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dc.contributor.authorRogov, Vladimir V.
dc.contributor.authorNezis, Ioannis P.
dc.contributor.authorTsapras, P
dc.contributor.authorZhang, Hong
dc.contributor.authorDagdas, Yasin
dc.contributor.authorNoda, Nobuo N
dc.contributor.authorNakatogawa, Hitoshi
dc.contributor.authorWirth, Martina
dc.contributor.authorMouilleron, Stephane
dc.contributor.authorMcEwan, David G.
dc.contributor.authorBehrends, Christian
dc.contributor.authorDeretic, Vojo P.
dc.contributor.authorElazar, Zvulun
dc.contributor.authorTooze, Sharon A.
dc.contributor.authorDikic, Ivan
dc.contributor.authorLamark, Trond
dc.contributor.authorJohansen, Terje
dc.date.accessioned2024-03-19T10:09:07Z
dc.date.available2024-03-19T10:09:07Z
dc.date.issued2023-03-19
dc.description.abstractThe 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.en_US
dc.identifier.citationRogov VV, Nezis IP, Tsapras, Zhang H, Dagdas Y, Noda, Nakatogawa H, Wirth M, Mouilleron S, McEwan DG, Behrends C, Deretic, Elazar Z, Tooze SA, Dikic I, Lamark T, Johansen T. Atg8 family proteins, LIR/AIM motifs and other interaction modes. Autophagy Reports. 2023;2(1)en_US
dc.identifier.cristinIDFRIDAID 2255489
dc.identifier.doi10.1080/27694127.2023.2188523
dc.identifier.issn2769-4127
dc.identifier.urihttps://hdl.handle.net/10037/33180
dc.language.isoengen_US
dc.publisherTaylor & Francisen_US
dc.relation.journalAutophagy Reports
dc.relation.projectIDinfo:eu-repo/grantAgreement/EC/H2020/875510/Germany/EUbOPEN: Enabling and Unlocking biology in the OPEN/EUbOPEN/en_US
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2023 The Author(s)en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.rightsAttribution 4.0 International (CC BY 4.0)en_US
dc.titleAtg8 family proteins, LIR/AIM motifs and other interaction modesen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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Attribution 4.0 International (CC BY 4.0)
Med mindre det står noe annet, er denne innførselens lisens beskrevet som Attribution 4.0 International (CC BY 4.0)