Protein aggregation in the cytoplasm

by Triana Amen
Doctoral thesis
Date of Examination:2020-04-30
Date of issue:2020-05-20
Advisor:Prof. Dr. Daniel Kaganovich
Referee:Prof. Dr. Daniel Kaganovich
Referee:Prof. Dr. Gerhard Braus
Referee:Prof. Dr. Jeffrey L. Brodsky
Persistent Address: http://dx.doi.org/10.53846/goediss-7981

 

 

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Abstract

English

The hypothesis motivating this thesis is that aggregation of proteins in the cytoplasm can have protective functions and can facilitate cell survival. Conversely, the disruption of functional aggregation can lead to cellular dysfunction and death. There is, therefore, a tremendous need to understand the mechanisms and precise sub-cellular architecture of functional aggregates. So far, the multitude of cellular aggregate structures or granules have been proposed to function as enzyme storage compartments, centers of memory retention, signaling hubs, mRNA triage compartments, degradation and protein refolding depots, structural elements, and transport granules. One of the unifying aspects of cytoplasmic granules appears to be stress dependent transient formation. In order to study cellular aggregation in live cells I chose to investigate factors that regulate the formation and clearance of cellular inclusions and their functions in cellular metabolism and signaling pathways. In this thesis I describe regulatory pathways that govern formation and function of granules with the focus on ribonucleoprotein granules, Stress Granules.
Keywords: Stress Granule, protein aggregation, fatty acid oxidation, lipid droplet, eisosome, signaling, mitochondria
 
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