Proteomics

Dataset Information

0

Label-free quantification of Xkr4 interactors


ABSTRACT: Membrane fractions of XRCC4 KO PLB cells expressing SPOT-Xkr4-FLAG and XRCC4 (WT or R270A) were solubilized by detergent and immunoprecipitated with anti-SPOT nanobody-conjugated beads to precipitate Xkr4 interactors, followed by mass spectrometry.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hidetaka Kosako 

PROVIDER: PXD023536 | JPOST Repository | Tue Jan 12 00:00:00 GMT 2021

REPOSITORIES: jPOST

Dataset's files

Source:
Action DRS
1_XRCC4_WT_minus.raw Raw
2_XRCC4_WT_STS.raw Raw
3_XRCC4_R270A_minus.raw Raw
4_XRCC4_R270A_STS.raw Raw
Xkr4_SPOTtrap_LFQ.xlsx Xlsx
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Publications

Caspase cleavage releases a nuclear protein fragment that stimulates phospholipid scrambling at the plasma membrane.

Maruoka Masahiro M   Zhang Panpan P   Mori Hiromi H   Imanishi Eiichi E   Packwood Daniel M DM   Harada Hiroshi H   Kosako Hidetaka H   Suzuki Jun J  

Molecular cell 20210315 7


Phospholipid scrambling in dying cells promotes phosphatidylserine exposure, a critical process for efferocytosis. We previously identified the Xkr family protein Xkr4 as a phospholipid-scrambling protein, but its activation mechanisms remain unknown. Here we show that Xkr4 is activated in two steps: dimer formation by caspase-mediated cleavage and structural change caused by activating factors. To identify the factors, we developed a new screening system, "revival screening," using a CRISPR sgR  ...[more]

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