Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains
α-catenin is an adhesion protein located at the cadherin-based cell–cell adherens junction. α-catenin cross-links β-catenin and actin fiber in the adhesion protein complex, and plays an important role in the formation and modulation of cell–cell adhesion. The central modulation domains can be unfold...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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World Scientific Publishing
2019-01-01
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| Series: | Journal of Innovative Optical Health Sciences |
| Subjects: | |
| Online Access: | http://www.worldscientific.com/doi/pdf/10.1142/S1793545818410018 |
| _version_ | 1828872142853242880 |
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| author | Xueping Li Weili Zhai Zilong Guo Hu Chen |
| author_facet | Xueping Li Weili Zhai Zilong Guo Hu Chen |
| author_sort | Xueping Li |
| collection | DOAJ |
| description | α-catenin is an adhesion protein located at the cadherin-based cell–cell adherens junction. α-catenin cross-links β-catenin and actin fiber in the adhesion protein complex, and plays an important role in the formation and modulation of cell–cell adhesion. The central modulation domains can be unfolded to expose binding site of vinculin when stretching force is applied. Here, we studied the force-induced unfolding dynamics of α-catenin modulation domains under different loading rates from which the unfolding distance of M2 and M3 domains is determined to be 5–7nm, and an unfolding intermediate state is identified. We also found that the folding process of M1–M3 domains goes through different pathways with cooperativity. |
| first_indexed | 2024-12-13T06:47:39Z |
| format | Article |
| id | doaj.art-df67978a61b542dc817a47560d498e65 |
| institution | Directory Open Access Journal |
| issn | 1793-5458 1793-7205 |
| language | English |
| last_indexed | 2024-12-13T06:47:39Z |
| publishDate | 2019-01-01 |
| publisher | World Scientific Publishing |
| record_format | Article |
| series | Journal of Innovative Optical Health Sciences |
| spelling | doaj.art-df67978a61b542dc817a47560d498e652022-12-21T23:56:13ZengWorld Scientific PublishingJournal of Innovative Optical Health Sciences1793-54581793-72052019-01-011211841001-11841001-710.1142/S179354581841001810.1142/S1793545818410018Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domainsXueping Li0Weili Zhai1Zilong Guo2Hu Chen3Research Institute for Biomimetics and Soft Matter, Fujian Provincial Key Lab for Soft Functional Materials Research, Department of Physics, Xiamen University, Xiamen, ChinaResearch Institute for Biomimetics and Soft Matter, Fujian Provincial Key Lab for Soft Functional Materials Research, Department of Physics, Xiamen University, Xiamen, ChinaResearch Institute for Biomimetics and Soft Matter, Fujian Provincial Key Lab for Soft Functional Materials Research, Department of Physics, Xiamen University, Xiamen, ChinaResearch Institute for Biomimetics and Soft Matter, Fujian Provincial Key Lab for Soft Functional Materials Research, Department of Physics, Xiamen University, Xiamen, Chinaα-catenin is an adhesion protein located at the cadherin-based cell–cell adherens junction. α-catenin cross-links β-catenin and actin fiber in the adhesion protein complex, and plays an important role in the formation and modulation of cell–cell adhesion. The central modulation domains can be unfolded to expose binding site of vinculin when stretching force is applied. Here, we studied the force-induced unfolding dynamics of α-catenin modulation domains under different loading rates from which the unfolding distance of M2 and M3 domains is determined to be 5–7nm, and an unfolding intermediate state is identified. We also found that the folding process of M1–M3 domains goes through different pathways with cooperativity.http://www.worldscientific.com/doi/pdf/10.1142/S1793545818410018α-cateninfolding and unfoldingmagnetic tweezerBell’s model |
| spellingShingle | Xueping Li Weili Zhai Zilong Guo Hu Chen Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains Journal of Innovative Optical Health Sciences α-catenin folding and unfolding magnetic tweezer Bell’s model |
| title | Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains |
| title_full | Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains |
| title_fullStr | Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains |
| title_full_unstemmed | Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains |
| title_short | Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains |
| title_sort | force dependent unfolding and folding dynamics of protein alpha catenin modulation domains |
| topic | α-catenin folding and unfolding magnetic tweezer Bell’s model |
| url | http://www.worldscientific.com/doi/pdf/10.1142/S1793545818410018 |
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