Proteomics

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ABIN1 is an signal-induced autophagy adaptor counteracting LUBAC-mediated linear ubiquitination


ABSTRACT: ABIN1 KO RAW264.7 cells and stably reconstituted with 3×FLAG-ABIN1 WT or D485N were subjected to mass spectrometric analysis. Three biological replicates were prepared for each condition. Cells were stimulated for 3 hours with 100 ng/ml LPS. ABIN1 was immunoprecipitated with 30 uL anti-FLAG M2 Magnetic Beads (M8823, Sigma-Aldrich) for 2 h at 4℃. Immunoprecipitated sample was eluted by incubation at 90°C for 5 min in 100 uL PTS buffer. Each sample was split into 3 tubes for protein digestion with Lys-C and trypsin, chymotrypsin, or Glu-C.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Kazuhiro Iwai 

PROVIDER: PXD024864 | JPOST Repository | Thu Feb 17 00:00:00 GMT 2022

REPOSITORIES: jPOST

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Publications

ABIN1 is a signal-induced autophagy receptor that attenuates NF-κB activation by recognizing linear ubiquitin chains.

Shinkawa Yutaka Y   Imami Koshi K   Fuseya Yasuhiro Y   Sasaki Katsuhiro K   Ohmura Koichiro K   Ishihama Yasushi Y   Morinobu Akio A   Iwai Kazuhiro K  

FEBS letters 20220304 9


Linear ubiquitin chains play pivotal roles in immune signaling by augmenting NF-κB activation and suppressing programmed cell death induced by various stimuli. A20-binding inhibitor of NF-κB 1 (ABIN1) binds to linear ubiquitin chains and attenuates NF-κB activation and cell death induction. Although interactions with linear ubiquitin chains are thought to play a role in ABIN1-mediated suppression of NF-κB and cell death, the underlying molecular mechanisms remain unclear. Here, we show that upon  ...[more]

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