Asssessing the Liquid-Liquid Phase Separation Abilities of Eyes Absent Protein

The Eyes Absent (EYA1-4) family of proteins are critical gatekeepers for cellular responses to environmental stressors. This gatekeeping function is exerted through two pathways; EYA proteins act as a switch between proliferation and apoptosis in response to DNA damage, and directly regulate transcriptional activity through interactions with other coregulators, namely the SIX family of proteins. EYA proteins are comprised of two domains: a folded “EYA domain” (ED) in the C-terminus containing tyrosine phosphatase activity, and an intrinsically disordered “transactivation domain” (TAD) in the N-terminus. Despite wide sequence variation in human EYA1-4 TADs, with approximately 40% identity conserved vs. 77% identity conserved in the ED, all four EYA TADs were identified as potential drivers of liquid-liquid phase separation in a proteome-wide screen. The apparent conservation of this physical potential within the disordered region of EYA proteins suggests that phase separation of this region may play a role in interactions between EYA and other proteins and in the transactivation activity of these proteins. This thesis project tested the hypothesis that the TAD of EYA2 phase-separates in vitro, and the results strongly indicate that EYA2-TAD is capable of self-association in vitro.

Name thesis:degree_name

Masters

Discipline thesis:degree_discipline

Biochemistry

Grantor

Texas State University

Year dc:date.issued

2024

Author dc:creator

• Remsing, Jaclyn

Advisor dc:contributor.advisor

• Lewis, Karen A.

Committee members dc:contributor.committeemember

• Whitten, Steven T.
• Xue, Xiaoyu

• biochemistry
• liquid-liquid phase separation
• proteins
• eyes
• absent protein
• EYA
• EYA1
• EYA2
• TAD

Language dc:language.iso

en

Handle dc:identifier.uri

https://hdl.handle.net/10877/20117

OAI identifier oai:identifier

oai:digital.library.txst.edu:10877/20117