Degree Type
Honors Capstone Project
Date of Submission
Spring 5-1-2019
Capstone Advisor
Carlos Castañeda
Honors Reader
Surabhi Raina
Capstone Major
Biology
Capstone College
Arts and Science
Audio/Visual Component
no
Capstone Prize Winner
no
Won Capstone Funding
no
Honors Categories
Sciences and Engineering
Subject Categories
Biology | Biotechnology | Life Sciences
Abstract
Liquid-liquid phase separation (LLPS), the mechanism by which macromolecules demix to form a dense liquid- like phase in equilibrium with a phase dilute of molecules, is hypothesized to be the dominant mechanism governing membraneless organelle formation inside the cell. Stress granules, a type of membraneless organelle that assemble reversibly in response to cellular stress, may be formed through LLPS. Dysregulation of this process may lead to disease aggregates in vivo. LLPS is thought to be governed by the occurrence of weak, multivalent interactions between molecules such as proteins and RNA molecules. Multivalent interactions, the proposed driving force governing LLPS, are weak, dynamic forces between multiple sites on different proteins, giving rise to liquid-like properties. Here, we use human UBQLN2 as a model system for studying molecular drivers of LLPS in vitro. UBQLN2 contains a domain that binds to ubiquitin, which marks proteins for degradation by the proteasome. Here, we show that ubiquitin interactions with UBQLN2 are altered by UBQLN2 amino acid substitutions.
Recommended Citation
Habjan, Christine, "MOLECULAR DETERMINANTS OF UBQLN2 LIQUID-LIQUID PHASE SEPARATION MODULATED BY UBIQUITIN" (2019). Renée Crown University Honors Thesis Projects - All. 1342.
https://surface.syr.edu/honors_capstone/1342
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
