PUBLICATION
            Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1
- Authors
- Yin, J., Schellinx, N., Maggi, L., Gundel, K., Wiesner, C., Kotini, M.P., Lee, M., Phng, L.K., Belting, H.G., Affolter, M.
- ID
- ZDB-PUB-241114-13
- Date
- 2024
- Source
- Nature communications 15: 97149714 (Journal)
- Registered Authors
- Affolter, Markus, Belting, Heinz-Georg Paul (Henry), Phng, Li-Kun
- Keywords
- none
- MeSH Terms
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                - Zebrafish Proteins*/genetics
- Zebrafish Proteins*/metabolism
- Zebrafish*
- Animals
- Cadherins/genetics
- Cadherins/metabolism
- Tight Junctions/metabolism
- Intercellular Junctions/metabolism
- Actomyosin*/metabolism
 
- PubMed
- 39521779 Full text @ Nat. Commun.
            Citation
        
        
            Yin, J., Schellinx, N., Maggi, L., Gundel, K., Wiesner, C., Kotini, M.P., Lee, M., Phng, L.K., Belting, H.G., Affolter, M. (2024) Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1. Nature communications. 15:97149714.
        
    
                
                    
                        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.
            
    
        
        
    
    
    
                
                    
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