An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

PLK4 deubiquitination by Spata2-CYLD suppresses NEK7-mediated NLRP3 inflammasome activation at the centrosome.

Yang XD, Li W, Zhang S, Wu D, Jiang X, Tan R, Niu X, Wang Q, Wu X, Liu Z, Chen LF, Qin J, Su B

The innate immune sensor NLRP3 assembles an inflammasome complex with NEK7 and ASC to activate caspase-1 and drive the maturation of proinflammatory cytokines IL-1? and IL-18. NLRP3 inflammasome activity must be tightly controlled, as its over-activation is involved in the pathogenesis of inflammatory diseases. Here, we show that NLRP3 inflammasome activation is suppressed by a centrosomal protein Spata2. Spata2 deficiency ... [more]

EMBO J. Dec. 15, 2019; 39(2);e102201 [Pubmed: 31762063]

Throughput

High Throughput

Additional Notes

assayed using BioID (proximity-dependent biotin identification)

Curated By

BioGRID

Interaction Summary

CYLD

Gene Ontology Biological Process

Gene Ontology Molecular Function

Lys63-specific deubiquitinase activity [IDA]proline-rich region binding [IPI]protein binding [IPI]protein kinase binding [IPI]structural constituent of ribosome [IBA]ubiquitin-specific protease activity [IDA]zinc ion binding [IDA]

Gene Ontology Cellular Component

CC2D1A