Proteomics

Dataset Information

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TurboID-mediated proximal labeling of Drosophila BubR1 and its cleavage variants

ABSTRACT: V5-TurboID-tagged Drosophila BubR1 and its cleavage variants were transiently expressed in Drosophila S2 cells in two biological replicates. Cells were treated with 500 µM biotin for 30 min for protein biotinylation. Biotinylated protein-containing lysate was subjected to FG-NeutrAvidin beads purification followed by on-beads trypsin digestion. Digested peptides were desalinated and purified using GL-tip SDB. Purified peptides were subjected to LC-MS/MS analysis.

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

SUBMITTER: Masayuki Miura 

PROVIDER: PXD033797 | JPOST Repository | Thu May 11 00:00:00 BST 2023

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
20211018_TurboIDBubR101.raw Raw
20211018_TurboIDBubR101_normalized.pdResult Other
20211018_TurboIDBubR102.raw Raw
20211018_TurboIDBubR104.raw Raw
20211018_TurboIDBubR105.raw Raw
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Publications

Caspase cleaves Drosophila BubR1 to modulate spindle assembly checkpoint function and lifespan of the organism.

Shinoda Natsuki N   Horikoshi Misuzu M   Taira Yusuke Y   Muramoto Masaya M   Hirayama Shoshiro S   Murata Shigeo S   Miura Masayuki M  

The FEBS journal 20230515 17

Caspases cleave over 1500 substrates in the human proteome in both lethal and non-lethal scenarios. However, reports of the physiological consequences of substrate cleavage are limited. Additionally, the manner in which caspase cleaves only a subset of substrates in the non-lethal scenario remains to be elucidated. BubR1, a spindle assembly checkpoint component, is a caspase substrate in humans, the physiological function of which remains unclear. Here, we found that caspases, especially Drice,  ...[more]

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