MYD88
Gene Ontology Biological Process
- 3'-UTR-mediated mRNA stabilization [IDA]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- cell surface receptor signaling pathway [TAS]
- cellular response to mechanical stimulus [IEP]
- defense response to Gram-positive bacterium [ISS]
- innate immune response [TAS]
- negative regulation of apoptotic process [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IEP]
- positive regulation of interleukin-17 production [ISS]
- positive regulation of interleukin-23 production [ISS]
- positive regulation of interleukin-6 production [ISS]
- positive regulation of type I interferon production [TAS]
- regulation of inflammatory response [ISS]
- response to interleukin-1 [IMP]
- signal transduction [NAS]
- toll-like receptor 10 signaling pathway [TAS]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor 5 signaling pathway [TAS]
- toll-like receptor 9 signaling pathway [TAS]
- toll-like receptor TLR1:TLR2 signaling pathway [TAS]
- toll-like receptor TLR6:TLR2 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
LRRFIP1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins.
Emerging evidences suggest TLR-mediated signaling is tightly regulated by a specific chain of intracellular protein-protein interactions, some of which are yet to be identified. Previously we utilized a dual-tagging quantitative proteomics approach to uncover MyD88 interactions in LPS-stimulated cells and described the function of Fliih, a leucine-rich repeat (LRR) protein that negatively regulates NF-kappaB activity. Here we characterize two distinct ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID