Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1
Abstract De novo lumen formation necessitates the precise segregation of junctional proteins from apical surfaces, yet the underlying mechanisms remain unclear. Using a zebrafish model, we develop a series of molecular reporters, photo-convertible and optogenetic tools to study the establishment of...
Saved in:
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2024-11-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-54143-y |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1846171847737999360 |
|---|---|
| author | Jianmin Yin Niels Schellinx Ludovico Maggi Kathrin Gundel Cora Wiesner Maria Paraskevi Kotini Minkyoung Lee Li-Kun Phng Heinz-Georg Belting Markus Affolter |
| author_facet | Jianmin Yin Niels Schellinx Ludovico Maggi Kathrin Gundel Cora Wiesner Maria Paraskevi Kotini Minkyoung Lee Li-Kun Phng Heinz-Georg Belting Markus Affolter |
| author_sort | Jianmin Yin |
| collection | DOAJ |
| description | Abstract De novo lumen formation necessitates the precise segregation of junctional proteins from apical surfaces, yet the underlying mechanisms remain unclear. Using a zebrafish model, we develop a series of molecular reporters, photo-convertible and optogenetic tools to study the establishment of apical domains. Our study identifies Rasip1 as one of the earliest apical proteins recruited, which suppresses actomyosin contractility at junctional patches by inhibiting NMII, thereby allowing for the sustained outward flow of junctional complexes. Following the establishment of apical compartments, Rasip1 shuttles between junctions and the apical compartments in response to local high tension. Rasip1 confines Cdh5 to junctions by suppressing apical contractility. Conversely, the recruitment of Rasip1 to junctions is regulated by Heg1 and Krit1 to modulate contractility along junctions. Overall, de novo lumen formation and maintenance depend on the precise control of contractility within apical compartments and junctions, orchestrated by the dynamic recruitment of Rasip1. |
| format | Article |
| id | doaj-art-cac7d75bd81e4deaae5f1a4918d65a3d |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2024-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-cac7d75bd81e4deaae5f1a4918d65a3d2024-11-10T12:32:56ZengNature PortfolioNature Communications2041-17232024-11-0115111810.1038/s41467-024-54143-yInitiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1Jianmin Yin0Niels Schellinx1Ludovico Maggi2Kathrin Gundel3Cora Wiesner4Maria Paraskevi Kotini5Minkyoung Lee6Li-Kun Phng7Heinz-Georg Belting8Markus Affolter9Department of Cell Biology, Biozentrum, University of BaselDepartment of Cell Biology, Biozentrum, University of BaselDepartment of Cell Biology, Biozentrum, University of BaselDepartment of Cell Biology, Biozentrum, University of BaselDepartment of Cell Biology, Biozentrum, University of BaselDepartment of Cell Biology, Biozentrum, University of BaselDepartment of Cell Biology, Biozentrum, University of BaselLaboratory for Vascular Morphogenesis, RIKEN Center for Biosystems Dynamics ResearchDepartment of Cell Biology, Biozentrum, University of BaselDepartment of Cell Biology, Biozentrum, University of BaselAbstract De novo lumen formation necessitates the precise segregation of junctional proteins from apical surfaces, yet the underlying mechanisms remain unclear. Using a zebrafish model, we develop a series of molecular reporters, photo-convertible and optogenetic tools to study the establishment of apical domains. Our study identifies Rasip1 as one of the earliest apical proteins recruited, which suppresses actomyosin contractility at junctional patches by inhibiting NMII, thereby allowing for the sustained outward flow of junctional complexes. Following the establishment of apical compartments, Rasip1 shuttles between junctions and the apical compartments in response to local high tension. Rasip1 confines Cdh5 to junctions by suppressing apical contractility. Conversely, the recruitment of Rasip1 to junctions is regulated by Heg1 and Krit1 to modulate contractility along junctions. Overall, de novo lumen formation and maintenance depend on the precise control of contractility within apical compartments and junctions, orchestrated by the dynamic recruitment of Rasip1.https://doi.org/10.1038/s41467-024-54143-y |
| spellingShingle | Jianmin Yin Niels Schellinx Ludovico Maggi Kathrin Gundel Cora Wiesner Maria Paraskevi Kotini Minkyoung Lee Li-Kun Phng Heinz-Georg Belting Markus Affolter Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1 Nature Communications |
| title | Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1 |
| title_full | Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1 |
| title_fullStr | Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1 |
| title_full_unstemmed | Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1 |
| title_short | Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1 |
| title_sort | initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of rasip1 |
| url | https://doi.org/10.1038/s41467-024-54143-y |
| work_keys_str_mv | AT jianminyin initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT nielsschellinx initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT ludovicomaggi initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT kathringundel initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT corawiesner initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT mariaparaskevikotini initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT minkyounglee initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT likunphng initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT heinzgeorgbelting initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 AT markusaffolter initiationoflumenformationfromjunctionsviadifferentialactomyosincontractilityregulatedbydynamicrecruitmentofrasip1 |