Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders
Protein functionality hinges on precise three-dimensional structures, while molecular chaperones orchestrate folding, proteome maintenance, and proteostasis. Recent attention has focused on BRICHOS domain from pro-proteins of pulmonary surfactant protein C (proSP-C), Bri2 and Bri3 as autonomous mole...
Saved in:
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
KeAi Communications Co., Ltd.
2024-12-01
|
| Series: | Supramolecular Materials |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S266724052300020X |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1846099820340576256 |
|---|---|
| author | Waqar Ahmad Tian Zhao KeFeng He Shi-Zhong Luo |
| author_facet | Waqar Ahmad Tian Zhao KeFeng He Shi-Zhong Luo |
| author_sort | Waqar Ahmad |
| collection | DOAJ |
| description | Protein functionality hinges on precise three-dimensional structures, while molecular chaperones orchestrate folding, proteome maintenance, and proteostasis. Recent attention has focused on BRICHOS domain from pro-proteins of pulmonary surfactant protein C (proSP-C), Bri2 and Bri3 as autonomous molecular chaperones, crucial for cellular quality control. Bri2, an integral protein, emerges with expressions ranging from the central nervous system to cancer and lung diseases and exhibits proficiency in combating amyloid aggregation, a hallmark of neurodegenerative disorders like Alzheimer's. The capability of Bri2-BRICHOS to shield aggregation-prone regions, unveiling its role as an intramolecular guardian. In this review, we explore the structure and function of BRI2 and its relation to neurodegenerative diseases, as well as the structural complexities, functional landscapes, and implications of BRICHOS domains in diverse neurodegenerative disorders. Furthermore, it sheds light on Bri2-BRICHOS as a possible candidate for therapeutic approaches in protein aggregation disorders. |
| format | Article |
| id | doaj-art-a721af9123a8473fbd3ed6ab841eaf06 |
| institution | Kabale University |
| issn | 2667-2405 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Supramolecular Materials |
| spelling | doaj-art-a721af9123a8473fbd3ed6ab841eaf062024-12-31T04:13:22ZengKeAi Communications Co., Ltd.Supramolecular Materials2667-24052024-12-013100050Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disordersWaqar Ahmad0Tian Zhao1KeFeng He2Shi-Zhong Luo3Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, ChinaBeijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, ChinaBeijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, ChinaCorresponding author.; Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, ChinaProtein functionality hinges on precise three-dimensional structures, while molecular chaperones orchestrate folding, proteome maintenance, and proteostasis. Recent attention has focused on BRICHOS domain from pro-proteins of pulmonary surfactant protein C (proSP-C), Bri2 and Bri3 as autonomous molecular chaperones, crucial for cellular quality control. Bri2, an integral protein, emerges with expressions ranging from the central nervous system to cancer and lung diseases and exhibits proficiency in combating amyloid aggregation, a hallmark of neurodegenerative disorders like Alzheimer's. The capability of Bri2-BRICHOS to shield aggregation-prone regions, unveiling its role as an intramolecular guardian. In this review, we explore the structure and function of BRI2 and its relation to neurodegenerative diseases, as well as the structural complexities, functional landscapes, and implications of BRICHOS domains in diverse neurodegenerative disorders. Furthermore, it sheds light on Bri2-BRICHOS as a possible candidate for therapeutic approaches in protein aggregation disorders.http://www.sciencedirect.com/science/article/pii/S266724052300020XBri2BRICHOSAmyloid aggregationNeurodegenerative disorders |
| spellingShingle | Waqar Ahmad Tian Zhao KeFeng He Shi-Zhong Luo Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders Supramolecular Materials Bri2 BRICHOS Amyloid aggregation Neurodegenerative disorders |
| title | Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders |
| title_full | Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders |
| title_fullStr | Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders |
| title_full_unstemmed | Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders |
| title_short | Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders |
| title_sort | exploring the role of british dementia protein 2 bri2 and its brichos domain in neurodegenerative disorders |
| topic | Bri2 BRICHOS Amyloid aggregation Neurodegenerative disorders |
| url | http://www.sciencedirect.com/science/article/pii/S266724052300020X |
| work_keys_str_mv | AT waqarahmad exploringtheroleofbritishdementiaprotein2bri2anditsbrichosdomaininneurodegenerativedisorders AT tianzhao exploringtheroleofbritishdementiaprotein2bri2anditsbrichosdomaininneurodegenerativedisorders AT kefenghe exploringtheroleofbritishdementiaprotein2bri2anditsbrichosdomaininneurodegenerativedisorders AT shizhongluo exploringtheroleofbritishdementiaprotein2bri2anditsbrichosdomaininneurodegenerativedisorders |