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A short isoform of ATG7 fails to lipidate LC3/GABARAP

A short isoform of ATG7 fails to lipidate LC3/GABARAP

Title: A short isoform of ATG7 fails to lipidate LC3/GABARAP
Author: Ogmundsdottir, Margret H
Fock, Valerie   orcid.org/0000-0002-7812-4340
Sooman, L.
Pogenberg, V.
Dilshat, R.
Bindesbøll, C.
Ögmundsdóttir, Helga M.
Simonsen, A.
Wilmanns, M.
Steingrimsson, Eirikur   orcid.org/0000-0001-5826-7486
Date: 2018-09-26
Language: English
Scope: 14391
University/Institute: Háskóli Íslands
University of Iceland
School: Heilbrigðisvísindasvið (HÍ)
School of Health Sciences (UI)
Department: Læknadeild (HÍ)
Faculty of Medicine (UI)
Lífvísindasetur (HÍ)
Biomedical Center (UI)
Series: Scientific Reports;8(1)
ISSN: 2045-2322
DOI: 10.1038/s41598-018-32694-7
Subject: Macroautophagy; Nutrient signalling; Líffærafræði; Sjálfsát
URI: https://hdl.handle.net/20.500.11815/1272

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Citation:

Ogmundsdottir, M. H., Fock, V., Sooman, L., Pogenberg, V., Dilshat, R., Bindesbøll, C., . . . Steingrimsson, E. (2018). A short isoform of ATG7 fails to lipidate LC3/GABARAP. Scientific Reports, 8(1), 14391. doi:10.1038/s41598-018-32694-7

Abstract:

Autophagy is a degradation pathway important for cellular homeostasis. The E1-like enzyme ATG7 is a key component of the autophagy machinery, with the main function of mediating the lipidation of LC3/GABARAP during autophagosome formation. By analysing mRNA-sequencing data we found that in addition to the full-length ATG7 isoform, various tissues express a shorter isoform lacking an exon of 27 amino acids in the C-terminal part of the protein, termed ATG7(2). We further show that ATG7(2) does not bind LC3B and fails to mediate the lipidation of members of the LC3/GABARAP family. We have thus identified an isoform of ATG7 that is unable to carry out the best characterized function of the protein during the autophagic response. This short isoform will have to be taken into consideration when further studying the role of ATG7.

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