Toll-interacting protein

Definition:

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

References:

[1]. K Burns, et al. Tollip, a new component of the IL-1RI pathway, links IRAK to the IL-1 receptor. Nat Cell Biol. 2000 Jun;2(6):346-51. [Content Brief]

[2]. Guolong Zhang, et al. Negative regulation of toll-like receptor-mediated signaling by Tollip. J Biol Chem. 2002 Mar 1;277(9):7059-65. [Content Brief]

[3]. Yohei Katoh, et al. Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes. J Biol Chem. 2004 Jun 4;279(23):24435-43. [Content Brief]

[4]. Kefeng Lu, et al. Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family. Cell. 2014 Jul 31;158(3):549-63. [Content Brief]

[5]. Shuyan Xiao, et al. Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. Structure. 2015 Oct 6;23(10):1910-1920. [Content Brief]

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