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Linear ubiquitination by LUBEL has a role in Drosophila heat stress response
Author(s) -
Asaoka Tomoko,
Almagro Jorge,
Ehrhardt Christine,
Tsai Isabella,
Schleiffer Alexander,
Deszcz Luiza,
Junttila Sini,
Ringrose Leonie,
Mechtler Karl,
Kavirayani Anoop,
Gyenesei Attila,
Hofmann Kay,
Duchek Peter,
Rittinger Katrin,
Ikeda Fumiyo
Publication year - 2016
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201642378
Subject(s) - ubiquitin , ubiquitin ligase , drosophila melanogaster , microbiology and biotechnology , biology , ubiquitin conjugating enzyme , ubiquitin protein ligases , drosophila (subgenus) , heat shock , heat shock protein , biochemistry , gene
The HOIP ubiquitin E3 ligase generates linear ubiquitin chains by forming a complex with HOIL ‐1L and SHARPIN in mammals. Here, we provide the first evidence of linear ubiquitination induced by a HOIP orthologue in Drosophila . We identify Drosophila CG 11321, which we named Linear Ubiquitin E3 ligase ( LUBEL ), and find that it catalyzes linear ubiquitination in vitro . We detect endogenous linear ubiquitin chain‐derived peptides by mass spectrometry in Drosophila Schneider 2 cells and adult flies. Furthermore, using CRISPR /Cas9 technology, we establish linear ubiquitination‐defective flies by mutating residues essential for the catalytic activity of LUBEL . Linear ubiquitination signals accumulate upon heat shock in flies. Interestingly, flies with LUBEL mutations display reduced survival and climbing defects upon heat shock, which is also observed upon specific LUBEL depletion in muscle. Thus, LUBEL is involved in the heat response by controlling linear ubiquitination in flies.