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Atg8-Family Proteins—Structural Features and Molecular Interactions in Autophagy and Beyond

by Nicole Wesch 1,†, Vladimir Kirkin 2,† and Vladimir V. Rogov 1,3,4,*
1
Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe-University Frankfurt, 60438 Frankfurt am Main, Germany
2
Cancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research London, Sutton SM2 5NG, UK
3
Structural Genomics Consortium, Buchmann Institute for Life Sciences, Goethe-University Frankfurt, 60438 Frankfurt am Main, Germany
4
Institute of Pharmaceutical Chemistry, Goethe-University Frankfurt, 60438 Frankfurt am Main, Germany
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Cells 2020, 9(9), 2008; https://doi.org/10.3390/cells9092008
Received: 8 August 2020 / Revised: 25 August 2020 / Accepted: 27 August 2020 / Published: 1 September 2020
(This article belongs to the Special Issue Ubiquitin and Autophagy)
Autophagy is a common name for a number of catabolic processes, which keep the cellular homeostasis by removing damaged and dysfunctional intracellular components. Impairment or misbalance of autophagy can lead to various diseases, such as neurodegeneration, infection diseases, and cancer. A central axis of autophagy is formed along the interactions of autophagy modifiers (Atg8-family proteins) with a variety of their cellular counter partners. Besides autophagy, Atg8-proteins participate in many other pathways, among which membrane trafficking and neuronal signaling are the most known. Despite the fact that autophagy modifiers are well-studied, as the small globular proteins show similarity to ubiquitin on a structural level, the mechanism of their interactions are still not completely understood. A thorough analysis and classification of all known mechanisms of Atg8-protein interactions could shed light on their functioning and connect the pathways involving Atg8-proteins. In this review, we present our views of the key features of the Atg8-proteins and describe the basic principles of their recognition and binding by interaction partners. We discuss affinity and selectivity of their interactions as well as provide perspectives for discovery of new Atg8-interacting proteins and therapeutic approaches to tackle major human diseases. View Full-Text
Keywords: Atg8; LC3; GABARAP; LIR motif; SAR; UBL; autophagy Atg8; LC3; GABARAP; LIR motif; SAR; UBL; autophagy
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Wesch, N.; Kirkin, V.; Rogov, V.V. Atg8-Family Proteins—Structural Features and Molecular Interactions in Autophagy and Beyond. Cells 2020, 9, 2008.

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