Chaperone-mediated formation of shell-like TDP-43 condensates
Transactivation response element DNA binding protein 43 (TDP-43), an RNA-binding protein is the major component of inclusion bodies in patients afflicted with Amyotrophic Lateral Sclerosis (ALS). A recent study established that a compromise in RNA-binding capacity of TDP-43, resulting from post-tra...
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Format: | Final Year Project (FYP) |
Language: | English |
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Nanyang Technological University
2022
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Online Access: | https://hdl.handle.net/10356/156869 |
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author | Kong, Jian Hua |
author2 | Choe Young Jun |
author_facet | Choe Young Jun Kong, Jian Hua |
author_sort | Kong, Jian Hua |
collection | NTU |
description | Transactivation response element DNA binding protein 43 (TDP-43), an RNA-binding protein is the major component of inclusion bodies in patients afflicted with Amyotrophic Lateral Sclerosis (ALS). A recent study established that a compromise in RNA-binding capacity of TDP-43, resulting from post-translational modifications or ALS-causing mutations, confers TDP-43 the ability to de-mix into intranuclear liquid spherical shells with a liquid core. The major chaperone, Heat shock protein 70 (Hsp70), was reported to be enriched within the liquid core and pivotal in maintenance of the shell structure.
To examine the presence of other chaperones in the core of the TDP-43 shell. Interestingly, reduced function of the Hsp70 system abrogated the shell formation. It is very likely that other chaperones are also enriched in the TDP-43 shell-like structures. Further investigation into how chaperones mediate TDP-43 phase separation could illuminate the molecular basis for ALS. |
first_indexed | 2024-10-01T05:58:44Z |
format | Final Year Project (FYP) |
id | ntu-10356/156869 |
institution | Nanyang Technological University |
language | English |
last_indexed | 2024-10-01T05:58:44Z |
publishDate | 2022 |
publisher | Nanyang Technological University |
record_format | dspace |
spelling | ntu-10356/1568692024-04-01T15:33:14Z Chaperone-mediated formation of shell-like TDP-43 condensates Kong, Jian Hua Choe Young Jun School of Biological Sciences yjchoe@ntu.edu.sg Science::Biological sciences::Molecular biology Transactivation response element DNA binding protein 43 (TDP-43), an RNA-binding protein is the major component of inclusion bodies in patients afflicted with Amyotrophic Lateral Sclerosis (ALS). A recent study established that a compromise in RNA-binding capacity of TDP-43, resulting from post-translational modifications or ALS-causing mutations, confers TDP-43 the ability to de-mix into intranuclear liquid spherical shells with a liquid core. The major chaperone, Heat shock protein 70 (Hsp70), was reported to be enriched within the liquid core and pivotal in maintenance of the shell structure. To examine the presence of other chaperones in the core of the TDP-43 shell. Interestingly, reduced function of the Hsp70 system abrogated the shell formation. It is very likely that other chaperones are also enriched in the TDP-43 shell-like structures. Further investigation into how chaperones mediate TDP-43 phase separation could illuminate the molecular basis for ALS. Bachelor of Science in Biological Sciences 2022-04-27T05:13:16Z 2022-04-27T05:13:16Z 2022 Final Year Project (FYP) Kong, J. H. (2022). Chaperone-mediated formation of shell-like TDP-43 condensates. Final Year Project (FYP), Nanyang Technological University, Singapore. https://hdl.handle.net/10356/156869 https://hdl.handle.net/10356/156869 en application/pdf Nanyang Technological University |
spellingShingle | Science::Biological sciences::Molecular biology Kong, Jian Hua Chaperone-mediated formation of shell-like TDP-43 condensates |
title | Chaperone-mediated formation of shell-like TDP-43 condensates |
title_full | Chaperone-mediated formation of shell-like TDP-43 condensates |
title_fullStr | Chaperone-mediated formation of shell-like TDP-43 condensates |
title_full_unstemmed | Chaperone-mediated formation of shell-like TDP-43 condensates |
title_short | Chaperone-mediated formation of shell-like TDP-43 condensates |
title_sort | chaperone mediated formation of shell like tdp 43 condensates |
topic | Science::Biological sciences::Molecular biology |
url | https://hdl.handle.net/10356/156869 |
work_keys_str_mv | AT kongjianhua chaperonemediatedformationofshellliketdp43condensates |