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Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1

Author

Listed:
  • Jianmin Yin

    (University of Basel)

  • Niels Schellinx

    (University of Basel)

  • Ludovico Maggi

    (University of Basel)

  • Kathrin Gundel

    (University of Basel
    Universitätsklinikum Bonn)

  • Cora Wiesner

    (University of Basel)

  • Maria Paraskevi Kotini

    (University of Basel)

  • Minkyoung Lee

    (University of Basel
    ETH Zürich)

  • Li-Kun Phng

    (RIKEN Center for Biosystems Dynamics Research)

  • Heinz-Georg Belting

    (University of Basel)

  • Markus Affolter

    (University of Basel)

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.

Suggested Citation

  • Jianmin Yin & Niels Schellinx & Ludovico Maggi & Kathrin Gundel & Cora Wiesner & Maria Paraskevi Kotini & Minkyoung Lee & Li-Kun Phng & Heinz-Georg Belting & Markus Affolter, 2024. "Initiation of lumen formation from junctions via differential actomyosin contractility regulated by dynamic recruitment of Rasip1," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54143-y
    DOI: 10.1038/s41467-024-54143-y
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    References listed on IDEAS

    as
    1. Ilkka Paatero & Loïc Sauteur & Minkyoung Lee & Anne K. Lagendijk & Daniel Heutschi & Cora Wiesner & Camilo Guzmán & Dimitri Bieli & Benjamin M. Hogan & Markus Affolter & Heinz-Georg Belting, 2018. "Junction-based lamellipodia drive endothelial cell rearrangements in vivo via a VE-cadherin-F-actin based oscillatory cell-cell interaction," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    2. Anne Karine Lagendijk & Guillermo A. Gomez & Sungmin Baek & Daniel Hesselson & William E. Hughes & Scott Paterson & Daniel E. Conway & Heinz-Georg Belting & Markus Affolter & Kelly A. Smith & Martin A, 2017. "Live imaging molecular changes in junctional tension upon VE-cadherin in zebrafish," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
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