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Ligand of ATE1 protein (LIAT1), also known as C17orf97, is a conserved, intrinsically disordered protein found in the nucleolus of animal cells. LIAT1 was identified through its binding to arginyl-tRNA protein transferase 1 (ATE1), but direct enzymatic or receptor activity has not been characterized. Its main known property is promoting liquid–liquid phase separation (LLPS) via its N-terminal intrinsically disordered region containing a poly-lysine motif, which is essential for its nucleolar localization and self-interaction. The post-translational modification of LIAT1 by Jumonji Domain Containing 6 (JMJD6) regulates its phase separation ability and nuclear targeting but its physiological role remains unclear. Despite molecular interest, LIAT1 is not established as a receptor, enzyme, transporter, or as a classical therapeutic target; its functions and disease associations are largely speculative. LIAT1 lacks known molecular or pharmaceutical targeting and is not a therapeutic target by current scientific and pharmacological definitions. There is no evidence for drug interactions, mechanism of action for pharmacology, biomarker status, nor clinical safety concerns. Though sometimes found in commercial antibody/protein catalogs, these listings are for research reagent purposes only, not as a drug target.
None known (no evidence for drug targeting)
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