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Autophagy. 2017 Jun 3;13(6):1086-1087. doi: 10.1080/15548627.2017.1307487. Epub 2017 Apr 3.

Galectins and TRIMs directly interact and orchestrate autophagic response to endomembrane damage.

Author information

1
a Department of Molecular Genetics and Microbiology , University of New Mexico Health Sciences Center , Northeast , Albuquerque , NM , USA.
2
b Molecular Cancer Research Group , Institute of Medical Biology, University of Tromsø - The Arctic University of Norway , Tromsø , Norway.

Abstract

Macroautophagy/autophagy is a homeostatic process delivering cytoplasmic targets, including damaged organelles, to lysosomes for degradation; however, it is not completely understood how compromised endomembranes are recognized by the autophagic apparatus. We have described previously that the TRIM family of proteins act as receptors for selective autophagy. In this study we uncovered the property of TRIMs to directly interact with members of the family of cytosolic lectins termed galectins. Galectins patrol the cytoplasm and recognize compromised membranes. We show that TRIM16 uses LGALS3 (galectin 3) to detect damaged lysosomes and phagosomes. TRIM16 assembles the core autophagic machinery and is found in protein complexes with MTOR and TFEB, thus regulating their activity to set in motion endomembrane quality control. The TRIM16-LGALS3 system plays a key role in autophagic homeostasis of lysosomes and in the control of Mycobacterium tuberculosis in vivo.

KEYWORDS:

TFEB; TOR; lysosome; phagosome; tuberculosis; ubiquitin E3 ligase

PMID:
28368693
PMCID:
PMC5486367
DOI:
10.1080/15548627.2017.1307487
[Indexed for MEDLINE]
Free PMC Article

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