Ubiquitin-Dependent And Independent Signals In Selective Autophagy

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• 作者：Aliaksandr Khaminets¹ ; ³ ; Christian Behl² ; Ivan Dikic¹ ; ³ ; ^{ivan.dikic@biochem2.de" class="auth_mail" title="E-mail the corresponding author}
• 关键词：autophagosome ; autophagy receptor ; LC3 ; UBL ; post-translational modification ; disease.
• 刊名：Trends in Cell Biology
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：26
• 期：1
• 页码：6-16
• 全文大小：1596 K

文摘

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.