Atg8 family proteins, LIR/AIM motifs and other interaction modes
The Atg8 family of ubiquitin-like proteins play pivotal roles in autophagy and other processes involving vesicle fusion and transport where the lysosome/vacuole is the end station. Nuclear roles of Atg8 proteins are also emerging. Here, we review the structural and functional features of Atg8 family...
| Main Authors: | , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2023-12-01
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| Series: | Autophagy Reports |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/27694127.2023.2188523 |
| _version_ | 1797685742240006144 |
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| author | Vladimir V. Rogov Ioannis P. Nezis Panagiotis Tsapras Hong Zhang Yasin Dagdas Nobuo N. Noda Hitoshi Nakatogawa Martina Wirth Stephane Mouilleron David G. McEwan Christian Behrends Vojo Deretic Zvulun Elazar Sharon A. Tooze Ivan Dikic Trond Lamark Terje Johansen |
| author_facet | Vladimir V. Rogov Ioannis P. Nezis Panagiotis Tsapras Hong Zhang Yasin Dagdas Nobuo N. Noda Hitoshi Nakatogawa Martina Wirth Stephane Mouilleron David G. McEwan Christian Behrends Vojo Deretic Zvulun Elazar Sharon A. Tooze Ivan Dikic Trond Lamark Terje Johansen |
| author_sort | Vladimir V. Rogov |
| collection | DOAJ |
| description | The Atg8 family of ubiquitin-like proteins play pivotal roles in autophagy and other processes involving vesicle fusion and transport where the lysosome/vacuole is the end station. Nuclear roles of Atg8 proteins are also emerging. Here, we review the structural and functional features of Atg8 family proteins and their protein-protein interaction modes in model organisms such as yeast, Arabidopsis, C. elegans and Drosophila to humans. Although varying in number of homologs, from one in yeast to seven in humans, and more than ten in some plants, there is a strong evolutionary conservation of structural features and interaction modes. The most prominent interaction mode is between the LC3 interacting region (LIR), also called Atg8 interacting motif (AIM), binding to the LIR docking site (LDS) in Atg8 homologs. There are variants of these motifs like “half-LIRs” and helical LIRs. We discuss details of the binding modes and how selectivity is achieved as well as the role of multivalent LIR-LDS interactions in selective autophagy. A number of LIR-LDS interactions are known to be regulated by phosphorylation. New methods to predict LIR motifs in proteins have emerged that will aid in discovery and analyses. There are also other interaction surfaces than the LDS becoming known where we presently lack detailed structural information, like the N-terminal arm region and the UIM-docking site (UDS). More interaction modes are likely to be discovered in future studies. |
| first_indexed | 2024-03-12T00:55:44Z |
| format | Article |
| id | doaj.art-efb1c686968d4bd0982e2069b219cc78 |
| institution | Directory Open Access Journal |
| issn | 2769-4127 |
| language | English |
| last_indexed | 2024-03-12T00:55:44Z |
| publishDate | 2023-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Autophagy Reports |
| spelling | doaj.art-efb1c686968d4bd0982e2069b219cc782023-09-14T13:24:41ZengTaylor & Francis GroupAutophagy Reports2769-41272023-12-012110.1080/27694127.2023.21885232188523Atg8 family proteins, LIR/AIM motifs and other interaction modesVladimir V. Rogov0Ioannis P. Nezis1Panagiotis Tsapras2Hong Zhang3Yasin Dagdas4Nobuo N. Noda5Hitoshi Nakatogawa6Martina Wirth7Stephane Mouilleron8David G. McEwan9Christian Behrends10Vojo Deretic11Zvulun Elazar12Sharon A. Tooze13Ivan Dikic14Trond Lamark15Terje Johansen16Chemistry and Pharmacy, Goethe University, 60438 Frankfurt, am Main, and Structural Genomics Consortium, Buchmann Institute for Molecular Life Sciences, Goethe UniversitySchool of Life Sciences, University of WarwickSchool of Life Sciences, University of WarwickNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China and College of Life Sciences, University of Chinese Academy of SciencesGregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenterInstitute for Genetic Medicine, Hokkaido UniversitySchool of Life Science and Technology, Tokyo Institute of TechnologyMolecular Cell Biology of Autophagy, The Francis Crick InstituteStructural Biology Science Technology Platform, The Francis Crick InstituteCancer Research UK Beatson InstituteMunich Cluster of Systems Neurology, Ludwig-Maximilians-Universität MünchenUniversity of New Mexico Health Sciences CenterThe Weizmann Institute of ScienceMolecular Cell Biology of Autophagy, The Francis Crick InstituteGoethe-University, Frankfurt am Main, and Buchmann Institute for Molecular Life SciencesUniversity of Tromsø - The Arctic University of NorwayUniversity of Tromsø - The Arctic University of NorwayThe Atg8 family of ubiquitin-like proteins play pivotal roles in autophagy and other processes involving vesicle fusion and transport where the lysosome/vacuole is the end station. Nuclear roles of Atg8 proteins are also emerging. Here, we review the structural and functional features of Atg8 family proteins and their protein-protein interaction modes in model organisms such as yeast, Arabidopsis, C. elegans and Drosophila to humans. Although varying in number of homologs, from one in yeast to seven in humans, and more than ten in some plants, there is a strong evolutionary conservation of structural features and interaction modes. The most prominent interaction mode is between the LC3 interacting region (LIR), also called Atg8 interacting motif (AIM), binding to the LIR docking site (LDS) in Atg8 homologs. There are variants of these motifs like “half-LIRs” and helical LIRs. We discuss details of the binding modes and how selectivity is achieved as well as the role of multivalent LIR-LDS interactions in selective autophagy. A number of LIR-LDS interactions are known to be regulated by phosphorylation. New methods to predict LIR motifs in proteins have emerged that will aid in discovery and analyses. There are also other interaction surfaces than the LDS becoming known where we presently lack detailed structural information, like the N-terminal arm region and the UIM-docking site (UDS). More interaction modes are likely to be discovered in future studies.http://dx.doi.org/10.1080/27694127.2023.2188523autophagyatg8aimlirldsudsprotein-protein interactionphosphorylation |
| spellingShingle | Vladimir V. Rogov Ioannis P. Nezis Panagiotis Tsapras Hong Zhang Yasin Dagdas Nobuo N. Noda Hitoshi Nakatogawa Martina Wirth Stephane Mouilleron David G. McEwan Christian Behrends Vojo Deretic Zvulun Elazar Sharon A. Tooze Ivan Dikic Trond Lamark Terje Johansen Atg8 family proteins, LIR/AIM motifs and other interaction modes Autophagy Reports autophagy atg8 aim lir lds uds protein-protein interaction phosphorylation |
| title | Atg8 family proteins, LIR/AIM motifs and other interaction modes |
| title_full | Atg8 family proteins, LIR/AIM motifs and other interaction modes |
| title_fullStr | Atg8 family proteins, LIR/AIM motifs and other interaction modes |
| title_full_unstemmed | Atg8 family proteins, LIR/AIM motifs and other interaction modes |
| title_short | Atg8 family proteins, LIR/AIM motifs and other interaction modes |
| title_sort | atg8 family proteins lir aim motifs and other interaction modes |
| topic | autophagy atg8 aim lir lds uds protein-protein interaction phosphorylation |
| url | http://dx.doi.org/10.1080/27694127.2023.2188523 |
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