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Trends Cell Biol. 2016 Jan;26(1):6-16. doi: 10.1016/j.tcb.2015.08.010. Epub 2015 Oct 1.

Ubiquitin-Dependent And Independent Signals In Selective Autophagy.

Author information

1
Institute of Biochemistry II, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany; Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Straße 15, 60438 Frankfurt am Main, Germany.
2
Institute of Pathobiochemistry, University Medical Center, Johannes Gutenberg University, Mainz, Germany.
3
Institute of Biochemistry II, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany; Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Straße 15, 60438 Frankfurt am Main, Germany. Electronic address: ivan.dikic@biochem2.de.

Abstract

Selective autophagy regulates the abundance of specific cellular components via a specialized arsenal of factors, termed autophagy receptors, that target protein complexes, aggregates, and whole organelles into lysosomes. Autophagy receptors bind to LC3/GABARAP proteins on phagophore and autophagosome membranes, and recognize signals on cargoes to deliver them to autophagy. Ubiquitin (Ub), a well-known signal for the degradation of polypeptides in the proteasome, also plays an important role in the recognition of cargoes destined for selective autophagy. In addition, a variety of cargoes are committed to selective autophagy pathways by Ub-independent mechanisms employing protein-protein interaction motifs, Ub-like modifiers, and sugar- or lipid-based signals. In this article we summarize Ub-dependent and independent selective autophagy pathways, and discuss regulatory mechanisms and challenges for future studies.

KEYWORDS:

LC3; UBL; autophagosome; autophagy receptor; disease.; post-translational modification

PMID:
26437584
DOI:
10.1016/j.tcb.2015.08.010
[Indexed for MEDLINE]

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