Liat1 nucleolar phase separation is regulated by Jmjd6
| dc.contributor.author | Arva, Akshaya | |
| dc.contributor.author | Brower, Christopher S. | |
| dc.date.accessioned | 2021-03-19T15:34:15Z | |
| dc.date.available | 2021-03-19T15:34:15Z | |
| dc.date.issued | 2021 | |
| dc.description | Creative Arts and Research Symposium | |
| dc.description | Creative Arts and Research Symposium | en_US |
| dc.description.abstract | The Ligand of Ate1 (Liat1) was discovered by its interaction with Ate1, involved in the Ndegron pathway of protein degradation. The characterization and functional significance of Liat1 awaits discovery. While the C-terminal half of Liat1 is necessary for Ate1-binding, it’s N-terminal half is intrinsically disordered and contains two regions of low sequence complexity, most notable a poly-lysine region. Intrinsically disordered proteins have recently been shown to participate in liquid phase separation, which facilitates the formation of membrane-lacking intracellular compartments such as the nucleolus. Using bimolecular fluorescence complementation (BiFC) and yeast-two hybrid analysis, we found that Liat1 self-interacts to undergo liquid phase separation. We also found that the poly-lysine region of Liat1 facilitates Liat1 targeting to the nucleolus. Finally, we found that the nucleolar phase separation of Liat1 is regulated by the lysl-hydroxylase activity of Jumonji Domain Containing 6 (Jmjd6). | |
| dc.description.department | Biology | |
| dc.description.sponsorship | Supported by the TWU Research Enhancement Program and NIH grant R15NS095317 | |
| dc.identifier.uri | https://hdl.handle.net/11274/12766 | |
| dc.language.iso | en_US | en_US |
| dc.title | Liat1 nucleolar phase separation is regulated by Jmjd6 | en_US |
| dc.type | Poster | en_US |
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