6533b7dbfe1ef96bd127164c

RESEARCH PRODUCT

Ubiquitin-Dependent And Independent Signals In Selective Autophagy.

Christian BehlAliaksandr KhaminetsIvan Dikic

subject

0301 basic medicineAutophagosomebiologyUbiquitinGABARAPAutophagyUbiquitinationCell BiologyBAG3BioinformaticsCell biology03 medical and health sciences030104 developmental biologyProteasomeUbiquitinProteolysisbiology.proteinAutophagyAnimalsHumansTarget proteinATG16L1Signal Transduction

description

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.

10.1016/j.tcb.2015.08.010https://pubmed.ncbi.nlm.nih.gov/26437584