Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci

Inês Catarina Ramos Barbosa (), Damien De Bellis, Isabelle Flückiger, Etienne Bellani, Mathieu Grangé-Guerment, Kian Hématy and Niko Geldner ()
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Inês Catarina Ramos Barbosa: University of Lausanne
Damien De Bellis: University of Lausanne
Isabelle Flückiger: University of Lausanne
Etienne Bellani: University of Lausanne
Mathieu Grangé-Guerment: University of Lausanne
Kian Hématy: University of Lausanne
Niko Geldner: University of Lausanne

Nature Communications, 2023, vol. 14, issue 1, 1-18

Abstract: Abstract Casparian strips (CS) are aligned bands of lignin-impregnated cell walls, building an extracellular diffusion barrier in roots. Their structure profoundly differs from tight junctions (TJ), analogous structures in animals. Nonetheless, CS membrane domain (CSD) proteins 1-5 (CASP1-5) are homologues of occludins, TJ components. CASP-marked membranes display cell wall (matrix) adhesion and membrane protein exclusion. A full CASP knock-out now reveals CASPs are not needed for localized lignification, since correctly positioned lignin microdomains still form in the mutant. Ultra-structurally, however, these microdomains are disorganized, showing excessive cell wall growth, lack of exclusion zone and matrix adhesion, and impaired exocyst dynamics. Proximity-labelling identifies a Rab-GTPase subfamily, known exocyst activators, as potential CASP-interactors and demonstrate their localization and function at the CSD. We propose that CASP microdomains displace initial secretory foci by excluding vesicle tethering factors, thereby ensuring rapid fusion of microdomains into a membrane-cell wall band that seals the extracellular space.

Date: 2023
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DOI: 10.1038/s41467-023-37265-7

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