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  Polychaetoid/ZO-1 strengthens cell junctions under tension while localizing differently than core adherens junction proteins

Peifer, M., Schmidt, A., Finegan, T., Häring, M., Kong, D., Fletcher, A. G., et al. (2023). Polychaetoid/ZO-1 strengthens cell junctions under tension while localizing differently than core adherens junction proteins. Molecular Biology of the Cell, 34(8): ar81. doi:10.1091/mbc.E23-03-0077.

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 Creators:
Peifer, Mark, Author
Schmidt, Anja, Author
Finegan, Tara, Author
Häring, Matthias1, Author           
Kong, Deqing, Author
Fletcher, Alexander G., Author
Alam, Zuhayr, Author
Grosshans, Jörg, Author
Wolf, Fred1, Author           
Yap, Alpha, Editor
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1Research Group Theoretical Neurophysics, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society, ou_2063289              

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 Abstract: During embryonic development, dramatic cell shape changes and movements reshape the embryonic body plan. These require robust but dynamic linkage between the cell–cell adherens junctions and the force-generating actomyosin cytoskeleton. Our view of this linkage has evolved, and we now realize linkage is mediated by mechanosensitive multiprotein complexes assembled via multivalent connections. Here we combine genetic, cell biological, and modeling approaches to define the mechanism of action and functions of an important player, Drosophila polychaetoid, homologue of mammalian ZO-1. Our data reveal that Pyd reinforces cell junctions under elevated tension, and facilitates cell rearrangements. Pyd is important to maintain junctional contractility and in its absence cell rearrangements stall. We next use structured illumination microscopy to define the molecular architecture of cell–cell junctions during these events. The cadherin–catenin complex and Cno both localize to puncta along the junctional membrane, but are differentially enriched in different puncta. Pyd, in contrast, exhibits a distinct localization to strands that extend out from the region occupied by core junction proteins. We then discuss the implications for the protein network at the junction–cytoskeletal interface, suggesting different proteins localize and function in distinct ways, perhaps in distinct subcomplexes, but combine to produce robust connections.

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Language(s): eng - English
 Dates: 2023-06-202023-07-01
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1091/mbc.E23-03-0077
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Project name : This work was supported by National Institutes of Health Grant no. R35 GM-118096 to M.P. A.S. was supported by DFG (Deutsche Forschungsgemeinschaft) SCHM 3628/1-1. Work in the Grosshans lab is supported by DFG GR1945/15-1, DFG INST1525/16-1 FUGG, and Volkswagenstiftung (A129197, ZN2632) and work in the Wolf lab by DFG FOR1756, GR1945/8-2, GR1945/10-1/2, WO1489/1-2, WO1489/5-1, and SFB 1286/C2, the Volkswagenstiftung (A129197, ZN2632), and the Cluster of Excellence Multiscale Bioimaging (MBExC)
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Title: Molecular Biology of the Cell
  Other : Mol. Biol. Cell
Source Genre: Journal
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Publ. Info: American Society for Cell Biology
Pages: - Volume / Issue: 34 (8) Sequence Number: ar81 Start / End Page: - Identifier: ISSN: 1059-1524
CoNE: https://pure.mpg.de/cone/journals/resource/954927716372_1