen, Denmark., Jäättelä M; Cell Death and Metabolism, Danish Cancer Institute, Copenhagen, Denmark.; Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark., Maeda K; Cell Death and Metabolism, Danish Cancer Institute, Copenhagen, Denmark., Nylandsted J; Membrane Integrity, Danish Cancer Institute, Copenhagen, Denmark.; Department of Molecular Medicine, University of Southern Denmark, Odense, Denmark.
Jazyk:	angličtina
Zdroj:	Frontiers in cell and developmental biology [Front Cell Dev Biol] 2024 Jan 23; Vol. 11, pp. 1211498. Date of Electronic Publication: 2024 Jan 23 (Print Publication: 2023).
DOI:	10.3389/fcell.2023.1211498
Abstrakt:	Lysosomes are crucial organelles essential for various cellular processes, and any damage to them can severely compromise cell viability. This study uncovers a previously unrecognized function of the calcium- and phospholipid-binding protein Annexin A7 in lysosome repair, which operates independently of the Endosomal Sorting Complex Required for Transport (ESCRT) machinery. Our research reveals that Annexin A7 plays a role in repairing damaged lysosomes, different from its role in repairing the plasma membrane, where it facilitates repair through the recruitment of ESCRT-III components. Notably, our findings strongly suggest that Annexin A7, like the ESCRT machinery, is dispensable for membrane contact site formation within the newly discovered phosphoinositide-initiated membrane tethering and lipid transport (PITT) pathway. Instead, we speculate that Annexin A7 is recruited to damaged lysosomes and promotes repair through its membrane curvature and cross-linking capabilities. Our findings provide new insights into the diverse mechanisms underlying lysosomal membrane repair and highlight the multifunctional role of Annexin A7 in membrane repair. Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. (Copyright © 2024 Ebstrup, Sønder, Fogde, Heitmann, Dietrich, Dias, Jäättelä, Maeda and Nylandsted.)
Databáze:	MEDLINE
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