Jump to Navigation

iLIR database: A web resource for LIR motif-containing proteins in eukaryotes.

TitleiLIR database: A web resource for LIR motif-containing proteins in eukaryotes.
Publication TypeJournal Article
Year of Publication2016
AuthorsJacomin, Anne-Claire, Siva Samavedam, V. J. Promponas, and Ioannis P. Nezis
Date Published2016 10 02
KeywordsAmino Acid Motifs, Amino Acid Sequence, Animals, Autophagy, Data Mining, Databases as Topic, Eukaryota, Gene Ontology, Humans, Internet, Mammals, Models, Biological, Proteome

Atg8-family proteins are the best-studied proteins of the core autophagic machinery. They are essential for the elongation and closure of the phagophore into a proper autophagosome. Moreover, Atg8-family proteins are associated with the phagophore from the initiation of the autophagic process to, or just prior to, the fusion between autophagosomes with lysosomes. In addition to their implication in autophagosome biogenesis, they are crucial for selective autophagy through their ability to interact with selective autophagy receptor proteins necessary for the specific targeting of substrates for autophagic degradation. In the past few years it has been revealed that Atg8-interacting proteins include not only receptors but also components of the core autophagic machinery, proteins associated with vesicles and their transport, and specific proteins that are selectively degraded by autophagy. Atg8-interacting proteins contain a short linear LC3-interacting region/LC3 recognition sequence/Atg8-interacting motif (LIR/LRS/AIM) motif which is responsible for their interaction with Atg8-family proteins. These proteins are referred to as LIR-containing proteins (LIRCPs). So far, many experimental efforts have been carried out to identify new LIRCPs, leading to the characterization of some of them in the past 10 years. Given the need for the identification of LIRCPs in various organisms, we developed the iLIR database ( https://ilir.warwick.ac.uk ) as a freely available web resource, listing all the putative canonical LIRCPs identified in silico in the proteomes of 8 model organisms using the iLIR server, combined with a Gene Ontology (GO) term analysis. Additionally, a curated text-mining analysis of the literature permitted us to identify novel putative LICRPs in mammals that have not previously been associated with autophagy.

Alternate JournalAutophagy

by Dr. Radut.