The ER-PM interaction is essential for cytokinesis and recruits the actin cytoskeleton through the SCAR/WAVE complex
Xu, Z; Zang, X; Zheng, Q; et al.Li, Y; Field, N; Fiserova, J; Hua, B; Kriechbaumer, V; Deeks, MJ; Hussey, PJ; Wang, P
Date: 6 February 2025
Article
Journal
Proceedings of the National Academy of Sciences (PNAS)
Publisher
National Academy of Sciences
Publisher DOI
Abstract
Plant cytokinesis requires coordination between the actin cytoskeleton, microtubules and membranes to guide division plane formation and cell plate expansion; how these regulatory factors are coordinated remains unknown. The actin cytoskeleton assembly is controlled by several actin nucleation factors, such as the SCAR/WAVE complex, ...
Plant cytokinesis requires coordination between the actin cytoskeleton, microtubules and membranes to guide division plane formation and cell plate expansion; how these regulatory factors are coordinated remains unknown. The actin cytoskeleton assembly is controlled by several actin nucleation factors, such as the SCAR/WAVE complex, which regulates actin nucleation and branching through the activation of the ARP2/3 complex. The activity of these actin regulatory proteins is likely influenced by interactions with specific membranes; however, the molecular basis and the biological relevance of SCAR-membrane interactions are also unclear. In this study, we demonstrate that the ER-PM tethering protein VAP27-1 directly interacts with SCAR2 at the ER membrane, and that they co-localise to guide cell plate orientation during cell division. In the root meristem, both VAP27-1 and SCAR2 exhibit polarised localisation at the cell plates, where the interaction between ER and PM is abundant. VAP27-1 recruits SCAR2 to the cell division plane, where there is a high concentration of actin filaments. In the vap27-1346 mutant, the densities of cortical ER, SCAR2 and consequently actin filaments are significantly reduced at the cell division plane, affecting cell plate orientation, cell division and root development. A similar phenomenon is also observed in the scar1234 mutant, suggesting that VAP27 and SCAR proteins regulate cell division through a similar pathway. In conclusion, our data reveal a plant-specific function of VAP27-regulated ER-PM interaction and advance our understanding of plant ER-PM contact site and its role in cell division.
Biosciences
Faculty of Health and Life Sciences
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