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The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji

Akshaya Arva¹, Yasar Arfat T Kasu¹, Jennifer Duncan¹

¹Department of Biology, Texas Woman's University, Denton, TX 76204.

Proceedings of the National Academy of Sciences of the United States of America

|January 14, 2021

Abstract:

The Ligand of Ate1 (Liat1) is a protein of unknown function that was originally discovered through its interaction with arginyl-tRNA protein transferase 1 (Ate1), a component of the Arg/N-degron pathway of protein degradation. Here, we characterized the functional domains of mouse Liat1 and found that its N-terminal half comprises an intrinsically disordered region (IDR) that facilitates its liquid-liquid phase separation (LLPS) in the nucleolus. Using bimolecular fluorescence complementation and immunocytochemistry, we found that Liat1 is targeted to the nucleolus by a low-complexity poly-K region within its IDR. We also found that the lysyl-hydroxylase activity of Jumonji Domain Containing 6 (Jmjd6) modifies Liat1, in a manner that requires the Liat1 poly-K region, and inhibits its nucleolar targeting and potential functions. In sum, this study reveals that Liat1 participates in nucleolar LLPS regulated by Jmjd6.

Keywords:

Jmjd6 Liat1 intrinsically disordered protein liquid–liquid phase separation nucleolus

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