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A short isoform of ATG7 fails to lipidate LC3/GABARAP

Standard

A short isoform of ATG7 fails to lipidate LC3/GABARAP. / Ogmundsdottir, H M; Fock, V; Sooman, L; Pogenberg, V; Dilshat, R; Bindesbøll, C; Ogmundsdottir, H M; Simonsen, A; Wilmanns, M; Steingrimsson, E.

in: SCI REP-UK, Jahrgang 8, Nr. 1, 26.09.2018, S. 14391.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Ogmundsdottir, HM, Fock, V, Sooman, L, Pogenberg, V, Dilshat, R, Bindesbøll, C, Ogmundsdottir, HM, Simonsen, A, Wilmanns, M & Steingrimsson, E 2018, 'A short isoform of ATG7 fails to lipidate LC3/GABARAP', SCI REP-UK, Jg. 8, Nr. 1, S. 14391. https://doi.org/10.1038/s41598-018-32694-7

APA

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

Vancouver

Ogmundsdottir HM, Fock V, Sooman L, Pogenberg V, Dilshat R, Bindesbøll C et al. A short isoform of ATG7 fails to lipidate LC3/GABARAP. SCI REP-UK. 2018 Sep 26;8(1):14391. https://doi.org/10.1038/s41598-018-32694-7

Bibtex

@article{b493e7f3d3024fb69717a1fcae2c64f2,
title = "A short isoform of ATG7 fails to lipidate LC3/GABARAP",
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.",
author = "Ogmundsdottir, {H M} and V Fock and L Sooman and V Pogenberg and R Dilshat and C Bindesb{\o}ll and Ogmundsdottir, {H M} and A Simonsen and M Wilmanns and E Steingrimsson",
year = "2018",
month = sep,
day = "26",
doi = "10.1038/s41598-018-32694-7",
language = "English",
volume = "8",
pages = "14391",
journal = "SCI REP-UK",
issn = "2045-2322",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - A short isoform of ATG7 fails to lipidate LC3/GABARAP

AU - Ogmundsdottir, H M

AU - Fock, V

AU - Sooman, L

AU - Pogenberg, V

AU - Dilshat, R

AU - Bindesbøll, C

AU - Ogmundsdottir, H M

AU - Simonsen, A

AU - Wilmanns, M

AU - Steingrimsson, E

PY - 2018/9/26

Y1 - 2018/9/26

N2 - 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.

AB - 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.

U2 - 10.1038/s41598-018-32694-7

DO - 10.1038/s41598-018-32694-7

M3 - SCORING: Journal article

C2 - 30258106

VL - 8

SP - 14391

JO - SCI REP-UK

JF - SCI REP-UK

SN - 2045-2322

IS - 1

ER -