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
TIRAP
Gene Ontology Biological Process
- 3'-UTR-mediated mRNA stabilization [IDA]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- TIRAP-dependent toll-like receptor 4 signaling pathway [IDA]
- cell surface receptor signaling pathway [ISS]
- cellular response to bacterial lipopeptide [ISS]
- cellular response to lipoteichoic acid [ISS]
- defense response to Gram-positive bacterium [ISS]
- innate immune response [TAS]
- myeloid cell differentiation [ISS]
- negative regulation of growth of symbiont in host [ISS]
- positive regulation of B cell proliferation [ISS]
- positive regulation of ERK1 and ERK2 cascade [IMP]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- positive regulation of JNK cascade [IMP]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of chemokine (C-X-C motif) ligand 1 production [ISS]
- positive regulation of chemokine (C-X-C motif) ligand 2 production [ISS]
- positive regulation of interleukin-12 production [ISS]
- positive regulation of interleukin-15 production [IDA]
- positive regulation of interleukin-6 biosynthetic process [IMP]
- positive regulation of interleukin-8 production [IMP]
- positive regulation of neutrophil chemotaxis [ISS]
- positive regulation of protein homodimerization activity [IDA]
- positive regulation of toll-like receptor 2 signaling pathway [IMP]
- positive regulation of toll-like receptor 3 signaling pathway [ISS]
- positive regulation of toll-like receptor 4 signaling pathway [IMP]
- positive regulation of tumor necrosis factor production [IMP]
- regulation of innate immune response [IC]
- regulation of interferon-beta production [ISS]
- response to lipopolysaccharide [IDA]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 4 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
PCA
A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.
Publication
Caspase-1 targets the TLR adaptor Mal at a crucial TIR-domain interaction site.
Toll-like receptors (TLRs) are crucial components of innate immunity, ensuring efficient responses against invading pathogens. After ligand binding, TLR signaling is initiated by recruitment of adaptor molecules, a step mediated by homotypic Toll-IL-1 receptor (TIR) domain interactions. Four TIR-containing TLR adaptor molecules are described, all of which are susceptible to modification and strict regulation. For example, caspase-1 is reported to ... [more]
Throughput
- Low Throughput
Additional Notes
- interaction detected by MAPPIT
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TIRAP MYD88 | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | 0.9998 | BioGRID | 3187111 | |
| MYD88 TIRAP | Affinity Capture-Western 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. | Low | - | BioGRID | - | |
| MYD88 TIRAP | Affinity Capture-Western 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. | Low | - | BioGRID | - | |
| TIRAP MYD88 | Affinity Capture-Western 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. | Low | - | BioGRID | - | |
| MYD88 TIRAP | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | 511234 | |
| TIRAP MYD88 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | 511239 | |
| TIRAP MYD88 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | 511257 | |
| TIRAP MYD88 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | 511279 | |
| TIRAP MYD88 | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | BioGRID | - | |
| TIRAP MYD88 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
| MYD88 TIRAP | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID