You are here
STUDIES ON THE POTENTIAL REGULATION OF USP30 BY OMI/HTRA2 PROTEASE
| Title: | STUDIES ON THE POTENTIAL REGULATION OF USP30 BY OMI/HTRA2 PROTEASE. |
 36 views 14 downloads |
|---|---|---|
| Name(s): |
Jin, Sunmi, Author Zervos, Antonis, Committee Chair University of Central Florida, Degree Grantor |
|
| Type of Resource: | text | |
| Date Issued: | 2019 | |
| Publisher: | University of Central Florida | |
| Language(s): | English | |
| Abstract/Description: | The intent of this thesis is to determine whether the deubiquitinating enzyme ubiquitin specific protease 30 (USP30) is cleaved by Omi/HtrA2 (hereafter referred to as Omi) protease during mitochondrial stress. USP30 is a mitochondrial protein that is anchored in the outer mitochondrial membrane and has components in the intermembrane space (IMS) as well as in the cytoplasm. USP30's IMS component has a six-amino-acid sequence that is very similar to Omi's consensus cleavage sites. Under normal conditions, Omi resides exclusively within the IMS; therefore, if Omi were to cleave USP30, it would target the part of the protein located in the IMS component. Omi is known to play a crucial role in a variety of diseases including cancers, neurodegenerative, and metabolic disorders. Since Omi is a serine protease, it is assumed to carry its normal function through the direct cleavage and degradation of specific substrates. If USP30 deubiquitinase is a bona fide substrate of Omi, this will provide new and important information on the mechanism by which Omi regulates the polyubiquitination process during mitochondrial stress. | |
| Identifier: | CFH2000498 (IID), ucf:45629 (fedora) | |
| Note(s): |
2019-05-01 B.S. College of Medicine, Burnett School of Biomedical Sciences Bachelors This record was generated from author submitted information. |
|
| Persistent Link to This Record: | http://purl.flvc.org/ucf/fd/CFH2000498 | |
| Restrictions on Access: | campus 2020-05-01 | |
| Host Institution: | UCF |
