Toll-interacting protein

Both ATG8-interaction motifs (AIM1 and AIM2) are required for the association with ATG8 family proteins.

The N-terminal TOM1-binding domain (residues 1-53) is a disordered domain that partially folds when bound to the GAT domain of TOM1.

Component of the signaling pathway of IL-1 and Toll-like receptors (PubMed:10854325, PubMed:11751856). Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex (PubMed:10854325). Inhibits IRAK1 phosphorylation and kinase activity (PubMed:11751856). Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates (PubMed:25042851). The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (PubMed:25042851). In a complex with TOM1, recruits ubiquitin-conjugated proteins onto early endosomes (PubMed:15047686). Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:26320582).

Phosphorylated by IRAK1 upon stimulation by IL-1 or microbial products.

Belongs to the tollip family.

• Cytoplasm
• Endosome
• Early endosome
• Localized to endo/exosomal vesicles.

Toll-interacting protein, TOLLIP

• entrezGene:54472
• omim:606277
• swissprot:Q9H0E2

Proteins

Neuroscience

30282Da